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+anno_start	anno_end	anno_text	entity_type	sentence	section
+0	17	Crystal structure	evidence	Crystal structure of SEL1L: Insight into the roles of SLR motifs in ERAD pathway	TITLE
+21	26	SEL1L	protein	Crystal structure of SEL1L: Insight into the roles of SLR motifs in ERAD pathway	TITLE
+54	57	SLR	structure_element	Crystal structure of SEL1L: Insight into the roles of SLR motifs in ERAD pathway	TITLE
+0	5	SEL1L	protein	SEL1L, a component of the ERAD machinery, plays an important role in selecting and transporting ERAD substrates for degradation.	ABSTRACT
+23	40	crystal structure	evidence	We have determined the crystal structure of the mouse SEL1L central domain comprising five Sel1-Like Repeats (SLR motifs 5 to 9; hereafter called SEL1Lcent).	ABSTRACT
+48	53	mouse	taxonomy_domain	We have determined the crystal structure of the mouse SEL1L central domain comprising five Sel1-Like Repeats (SLR motifs 5 to 9; hereafter called SEL1Lcent).	ABSTRACT
+54	59	SEL1L	protein	We have determined the crystal structure of the mouse SEL1L central domain comprising five Sel1-Like Repeats (SLR motifs 5 to 9; hereafter called SEL1Lcent).	ABSTRACT
+60	74	central domain	structure_element	We have determined the crystal structure of the mouse SEL1L central domain comprising five Sel1-Like Repeats (SLR motifs 5 to 9; hereafter called SEL1Lcent).	ABSTRACT
+91	108	Sel1-Like Repeats	structure_element	We have determined the crystal structure of the mouse SEL1L central domain comprising five Sel1-Like Repeats (SLR motifs 5 to 9; hereafter called SEL1Lcent).	ABSTRACT
+110	127	SLR motifs 5 to 9	structure_element	We have determined the crystal structure of the mouse SEL1L central domain comprising five Sel1-Like Repeats (SLR motifs 5 to 9; hereafter called SEL1Lcent).	ABSTRACT
+146	155	SEL1Lcent	structure_element	We have determined the crystal structure of the mouse SEL1L central domain comprising five Sel1-Like Repeats (SLR motifs 5 to 9; hereafter called SEL1Lcent).	ABSTRACT
+12	21	SEL1Lcent	structure_element	Strikingly, SEL1Lcent forms a homodimer with two-fold symmetry in a head-to-tail manner.	ABSTRACT
+30	39	homodimer	oligomeric_state	Strikingly, SEL1Lcent forms a homodimer with two-fold symmetry in a head-to-tail manner.	ABSTRACT
+68	80	head-to-tail	protein_state	Strikingly, SEL1Lcent forms a homodimer with two-fold symmetry in a head-to-tail manner.	ABSTRACT
+18	29	SLR motif 9	structure_element	Particularly, the SLR motif 9 plays an important role in dimer formation by adopting a domain-swapped structure and providing an extensive dimeric interface.	ABSTRACT
+57	62	dimer	oligomeric_state	Particularly, the SLR motif 9 plays an important role in dimer formation by adopting a domain-swapped structure and providing an extensive dimeric interface.	ABSTRACT
+87	101	domain-swapped	protein_state	Particularly, the SLR motif 9 plays an important role in dimer formation by adopting a domain-swapped structure and providing an extensive dimeric interface.	ABSTRACT
+139	156	dimeric interface	site	Particularly, the SLR motif 9 plays an important role in dimer formation by adopting a domain-swapped structure and providing an extensive dimeric interface.	ABSTRACT
+23	34	full-length	protein_state	We identified that the full-length SEL1L forms a self-oligomer through the SEL1Lcent domain in mammalian cells.	ABSTRACT
+35	40	SEL1L	protein	We identified that the full-length SEL1L forms a self-oligomer through the SEL1Lcent domain in mammalian cells.	ABSTRACT
+49	62	self-oligomer	oligomeric_state	We identified that the full-length SEL1L forms a self-oligomer through the SEL1Lcent domain in mammalian cells.	ABSTRACT
+75	84	SEL1Lcent	structure_element	We identified that the full-length SEL1L forms a self-oligomer through the SEL1Lcent domain in mammalian cells.	ABSTRACT
+95	104	mammalian	taxonomy_domain	We identified that the full-length SEL1L forms a self-oligomer through the SEL1Lcent domain in mammalian cells.	ABSTRACT
+36	41	SLR-C	structure_element	Furthermore, we discovered that the SLR-C, comprising SLR motifs 10 and 11, of SEL1L directly interacts with the N-terminus luminal loops of HRD1.	ABSTRACT
+54	74	SLR motifs 10 and 11	structure_element	Furthermore, we discovered that the SLR-C, comprising SLR motifs 10 and 11, of SEL1L directly interacts with the N-terminus luminal loops of HRD1.	ABSTRACT
+79	84	SEL1L	protein	Furthermore, we discovered that the SLR-C, comprising SLR motifs 10 and 11, of SEL1L directly interacts with the N-terminus luminal loops of HRD1.	ABSTRACT
+124	137	luminal loops	structure_element	Furthermore, we discovered that the SLR-C, comprising SLR motifs 10 and 11, of SEL1L directly interacts with the N-terminus luminal loops of HRD1.	ABSTRACT
+141	145	HRD1	protein	Furthermore, we discovered that the SLR-C, comprising SLR motifs 10 and 11, of SEL1L directly interacts with the N-terminus luminal loops of HRD1.	ABSTRACT
+35	38	SLR	structure_element	Therefore, we propose that certain SLR motifs of SEL1L play a unique role in membrane bound ERAD machinery.	ABSTRACT
+49	54	SEL1L	protein	Therefore, we propose that certain SLR motifs of SEL1L play a unique role in membrane bound ERAD machinery.	ABSTRACT
+114	124	eukaryotes	taxonomy_domain	Protein quality control in the endoplasmic reticulum (ER) is essential for maintenance of cellular homeostasis in eukaryotes and is implicated in many severe diseases.	INTRO
+105	122	polyubiquitinated	protein_state	Terminally misfolded proteins in the lumen or membrane of the ER are retrotranslocated into the cytosol, polyubiquitinated, and degraded by the proteasome.	INTRO
+144	154	proteasome	complex_assembly	Terminally misfolded proteins in the lumen or membrane of the ER are retrotranslocated into the cytosol, polyubiquitinated, and degraded by the proteasome.	INTRO
+70	79	conserved	protein_state	The process is called ER-associated protein degradation (ERAD) and is conserved in all eukaryotes.	INTRO
+87	97	eukaryotes	taxonomy_domain	The process is called ER-associated protein degradation (ERAD) and is conserved in all eukaryotes.	INTRO
+72	76	HRD1	protein	Accumulating studies have identified key components for ERAD, including HRD1, SEL1L (Hrd3p), Derlin-1, -2, -3 (Der1p), HERP-1, -2 (Usa1p), OS9 (Yos9), XTP-B, and Grp94, all of which are involved in the recognition and translocation of the ERAD substrates in yeast and metazoans.	INTRO
+78	83	SEL1L	protein	Accumulating studies have identified key components for ERAD, including HRD1, SEL1L (Hrd3p), Derlin-1, -2, -3 (Der1p), HERP-1, -2 (Usa1p), OS9 (Yos9), XTP-B, and Grp94, all of which are involved in the recognition and translocation of the ERAD substrates in yeast and metazoans.	INTRO
+85	90	Hrd3p	protein	Accumulating studies have identified key components for ERAD, including HRD1, SEL1L (Hrd3p), Derlin-1, -2, -3 (Der1p), HERP-1, -2 (Usa1p), OS9 (Yos9), XTP-B, and Grp94, all of which are involved in the recognition and translocation of the ERAD substrates in yeast and metazoans.	INTRO
+93	109	Derlin-1, -2, -3	protein	Accumulating studies have identified key components for ERAD, including HRD1, SEL1L (Hrd3p), Derlin-1, -2, -3 (Der1p), HERP-1, -2 (Usa1p), OS9 (Yos9), XTP-B, and Grp94, all of which are involved in the recognition and translocation of the ERAD substrates in yeast and metazoans.	INTRO
+111	116	Der1p	protein	Accumulating studies have identified key components for ERAD, including HRD1, SEL1L (Hrd3p), Derlin-1, -2, -3 (Der1p), HERP-1, -2 (Usa1p), OS9 (Yos9), XTP-B, and Grp94, all of which are involved in the recognition and translocation of the ERAD substrates in yeast and metazoans.	INTRO
+119	129	HERP-1, -2	protein	Accumulating studies have identified key components for ERAD, including HRD1, SEL1L (Hrd3p), Derlin-1, -2, -3 (Der1p), HERP-1, -2 (Usa1p), OS9 (Yos9), XTP-B, and Grp94, all of which are involved in the recognition and translocation of the ERAD substrates in yeast and metazoans.	INTRO
+131	136	Usa1p	protein	Accumulating studies have identified key components for ERAD, including HRD1, SEL1L (Hrd3p), Derlin-1, -2, -3 (Der1p), HERP-1, -2 (Usa1p), OS9 (Yos9), XTP-B, and Grp94, all of which are involved in the recognition and translocation of the ERAD substrates in yeast and metazoans.	INTRO
+139	142	OS9	protein	Accumulating studies have identified key components for ERAD, including HRD1, SEL1L (Hrd3p), Derlin-1, -2, -3 (Der1p), HERP-1, -2 (Usa1p), OS9 (Yos9), XTP-B, and Grp94, all of which are involved in the recognition and translocation of the ERAD substrates in yeast and metazoans.	INTRO
+144	148	Yos9	protein	Accumulating studies have identified key components for ERAD, including HRD1, SEL1L (Hrd3p), Derlin-1, -2, -3 (Der1p), HERP-1, -2 (Usa1p), OS9 (Yos9), XTP-B, and Grp94, all of which are involved in the recognition and translocation of the ERAD substrates in yeast and metazoans.	INTRO
+151	156	XTP-B	protein	Accumulating studies have identified key components for ERAD, including HRD1, SEL1L (Hrd3p), Derlin-1, -2, -3 (Der1p), HERP-1, -2 (Usa1p), OS9 (Yos9), XTP-B, and Grp94, all of which are involved in the recognition and translocation of the ERAD substrates in yeast and metazoans.	INTRO
+162	167	Grp94	protein	Accumulating studies have identified key components for ERAD, including HRD1, SEL1L (Hrd3p), Derlin-1, -2, -3 (Der1p), HERP-1, -2 (Usa1p), OS9 (Yos9), XTP-B, and Grp94, all of which are involved in the recognition and translocation of the ERAD substrates in yeast and metazoans.	INTRO
+258	263	yeast	taxonomy_domain	Accumulating studies have identified key components for ERAD, including HRD1, SEL1L (Hrd3p), Derlin-1, -2, -3 (Der1p), HERP-1, -2 (Usa1p), OS9 (Yos9), XTP-B, and Grp94, all of which are involved in the recognition and translocation of the ERAD substrates in yeast and metazoans.	INTRO
+268	277	metazoans	taxonomy_domain	Accumulating studies have identified key components for ERAD, including HRD1, SEL1L (Hrd3p), Derlin-1, -2, -3 (Der1p), HERP-1, -2 (Usa1p), OS9 (Yos9), XTP-B, and Grp94, all of which are involved in the recognition and translocation of the ERAD substrates in yeast and metazoans.	INTRO
+0	5	Yeast	taxonomy_domain	Yeast ERAD components, which have been extensively characterized through genetic and biochemical studies, are comparable with mammalian ERAD components, sharing similar molecular functions and structural composition.	INTRO
+73	104	genetic and biochemical studies	experimental_method	Yeast ERAD components, which have been extensively characterized through genetic and biochemical studies, are comparable with mammalian ERAD components, sharing similar molecular functions and structural composition.	INTRO
+126	135	mammalian	taxonomy_domain	Yeast ERAD components, which have been extensively characterized through genetic and biochemical studies, are comparable with mammalian ERAD components, sharing similar molecular functions and structural composition.	INTRO
+4	8	HRD1	protein	The HRD1 E3 ubiquitin ligase, which is embedded in the ER membrane, is involved in translocating ERAD substrates across the ER membrane and catalyzing substrate ubiquitination via its cytosolic RING finger domain.	INTRO
+9	28	E3 ubiquitin ligase	protein_type	The HRD1 E3 ubiquitin ligase, which is embedded in the ER membrane, is involved in translocating ERAD substrates across the ER membrane and catalyzing substrate ubiquitination via its cytosolic RING finger domain.	INTRO
+194	212	RING finger domain	structure_element	The HRD1 E3 ubiquitin ligase, which is embedded in the ER membrane, is involved in translocating ERAD substrates across the ER membrane and catalyzing substrate ubiquitination via its cytosolic RING finger domain.	INTRO
+0	5	SEL1L	protein	SEL1L, the mammalian homolog of Hrd3p, associates with HRD1, mediates HRD1 interactions with the ER luminal lectin OS9, and recognizes substrates to be degraded.	INTRO
+11	20	mammalian	taxonomy_domain	SEL1L, the mammalian homolog of Hrd3p, associates with HRD1, mediates HRD1 interactions with the ER luminal lectin OS9, and recognizes substrates to be degraded.	INTRO
+32	37	Hrd3p	protein	SEL1L, the mammalian homolog of Hrd3p, associates with HRD1, mediates HRD1 interactions with the ER luminal lectin OS9, and recognizes substrates to be degraded.	INTRO
+55	59	HRD1	protein	SEL1L, the mammalian homolog of Hrd3p, associates with HRD1, mediates HRD1 interactions with the ER luminal lectin OS9, and recognizes substrates to be degraded.	INTRO
+70	74	HRD1	protein	SEL1L, the mammalian homolog of Hrd3p, associates with HRD1, mediates HRD1 interactions with the ER luminal lectin OS9, and recognizes substrates to be degraded.	INTRO
+108	114	lectin	protein_type	SEL1L, the mammalian homolog of Hrd3p, associates with HRD1, mediates HRD1 interactions with the ER luminal lectin OS9, and recognizes substrates to be degraded.	INTRO
+115	118	OS9	protein	SEL1L, the mammalian homolog of Hrd3p, associates with HRD1, mediates HRD1 interactions with the ER luminal lectin OS9, and recognizes substrates to be degraded.	INTRO
+15	20	SEL1L	protein	In particular, SEL1L is crucial for translocation of Class I major histocompatibility complex (MHC) heavy chains (HCs).	INTRO
+53	93	Class I major histocompatibility complex	complex_assembly	In particular, SEL1L is crucial for translocation of Class I major histocompatibility complex (MHC) heavy chains (HCs).	INTRO
+95	98	MHC	complex_assembly	In particular, SEL1L is crucial for translocation of Class I major histocompatibility complex (MHC) heavy chains (HCs).	INTRO
+100	112	heavy chains	protein_type	In particular, SEL1L is crucial for translocation of Class I major histocompatibility complex (MHC) heavy chains (HCs).	INTRO
+114	117	HCs	protein_type	In particular, SEL1L is crucial for translocation of Class I major histocompatibility complex (MHC) heavy chains (HCs).	INTRO
+39	44	Sel1l	gene	Recent research based on the inducible Sel1l knockout mouse model highlights the physiological functions of SEL1L.	INTRO
+45	59	knockout mouse	experimental_method	Recent research based on the inducible Sel1l knockout mouse model highlights the physiological functions of SEL1L.	INTRO
+108	113	SEL1L	protein	Recent research based on the inducible Sel1l knockout mouse model highlights the physiological functions of SEL1L.	INTRO
+0	5	SEL1L	protein	SEL1L is required for ER homeostasis, which is essential for protein translation, pancreatic function, and cellular and organismal survival.	INTRO
+46	51	SEL1L	protein	However, despite the functional importance of SEL1L, the molecular structure of SEL1L has not been solved.	INTRO
+67	76	structure	evidence	However, despite the functional importance of SEL1L, the molecular structure of SEL1L has not been solved.	INTRO
+80	85	SEL1L	protein	However, despite the functional importance of SEL1L, the molecular structure of SEL1L has not been solved.	INTRO
+9	28	biochemical studies	experimental_method	Previous biochemical studies reveal that SEL1L is a type I transmembrane protein and has a large luminal domain comprising sets of repeated Sel1-like (SLR) motifs.	INTRO
+41	46	SEL1L	protein	Previous biochemical studies reveal that SEL1L is a type I transmembrane protein and has a large luminal domain comprising sets of repeated Sel1-like (SLR) motifs.	INTRO
+52	80	type I transmembrane protein	protein_type	Previous biochemical studies reveal that SEL1L is a type I transmembrane protein and has a large luminal domain comprising sets of repeated Sel1-like (SLR) motifs.	INTRO
+97	111	luminal domain	structure_element	Previous biochemical studies reveal that SEL1L is a type I transmembrane protein and has a large luminal domain comprising sets of repeated Sel1-like (SLR) motifs.	INTRO
+131	149	repeated Sel1-like	structure_element	Previous biochemical studies reveal that SEL1L is a type I transmembrane protein and has a large luminal domain comprising sets of repeated Sel1-like (SLR) motifs.	INTRO
+151	154	SLR	structure_element	Previous biochemical studies reveal that SEL1L is a type I transmembrane protein and has a large luminal domain comprising sets of repeated Sel1-like (SLR) motifs.	INTRO
+4	7	SLR	structure_element	The SLR motif is a structural motif that closely resembles the tetratricopeptide-repeat (TPR) motif, which is a protein-protein interaction module.	INTRO
+63	87	tetratricopeptide-repeat	structure_element	The SLR motif is a structural motif that closely resembles the tetratricopeptide-repeat (TPR) motif, which is a protein-protein interaction module.	INTRO
+89	92	TPR	structure_element	The SLR motif is a structural motif that closely resembles the tetratricopeptide-repeat (TPR) motif, which is a protein-protein interaction module.	INTRO
+36	50	luminal domain	structure_element	Although there is evidence that the luminal domain of SEL1L is involved in substrate recognition or in forming complexes with chaperones, it is not known how the unique structure of the repeated SLR motifs contributes to the molecular function of the HRD1-SEL1L E3 ligase complex and affects ERAD at the molecular level.	INTRO
+54	59	SEL1L	protein	Although there is evidence that the luminal domain of SEL1L is involved in substrate recognition or in forming complexes with chaperones, it is not known how the unique structure of the repeated SLR motifs contributes to the molecular function of the HRD1-SEL1L E3 ligase complex and affects ERAD at the molecular level.	INTRO
+126	136	chaperones	protein_type	Although there is evidence that the luminal domain of SEL1L is involved in substrate recognition or in forming complexes with chaperones, it is not known how the unique structure of the repeated SLR motifs contributes to the molecular function of the HRD1-SEL1L E3 ligase complex and affects ERAD at the molecular level.	INTRO
+195	198	SLR	structure_element	Although there is evidence that the luminal domain of SEL1L is involved in substrate recognition or in forming complexes with chaperones, it is not known how the unique structure of the repeated SLR motifs contributes to the molecular function of the HRD1-SEL1L E3 ligase complex and affects ERAD at the molecular level.	INTRO
+251	261	HRD1-SEL1L	complex_assembly	Although there is evidence that the luminal domain of SEL1L is involved in substrate recognition or in forming complexes with chaperones, it is not known how the unique structure of the repeated SLR motifs contributes to the molecular function of the HRD1-SEL1L E3 ligase complex and affects ERAD at the molecular level.	INTRO
+262	271	E3 ligase	protein_type	Although there is evidence that the luminal domain of SEL1L is involved in substrate recognition or in forming complexes with chaperones, it is not known how the unique structure of the repeated SLR motifs contributes to the molecular function of the HRD1-SEL1L E3 ligase complex and affects ERAD at the molecular level.	INTRO
+28	31	SLR	structure_element	Furthermore, while repeated SLR motifs are commonly found in tandem arrays, the SLR motifs in SEL1L are, according to the primary structure prediction of SEL1L, interspersed among other sequences in the luminal domain and form three SLR domain clusters.	INTRO
+80	83	SLR	structure_element	Furthermore, while repeated SLR motifs are commonly found in tandem arrays, the SLR motifs in SEL1L are, according to the primary structure prediction of SEL1L, interspersed among other sequences in the luminal domain and form three SLR domain clusters.	INTRO
+94	99	SEL1L	protein	Furthermore, while repeated SLR motifs are commonly found in tandem arrays, the SLR motifs in SEL1L are, according to the primary structure prediction of SEL1L, interspersed among other sequences in the luminal domain and form three SLR domain clusters.	INTRO
+154	159	SEL1L	protein	Furthermore, while repeated SLR motifs are commonly found in tandem arrays, the SLR motifs in SEL1L are, according to the primary structure prediction of SEL1L, interspersed among other sequences in the luminal domain and form three SLR domain clusters.	INTRO
+203	217	luminal domain	structure_element	Furthermore, while repeated SLR motifs are commonly found in tandem arrays, the SLR motifs in SEL1L are, according to the primary structure prediction of SEL1L, interspersed among other sequences in the luminal domain and form three SLR domain clusters.	INTRO
+233	236	SLR	structure_element	Furthermore, while repeated SLR motifs are commonly found in tandem arrays, the SLR motifs in SEL1L are, according to the primary structure prediction of SEL1L, interspersed among other sequences in the luminal domain and form three SLR domain clusters.	INTRO
+64	69	SEL1L	protein	Therefore, the way in which these unique structural features of SEL1L are related to its critical function in ERAD remains to be elucidated.	INTRO
+50	53	SLR	structure_element	To clearly understand the biochemical role of the SLR domains of SEL1L in ERAD, we determined the crystal structure of the central SLR domain of SEL1L.	INTRO
+65	70	SEL1L	protein	To clearly understand the biochemical role of the SLR domains of SEL1L in ERAD, we determined the crystal structure of the central SLR domain of SEL1L.	INTRO
+98	115	crystal structure	evidence	To clearly understand the biochemical role of the SLR domains of SEL1L in ERAD, we determined the crystal structure of the central SLR domain of SEL1L.	INTRO
+131	134	SLR	structure_element	To clearly understand the biochemical role of the SLR domains of SEL1L in ERAD, we determined the crystal structure of the central SLR domain of SEL1L.	INTRO
+145	150	SEL1L	protein	To clearly understand the biochemical role of the SLR domains of SEL1L in ERAD, we determined the crystal structure of the central SLR domain of SEL1L.	INTRO
+18	32	central domain	structure_element	We found that the central domain of SEL1L, comprising SLR motifs 5 through 9 (SEL1Lcent), forms a tight dimer with two-fold symmetry due to domain swapping of the SLR motif 9.	INTRO
+36	41	SEL1L	protein	We found that the central domain of SEL1L, comprising SLR motifs 5 through 9 (SEL1Lcent), forms a tight dimer with two-fold symmetry due to domain swapping of the SLR motif 9.	INTRO
+54	76	SLR motifs 5 through 9	structure_element	We found that the central domain of SEL1L, comprising SLR motifs 5 through 9 (SEL1Lcent), forms a tight dimer with two-fold symmetry due to domain swapping of the SLR motif 9.	INTRO
+78	87	SEL1Lcent	structure_element	We found that the central domain of SEL1L, comprising SLR motifs 5 through 9 (SEL1Lcent), forms a tight dimer with two-fold symmetry due to domain swapping of the SLR motif 9.	INTRO
+104	109	dimer	oligomeric_state	We found that the central domain of SEL1L, comprising SLR motifs 5 through 9 (SEL1Lcent), forms a tight dimer with two-fold symmetry due to domain swapping of the SLR motif 9.	INTRO
+163	174	SLR motif 9	structure_element	We found that the central domain of SEL1L, comprising SLR motifs 5 through 9 (SEL1Lcent), forms a tight dimer with two-fold symmetry due to domain swapping of the SLR motif 9.	INTRO
+19	24	SLR-C	structure_element	We also found that SLR-C, consisting of SLR motifs 10 and 11, directly interacts with the N-terminus luminal loop of HRD1.	INTRO
+40	60	SLR motifs 10 and 11	structure_element	We also found that SLR-C, consisting of SLR motifs 10 and 11, directly interacts with the N-terminus luminal loop of HRD1.	INTRO
+101	113	luminal loop	structure_element	We also found that SLR-C, consisting of SLR motifs 10 and 11, directly interacts with the N-terminus luminal loop of HRD1.	INTRO
+117	121	HRD1	protein	We also found that SLR-C, consisting of SLR motifs 10 and 11, directly interacts with the N-terminus luminal loop of HRD1.	INTRO
+60	63	SLR	structure_element	Based on these observations, we propose a model wherein the SLR domains of SEL1L contribute to the formation of stable oligomers of the ERAD translocation machinery, which is indispensable for ERAD.	INTRO
+75	80	SEL1L	protein	Based on these observations, we propose a model wherein the SLR domains of SEL1L contribute to the formation of stable oligomers of the ERAD translocation machinery, which is indispensable for ERAD.	INTRO
+112	118	stable	protein_state	Based on these observations, we propose a model wherein the SLR domains of SEL1L contribute to the formation of stable oligomers of the ERAD translocation machinery, which is indispensable for ERAD.	INTRO
+119	128	oligomers	oligomeric_state	Based on these observations, we propose a model wherein the SLR domains of SEL1L contribute to the formation of stable oligomers of the ERAD translocation machinery, which is indispensable for ERAD.	INTRO
+0	23	Structure Determination	experimental_method	Structure Determination of SEL1Lcent	RESULTS
+27	36	SEL1Lcent	structure_element	Structure Determination of SEL1Lcent	RESULTS
+4	16	Mus musculus	species	The Mus musculus SEL1L protein contains 790 amino acids and has 17% sequence identity to its yeast homolog, Hrd3p.	RESULTS
+17	22	SEL1L	protein	The Mus musculus SEL1L protein contains 790 amino acids and has 17% sequence identity to its yeast homolog, Hrd3p.	RESULTS
+93	98	yeast	taxonomy_domain	The Mus musculus SEL1L protein contains 790 amino acids and has 17% sequence identity to its yeast homolog, Hrd3p.	RESULTS
+108	113	Hrd3p	protein	The Mus musculus SEL1L protein contains 790 amino acids and has 17% sequence identity to its yeast homolog, Hrd3p.	RESULTS
+0	5	Mouse	taxonomy_domain	Mouse SEL1L contains a fibronectin type II domain at the N-terminus, followed by 11 SLR motifs and a single transmembrane domain at the C-terminus (Fig. 1A).	RESULTS
+6	11	SEL1L	protein	Mouse SEL1L contains a fibronectin type II domain at the N-terminus, followed by 11 SLR motifs and a single transmembrane domain at the C-terminus (Fig. 1A).	RESULTS
+23	49	fibronectin type II domain	structure_element	Mouse SEL1L contains a fibronectin type II domain at the N-terminus, followed by 11 SLR motifs and a single transmembrane domain at the C-terminus (Fig. 1A).	RESULTS
+84	87	SLR	structure_element	Mouse SEL1L contains a fibronectin type II domain at the N-terminus, followed by 11 SLR motifs and a single transmembrane domain at the C-terminus (Fig. 1A).	RESULTS
+108	128	transmembrane domain	structure_element	Mouse SEL1L contains a fibronectin type II domain at the N-terminus, followed by 11 SLR motifs and a single transmembrane domain at the C-terminus (Fig. 1A).	RESULTS
+7	10	SLR	structure_element	The 11 SLR motifs are located in the ER lumen and account for more than two thirds of the mass of full-length SEL1L.	RESULTS
+98	109	full-length	protein_state	The 11 SLR motifs are located in the ER lumen and account for more than two thirds of the mass of full-length SEL1L.	RESULTS
+110	115	SEL1L	protein	The 11 SLR motifs are located in the ER lumen and account for more than two thirds of the mass of full-length SEL1L.	RESULTS
+4	7	SLR	structure_element	The SLR motifs can be grouped into three regions due to the presence of linker sequences among the groups of SLR motifs: SLR-N (SLR motifs 1 to 4), SLR-M (SLR motifs 5 to 9), and SLR-C (SLR motifs 10 to 11) (Fig. 1A).	RESULTS
+72	88	linker sequences	structure_element	The SLR motifs can be grouped into three regions due to the presence of linker sequences among the groups of SLR motifs: SLR-N (SLR motifs 1 to 4), SLR-M (SLR motifs 5 to 9), and SLR-C (SLR motifs 10 to 11) (Fig. 1A).	RESULTS
+109	112	SLR	structure_element	The SLR motifs can be grouped into three regions due to the presence of linker sequences among the groups of SLR motifs: SLR-N (SLR motifs 1 to 4), SLR-M (SLR motifs 5 to 9), and SLR-C (SLR motifs 10 to 11) (Fig. 1A).	RESULTS
+121	126	SLR-N	structure_element	The SLR motifs can be grouped into three regions due to the presence of linker sequences among the groups of SLR motifs: SLR-N (SLR motifs 1 to 4), SLR-M (SLR motifs 5 to 9), and SLR-C (SLR motifs 10 to 11) (Fig. 1A).	RESULTS
+128	145	SLR motifs 1 to 4	structure_element	The SLR motifs can be grouped into three regions due to the presence of linker sequences among the groups of SLR motifs: SLR-N (SLR motifs 1 to 4), SLR-M (SLR motifs 5 to 9), and SLR-C (SLR motifs 10 to 11) (Fig. 1A).	RESULTS
+148	153	SLR-M	structure_element	The SLR motifs can be grouped into three regions due to the presence of linker sequences among the groups of SLR motifs: SLR-N (SLR motifs 1 to 4), SLR-M (SLR motifs 5 to 9), and SLR-C (SLR motifs 10 to 11) (Fig. 1A).	RESULTS
+155	172	SLR motifs 5 to 9	structure_element	The SLR motifs can be grouped into three regions due to the presence of linker sequences among the groups of SLR motifs: SLR-N (SLR motifs 1 to 4), SLR-M (SLR motifs 5 to 9), and SLR-C (SLR motifs 10 to 11) (Fig. 1A).	RESULTS
+179	184	SLR-C	structure_element	The SLR motifs can be grouped into three regions due to the presence of linker sequences among the groups of SLR motifs: SLR-N (SLR motifs 1 to 4), SLR-M (SLR motifs 5 to 9), and SLR-C (SLR motifs 10 to 11) (Fig. 1A).	RESULTS
+186	205	SLR motifs 10 to 11	structure_element	The SLR motifs can be grouped into three regions due to the presence of linker sequences among the groups of SLR motifs: SLR-N (SLR motifs 1 to 4), SLR-M (SLR motifs 5 to 9), and SLR-C (SLR motifs 10 to 11) (Fig. 1A).	RESULTS
+0	18	Sequence alignment	experimental_method	Sequence alignment of the SLR motifs revealed that there is a short linker sequence (residues 336–345) between SLR-N and SLR-M and a long linker sequence (residues 528–635) between SLR-M and SLR-C (Fig. 1A).	RESULTS
+26	29	SLR	structure_element	Sequence alignment of the SLR motifs revealed that there is a short linker sequence (residues 336–345) between SLR-N and SLR-M and a long linker sequence (residues 528–635) between SLR-M and SLR-C (Fig. 1A).	RESULTS
+68	83	linker sequence	structure_element	Sequence alignment of the SLR motifs revealed that there is a short linker sequence (residues 336–345) between SLR-N and SLR-M and a long linker sequence (residues 528–635) between SLR-M and SLR-C (Fig. 1A).	RESULTS
+94	101	336–345	residue_range	Sequence alignment of the SLR motifs revealed that there is a short linker sequence (residues 336–345) between SLR-N and SLR-M and a long linker sequence (residues 528–635) between SLR-M and SLR-C (Fig. 1A).	RESULTS
+111	116	SLR-N	structure_element	Sequence alignment of the SLR motifs revealed that there is a short linker sequence (residues 336–345) between SLR-N and SLR-M and a long linker sequence (residues 528–635) between SLR-M and SLR-C (Fig. 1A).	RESULTS
+121	126	SLR-M	structure_element	Sequence alignment of the SLR motifs revealed that there is a short linker sequence (residues 336–345) between SLR-N and SLR-M and a long linker sequence (residues 528–635) between SLR-M and SLR-C (Fig. 1A).	RESULTS
+138	153	linker sequence	structure_element	Sequence alignment of the SLR motifs revealed that there is a short linker sequence (residues 336–345) between SLR-N and SLR-M and a long linker sequence (residues 528–635) between SLR-M and SLR-C (Fig. 1A).	RESULTS
+164	171	528–635	residue_range	Sequence alignment of the SLR motifs revealed that there is a short linker sequence (residues 336–345) between SLR-N and SLR-M and a long linker sequence (residues 528–635) between SLR-M and SLR-C (Fig. 1A).	RESULTS
+181	186	SLR-M	structure_element	Sequence alignment of the SLR motifs revealed that there is a short linker sequence (residues 336–345) between SLR-N and SLR-M and a long linker sequence (residues 528–635) between SLR-M and SLR-C (Fig. 1A).	RESULTS
+191	196	SLR-C	structure_element	Sequence alignment of the SLR motifs revealed that there is a short linker sequence (residues 336–345) between SLR-N and SLR-M and a long linker sequence (residues 528–635) between SLR-M and SLR-C (Fig. 1A).	RESULTS
+30	41	full-length	protein_state	We first tried to prepare the full-length mouse SEL1L protein, excluding the transmembrane domain at the C-terminus (residues 735–755), by expression in bacteria.	RESULTS
+42	47	mouse	taxonomy_domain	We first tried to prepare the full-length mouse SEL1L protein, excluding the transmembrane domain at the C-terminus (residues 735–755), by expression in bacteria.	RESULTS
+48	53	SEL1L	protein	We first tried to prepare the full-length mouse SEL1L protein, excluding the transmembrane domain at the C-terminus (residues 735–755), by expression in bacteria.	RESULTS
+77	97	transmembrane domain	structure_element	We first tried to prepare the full-length mouse SEL1L protein, excluding the transmembrane domain at the C-terminus (residues 735–755), by expression in bacteria.	RESULTS
+126	133	735–755	residue_range	We first tried to prepare the full-length mouse SEL1L protein, excluding the transmembrane domain at the C-terminus (residues 735–755), by expression in bacteria.	RESULTS
+139	161	expression in bacteria	experimental_method	We first tried to prepare the full-length mouse SEL1L protein, excluding the transmembrane domain at the C-terminus (residues 735–755), by expression in bacteria.	RESULTS
+13	24	full-length	protein_state	However, the full-length SEL1L protein aggregated in solution and produced no soluble protein.	RESULTS
+25	30	SEL1L	protein	However, the full-length SEL1L protein aggregated in solution and produced no soluble protein.	RESULTS
+30	35	SEL1L	protein	To identify a soluble form of SEL1L, we generated serial truncation constructs of SEL1L based on the predicted SLR motifs and highly conserved regions across several different species.	RESULTS
+50	78	serial truncation constructs	experimental_method	To identify a soluble form of SEL1L, we generated serial truncation constructs of SEL1L based on the predicted SLR motifs and highly conserved regions across several different species.	RESULTS
+82	87	SEL1L	protein	To identify a soluble form of SEL1L, we generated serial truncation constructs of SEL1L based on the predicted SLR motifs and highly conserved regions across several different species.	RESULTS
+111	114	SLR	structure_element	To identify a soluble form of SEL1L, we generated serial truncation constructs of SEL1L based on the predicted SLR motifs and highly conserved regions across several different species.	RESULTS
+126	142	highly conserved	protein_state	To identify a soluble form of SEL1L, we generated serial truncation constructs of SEL1L based on the predicted SLR motifs and highly conserved regions across several different species.	RESULTS
+5	10	SLR-N	structure_element	Both SLR-N (residues 194–343) and SLR-C (residues 639–719) alone could be solubilized with an MBP tag at the N-terminus, but appeared to be polydisperse when analyzed by size-exclusion chromatography.	RESULTS
+21	28	194–343	residue_range	Both SLR-N (residues 194–343) and SLR-C (residues 639–719) alone could be solubilized with an MBP tag at the N-terminus, but appeared to be polydisperse when analyzed by size-exclusion chromatography.	RESULTS
+34	39	SLR-C	structure_element	Both SLR-N (residues 194–343) and SLR-C (residues 639–719) alone could be solubilized with an MBP tag at the N-terminus, but appeared to be polydisperse when analyzed by size-exclusion chromatography.	RESULTS
+50	57	639–719	residue_range	Both SLR-N (residues 194–343) and SLR-C (residues 639–719) alone could be solubilized with an MBP tag at the N-terminus, but appeared to be polydisperse when analyzed by size-exclusion chromatography.	RESULTS
+94	119	MBP tag at the N-terminus	experimental_method	Both SLR-N (residues 194–343) and SLR-C (residues 639–719) alone could be solubilized with an MBP tag at the N-terminus, but appeared to be polydisperse when analyzed by size-exclusion chromatography.	RESULTS
+170	199	size-exclusion chromatography	experimental_method	Both SLR-N (residues 194–343) and SLR-C (residues 639–719) alone could be solubilized with an MBP tag at the N-terminus, but appeared to be polydisperse when analyzed by size-exclusion chromatography.	RESULTS
+13	27	central region	structure_element	However, the central region of SEL1L, comprising residues 337–554, was soluble and homogenous in size, as determined by size-exclusion chromatography.	RESULTS
+31	36	SEL1L	protein	However, the central region of SEL1L, comprising residues 337–554, was soluble and homogenous in size, as determined by size-exclusion chromatography.	RESULTS
+58	65	337–554	residue_range	However, the central region of SEL1L, comprising residues 337–554, was soluble and homogenous in size, as determined by size-exclusion chromatography.	RESULTS
+120	149	size-exclusion chromatography	experimental_method	However, the central region of SEL1L, comprising residues 337–554, was soluble and homogenous in size, as determined by size-exclusion chromatography.	RESULTS
+44	58	central region	structure_element	To define compact domain boundaries for the central region of SEL1L, we digested the protein with trypsin and analyzed the proteolysis products by SDS-PAGE and N-terminal sequencing.	RESULTS
+62	67	SEL1L	protein	To define compact domain boundaries for the central region of SEL1L, we digested the protein with trypsin and analyzed the proteolysis products by SDS-PAGE and N-terminal sequencing.	RESULTS
+72	105	digested the protein with trypsin	experimental_method	To define compact domain boundaries for the central region of SEL1L, we digested the protein with trypsin and analyzed the proteolysis products by SDS-PAGE and N-terminal sequencing.	RESULTS
+147	155	SDS-PAGE	experimental_method	To define compact domain boundaries for the central region of SEL1L, we digested the protein with trypsin and analyzed the proteolysis products by SDS-PAGE and N-terminal sequencing.	RESULTS
+160	181	N-terminal sequencing	experimental_method	To define compact domain boundaries for the central region of SEL1L, we digested the protein with trypsin and analyzed the proteolysis products by SDS-PAGE and N-terminal sequencing.	RESULTS
+68	73	SEL1L	protein	The results of this preliminary biochemical analysis suggested that SEL1L residues 348–533 (SEL1Lcent) would be amenable to structural analysis (Fig. 1A).	RESULTS
+83	90	348–533	residue_range	The results of this preliminary biochemical analysis suggested that SEL1L residues 348–533 (SEL1Lcent) would be amenable to structural analysis (Fig. 1A).	RESULTS
+92	101	SEL1Lcent	structure_element	The results of this preliminary biochemical analysis suggested that SEL1L residues 348–533 (SEL1Lcent) would be amenable to structural analysis (Fig. 1A).	RESULTS
+124	143	structural analysis	experimental_method	The results of this preliminary biochemical analysis suggested that SEL1L residues 348–533 (SEL1Lcent) would be amenable to structural analysis (Fig. 1A).	RESULTS
+0	8	Crystals	evidence	Crystals of SEL1Lcent grew in space group P21 with four copies of SEL1Lcent (a total of 82 kDa) in the asymmetric unit.	RESULTS
+12	21	SEL1Lcent	structure_element	Crystals of SEL1Lcent grew in space group P21 with four copies of SEL1Lcent (a total of 82 kDa) in the asymmetric unit.	RESULTS
+66	75	SEL1Lcent	structure_element	Crystals of SEL1Lcent grew in space group P21 with four copies of SEL1Lcent (a total of 82 kDa) in the asymmetric unit.	RESULTS
+4	13	structure	evidence	The structure was determined by the single-wavelength anomalous diffraction (SAD) method using selenium as the anomalous scatterer (Table 1 and Methods).	RESULTS
+36	75	single-wavelength anomalous diffraction	experimental_method	The structure was determined by the single-wavelength anomalous diffraction (SAD) method using selenium as the anomalous scatterer (Table 1 and Methods).	RESULTS
+77	80	SAD	experimental_method	The structure was determined by the single-wavelength anomalous diffraction (SAD) method using selenium as the anomalous scatterer (Table 1 and Methods).	RESULTS
+95	103	selenium	chemical	The structure was determined by the single-wavelength anomalous diffraction (SAD) method using selenium as the anomalous scatterer (Table 1 and Methods).	RESULTS
+66	74	selenium	chemical	The assignment of residues during model building was aided by the selenium atom positions, and the structure was refined with native data to 2.6 Å resolution with Rwork/Rfree values of 20.7/27.7%.	RESULTS
+99	108	structure	evidence	The assignment of residues during model building was aided by the selenium atom positions, and the structure was refined with native data to 2.6 Å resolution with Rwork/Rfree values of 20.7/27.7%.	RESULTS
+163	174	Rwork/Rfree	evidence	The assignment of residues during model building was aided by the selenium atom positions, and the structure was refined with native data to 2.6 Å resolution with Rwork/Rfree values of 20.7/27.7%.	RESULTS
+8	17	Structure	evidence	Overall Structure of SEL1Lcent	RESULTS
+21	30	SEL1Lcent	structure_element	Overall Structure of SEL1Lcent	RESULTS
+4	9	mouse	taxonomy_domain	The mouse SEL1Lcent crystallized as a homodimer, and there were two homodimers in the crystal asymmetric unit (Fig. 1B,C, Supplementary Fig. 1).	RESULTS
+10	19	SEL1Lcent	structure_element	The mouse SEL1Lcent crystallized as a homodimer, and there were two homodimers in the crystal asymmetric unit (Fig. 1B,C, Supplementary Fig. 1).	RESULTS
+20	32	crystallized	experimental_method	The mouse SEL1Lcent crystallized as a homodimer, and there were two homodimers in the crystal asymmetric unit (Fig. 1B,C, Supplementary Fig. 1).	RESULTS
+38	47	homodimer	oligomeric_state	The mouse SEL1Lcent crystallized as a homodimer, and there were two homodimers in the crystal asymmetric unit (Fig. 1B,C, Supplementary Fig. 1).	RESULTS
+68	78	homodimers	oligomeric_state	The mouse SEL1Lcent crystallized as a homodimer, and there were two homodimers in the crystal asymmetric unit (Fig. 1B,C, Supplementary Fig. 1).	RESULTS
+8	17	SEL1Lcent	structure_element	The two SEL1Lcent molecules dimerize in a head-to-tail manner through a two-fold symmetry interface resulting in a cosmos-like shaped structure (Fig. 1B).	RESULTS
+28	36	dimerize	oligomeric_state	The two SEL1Lcent molecules dimerize in a head-to-tail manner through a two-fold symmetry interface resulting in a cosmos-like shaped structure (Fig. 1B).	RESULTS
+42	54	head-to-tail	protein_state	The two SEL1Lcent molecules dimerize in a head-to-tail manner through a two-fold symmetry interface resulting in a cosmos-like shaped structure (Fig. 1B).	RESULTS
+72	99	two-fold symmetry interface	site	The two SEL1Lcent molecules dimerize in a head-to-tail manner through a two-fold symmetry interface resulting in a cosmos-like shaped structure (Fig. 1B).	RESULTS
+134	143	structure	evidence	The two SEL1Lcent molecules dimerize in a head-to-tail manner through a two-fold symmetry interface resulting in a cosmos-like shaped structure (Fig. 1B).	RESULTS
+14	23	structure	evidence	The resulting structure resembles the yin-yang symbol with overall dimensions of 60 × 60 × 25 Å, where a SEL1Lcent monomer corresponds to half the symbol.	RESULTS
+105	114	SEL1Lcent	structure_element	The resulting structure resembles the yin-yang symbol with overall dimensions of 60 × 60 × 25 Å, where a SEL1Lcent monomer corresponds to half the symbol.	RESULTS
+115	122	monomer	oligomeric_state	The resulting structure resembles the yin-yang symbol with overall dimensions of 60 × 60 × 25 Å, where a SEL1Lcent monomer corresponds to half the symbol.	RESULTS
+4	9	dimer	oligomeric_state	The dimer formation buries a surface area of 1670 Å2 for each monomer, and no significant differences between the protomers were displayed (final root mean square deviation (RMSD) of 0.6 Å for all Cα atoms).	RESULTS
+62	69	monomer	oligomeric_state	The dimer formation buries a surface area of 1670 Å2 for each monomer, and no significant differences between the protomers were displayed (final root mean square deviation (RMSD) of 0.6 Å for all Cα atoms).	RESULTS
+114	123	protomers	oligomeric_state	The dimer formation buries a surface area of 1670 Å2 for each monomer, and no significant differences between the protomers were displayed (final root mean square deviation (RMSD) of 0.6 Å for all Cα atoms).	RESULTS
+146	172	root mean square deviation	evidence	The dimer formation buries a surface area of 1670 Å2 for each monomer, and no significant differences between the protomers were displayed (final root mean square deviation (RMSD) of 0.6 Å for all Cα atoms).	RESULTS
+174	178	RMSD	evidence	The dimer formation buries a surface area of 1670 Å2 for each monomer, and no significant differences between the protomers were displayed (final root mean square deviation (RMSD) of 0.6 Å for all Cα atoms).	RESULTS
+5	13	protomer	oligomeric_state	Each protomer is composed of ten α-helices, which form the five SLRs, resulting in an elongated curved structure, confirming the primary structure prediction (Fig. 1D).	RESULTS
+33	42	α-helices	structure_element	Each protomer is composed of ten α-helices, which form the five SLRs, resulting in an elongated curved structure, confirming the primary structure prediction (Fig. 1D).	RESULTS
+64	68	SLRs	structure_element	Each protomer is composed of ten α-helices, which form the five SLRs, resulting in an elongated curved structure, confirming the primary structure prediction (Fig. 1D).	RESULTS
+4	13	α-helices	structure_element	The α-helices subdivide the structure into five pairs (A and B) as shown in a number of TPRs and SLRs.	RESULTS
+28	37	structure	evidence	The α-helices subdivide the structure into five pairs (A and B) as shown in a number of TPRs and SLRs.	RESULTS
+55	56	A	structure_element	The α-helices subdivide the structure into five pairs (A and B) as shown in a number of TPRs and SLRs.	RESULTS
+61	62	B	structure_element	The α-helices subdivide the structure into five pairs (A and B) as shown in a number of TPRs and SLRs.	RESULTS
+88	92	TPRs	structure_element	The α-helices subdivide the structure into five pairs (A and B) as shown in a number of TPRs and SLRs.	RESULTS
+97	101	SLRs	structure_element	The α-helices subdivide the structure into five pairs (A and B) as shown in a number of TPRs and SLRs.	RESULTS
+0	15	Helices A and B	structure_element	Helices A and B are 14 and 13 residues long, respectively, and the two helices are connected by a short turn and loop (Fig. 1D).	RESULTS
+71	78	helices	structure_element	Helices A and B are 14 and 13 residues long, respectively, and the two helices are connected by a short turn and loop (Fig. 1D).	RESULTS
+104	108	turn	structure_element	Helices A and B are 14 and 13 residues long, respectively, and the two helices are connected by a short turn and loop (Fig. 1D).	RESULTS
+113	117	loop	structure_element	Helices A and B are 14 and 13 residues long, respectively, and the two helices are connected by a short turn and loop (Fig. 1D).	RESULTS
+22	26	loop	structure_element	In addition, a longer loop, consisting of approximately eight amino acids, is inserted between helix B of one SLR and helix A of the next SLR.	RESULTS
+95	102	helix B	structure_element	In addition, a longer loop, consisting of approximately eight amino acids, is inserted between helix B of one SLR and helix A of the next SLR.	RESULTS
+110	113	SLR	structure_element	In addition, a longer loop, consisting of approximately eight amino acids, is inserted between helix B of one SLR and helix A of the next SLR.	RESULTS
+118	125	helix A	structure_element	In addition, a longer loop, consisting of approximately eight amino acids, is inserted between helix B of one SLR and helix A of the next SLR.	RESULTS
+138	141	SLR	structure_element	In addition, a longer loop, consisting of approximately eight amino acids, is inserted between helix B of one SLR and helix A of the next SLR.	RESULTS
+41	45	SLRs	structure_element	This arrangement is a unique feature for SLRs among the major classes of repeats containing an α-solenoid.	RESULTS
+95	105	α-solenoid	structure_element	This arrangement is a unique feature for SLRs among the major classes of repeats containing an α-solenoid.	RESULTS
+34	44	α-solenoid	structure_element	Starting from its N-terminus, the α-solenoid of SEL1L extends across a semi-circle in a right-handed superhelix fashion along the rotation axis of the yin-yang circle.	RESULTS
+48	53	SEL1L	protein	Starting from its N-terminus, the α-solenoid of SEL1L extends across a semi-circle in a right-handed superhelix fashion along the rotation axis of the yin-yang circle.	RESULTS
+151	166	yin-yang circle	structure_element	Starting from its N-terminus, the α-solenoid of SEL1L extends across a semi-circle in a right-handed superhelix fashion along the rotation axis of the yin-yang circle.	RESULTS
+25	27	9B	structure_element	However, the last helix, 9B, at the C-terminus adopts a different conformation, lying parallel to the long axis of helix 9A instead of forming an antiparallel SLR.	RESULTS
+115	123	helix 9A	structure_element	However, the last helix, 9B, at the C-terminus adopts a different conformation, lying parallel to the long axis of helix 9A instead of forming an antiparallel SLR.	RESULTS
+159	162	SLR	structure_element	However, the last helix, 9B, at the C-terminus adopts a different conformation, lying parallel to the long axis of helix 9A instead of forming an antiparallel SLR.	RESULTS
+28	36	helix 9B	structure_element	This unique conformation of helix 9B most likely contributes to formation of the dimer structure of SEL1Lcent, as detailed below.	RESULTS
+81	86	dimer	oligomeric_state	This unique conformation of helix 9B most likely contributes to formation of the dimer structure of SEL1Lcent, as detailed below.	RESULTS
+100	109	SEL1Lcent	structure_element	This unique conformation of helix 9B most likely contributes to formation of the dimer structure of SEL1Lcent, as detailed below.	RESULTS
+31	34	SLR	structure_element	With the exception of the last SLR, the four α-helix pairs possess similar conformations, with RMSD values of 0.7 Å for all Cα atoms.	RESULTS
+45	52	α-helix	structure_element	With the exception of the last SLR, the four α-helix pairs possess similar conformations, with RMSD values of 0.7 Å for all Cα atoms.	RESULTS
+95	99	RMSD	evidence	With the exception of the last SLR, the four α-helix pairs possess similar conformations, with RMSD values of 0.7 Å for all Cα atoms.	RESULTS
+41	60	pairwise alignments	experimental_method	Although the sequence similarity for the pairwise alignments varies between 25% and 35%, all the residues present in the SLR motifs are conserved among the five pairs.	RESULTS
+121	124	SLR	structure_element	Although the sequence similarity for the pairwise alignments varies between 25% and 35%, all the residues present in the SLR motifs are conserved among the five pairs.	RESULTS
+136	145	conserved	protein_state	Although the sequence similarity for the pairwise alignments varies between 25% and 35%, all the residues present in the SLR motifs are conserved among the five pairs.	RESULTS
+4	7	SLR	structure_element	The SLR domain of SLR-M ends at residue 524, and C-terminal amino acids 525–533 of the protein are not visible in the electron density map, suggesting that this region is highly flexible.	RESULTS
+18	23	SLR-M	structure_element	The SLR domain of SLR-M ends at residue 524, and C-terminal amino acids 525–533 of the protein are not visible in the electron density map, suggesting that this region is highly flexible.	RESULTS
+40	43	524	residue_number	The SLR domain of SLR-M ends at residue 524, and C-terminal amino acids 525–533 of the protein are not visible in the electron density map, suggesting that this region is highly flexible.	RESULTS
+72	79	525–533	residue_range	The SLR domain of SLR-M ends at residue 524, and C-terminal amino acids 525–533 of the protein are not visible in the electron density map, suggesting that this region is highly flexible.	RESULTS
+118	138	electron density map	evidence	The SLR domain of SLR-M ends at residue 524, and C-terminal amino acids 525–533 of the protein are not visible in the electron density map, suggesting that this region is highly flexible.	RESULTS
+171	186	highly flexible	protein_state	The SLR domain of SLR-M ends at residue 524, and C-terminal amino acids 525–533 of the protein are not visible in the electron density map, suggesting that this region is highly flexible.	RESULTS
+31	36	dimer	oligomeric_state	Since no information regarding dimer formation by SEL1L through its SLR motifs is available, we tested whether the SEL1Lcent dimer shown in our crystal structure is a biological unit.	RESULTS
+50	55	SEL1L	protein	Since no information regarding dimer formation by SEL1L through its SLR motifs is available, we tested whether the SEL1Lcent dimer shown in our crystal structure is a biological unit.	RESULTS
+68	71	SLR	structure_element	Since no information regarding dimer formation by SEL1L through its SLR motifs is available, we tested whether the SEL1Lcent dimer shown in our crystal structure is a biological unit.	RESULTS
+115	124	SEL1Lcent	structure_element	Since no information regarding dimer formation by SEL1L through its SLR motifs is available, we tested whether the SEL1Lcent dimer shown in our crystal structure is a biological unit.	RESULTS
+125	130	dimer	oligomeric_state	Since no information regarding dimer formation by SEL1L through its SLR motifs is available, we tested whether the SEL1Lcent dimer shown in our crystal structure is a biological unit.	RESULTS
+144	161	crystal structure	evidence	Since no information regarding dimer formation by SEL1L through its SLR motifs is available, we tested whether the SEL1Lcent dimer shown in our crystal structure is a biological unit.	RESULTS
+10	22	cross-linked	experimental_method	First, we cross-linked SEL1Lcent or a longer construct of SEL1L (SEL1Llong, residues 337–554) using various concentrations of glutaraldehyde (GA) or dimethyl suberimidate (DMS) and analyzed the products by SDS-PAGE.	RESULTS
+23	32	SEL1Lcent	structure_element	First, we cross-linked SEL1Lcent or a longer construct of SEL1L (SEL1Llong, residues 337–554) using various concentrations of glutaraldehyde (GA) or dimethyl suberimidate (DMS) and analyzed the products by SDS-PAGE.	RESULTS
+58	63	SEL1L	protein	First, we cross-linked SEL1Lcent or a longer construct of SEL1L (SEL1Llong, residues 337–554) using various concentrations of glutaraldehyde (GA) or dimethyl suberimidate (DMS) and analyzed the products by SDS-PAGE.	RESULTS
+65	74	SEL1Llong	mutant	First, we cross-linked SEL1Lcent or a longer construct of SEL1L (SEL1Llong, residues 337–554) using various concentrations of glutaraldehyde (GA) or dimethyl suberimidate (DMS) and analyzed the products by SDS-PAGE.	RESULTS
+85	92	337–554	residue_range	First, we cross-linked SEL1Lcent or a longer construct of SEL1L (SEL1Llong, residues 337–554) using various concentrations of glutaraldehyde (GA) or dimethyl suberimidate (DMS) and analyzed the products by SDS-PAGE.	RESULTS
+126	140	glutaraldehyde	chemical	First, we cross-linked SEL1Lcent or a longer construct of SEL1L (SEL1Llong, residues 337–554) using various concentrations of glutaraldehyde (GA) or dimethyl suberimidate (DMS) and analyzed the products by SDS-PAGE.	RESULTS
+142	144	GA	chemical	First, we cross-linked SEL1Lcent or a longer construct of SEL1L (SEL1Llong, residues 337–554) using various concentrations of glutaraldehyde (GA) or dimethyl suberimidate (DMS) and analyzed the products by SDS-PAGE.	RESULTS
+149	170	dimethyl suberimidate	chemical	First, we cross-linked SEL1Lcent or a longer construct of SEL1L (SEL1Llong, residues 337–554) using various concentrations of glutaraldehyde (GA) or dimethyl suberimidate (DMS) and analyzed the products by SDS-PAGE.	RESULTS
+172	175	DMS	chemical	First, we cross-linked SEL1Lcent or a longer construct of SEL1L (SEL1Llong, residues 337–554) using various concentrations of glutaraldehyde (GA) or dimethyl suberimidate (DMS) and analyzed the products by SDS-PAGE.	RESULTS
+206	214	SDS-PAGE	experimental_method	First, we cross-linked SEL1Lcent or a longer construct of SEL1L (SEL1Llong, residues 337–554) using various concentrations of glutaraldehyde (GA) or dimethyl suberimidate (DMS) and analyzed the products by SDS-PAGE.	RESULTS
+35	40	dimer	oligomeric_state	We detected bands at the mass of a dimer for both SEL1Lcent and SEL1Llong when cross-linked with low concentrations of GA (0.005%) or DMS (0.3 mM) (Supplementary Fig. 2A,B).	RESULTS
+50	59	SEL1Lcent	structure_element	We detected bands at the mass of a dimer for both SEL1Lcent and SEL1Llong when cross-linked with low concentrations of GA (0.005%) or DMS (0.3 mM) (Supplementary Fig. 2A,B).	RESULTS
+64	73	SEL1Llong	mutant	We detected bands at the mass of a dimer for both SEL1Lcent and SEL1Llong when cross-linked with low concentrations of GA (0.005%) or DMS (0.3 mM) (Supplementary Fig. 2A,B).	RESULTS
+79	91	cross-linked	experimental_method	We detected bands at the mass of a dimer for both SEL1Lcent and SEL1Llong when cross-linked with low concentrations of GA (0.005%) or DMS (0.3 mM) (Supplementary Fig. 2A,B).	RESULTS
+119	121	GA	chemical	We detected bands at the mass of a dimer for both SEL1Lcent and SEL1Llong when cross-linked with low concentrations of GA (0.005%) or DMS (0.3 mM) (Supplementary Fig. 2A,B).	RESULTS
+134	137	DMS	chemical	We detected bands at the mass of a dimer for both SEL1Lcent and SEL1Llong when cross-linked with low concentrations of GA (0.005%) or DMS (0.3 mM) (Supplementary Fig. 2A,B).	RESULTS
+19	49	analytical ultracentrifugation	experimental_method	Next, we conducted analytical ultracentrifugation of SEL1Lcent.	RESULTS
+53	62	SEL1Lcent	structure_element	Next, we conducted analytical ultracentrifugation of SEL1Lcent.	RESULTS
+20	33	cross-linking	experimental_method	Consistent with the cross-linking data, analytical ultracentrifugation revealed that the molecular weight of SEL1Lcent corresponds to a dimer (Supplementary Fig. 2C).	RESULTS
+40	70	analytical ultracentrifugation	experimental_method	Consistent with the cross-linking data, analytical ultracentrifugation revealed that the molecular weight of SEL1Lcent corresponds to a dimer (Supplementary Fig. 2C).	RESULTS
+89	105	molecular weight	evidence	Consistent with the cross-linking data, analytical ultracentrifugation revealed that the molecular weight of SEL1Lcent corresponds to a dimer (Supplementary Fig. 2C).	RESULTS
+109	118	SEL1Lcent	structure_element	Consistent with the cross-linking data, analytical ultracentrifugation revealed that the molecular weight of SEL1Lcent corresponds to a dimer (Supplementary Fig. 2C).	RESULTS
+136	141	dimer	oligomeric_state	Consistent with the cross-linking data, analytical ultracentrifugation revealed that the molecular weight of SEL1Lcent corresponds to a dimer (Supplementary Fig. 2C).	RESULTS
+54	59	dimer	oligomeric_state	Taken together, these data indicate that some kind of dimer is formed in solution.	RESULTS
+0	15	Dimer Interface	site	Dimer Interface of SEL1Lcent	RESULTS
+19	28	SEL1Lcent	structure_element	Dimer Interface of SEL1Lcent	RESULTS
+38	67	SLR motif containing proteins	protein_type	In contrast to a previously described SLR motif containing proteins that exist as monomers in solution, SEL1Lcent forms an intimate two-fold homotypic dimer interface (Figs 1B and 2A).	RESULTS
+82	90	monomers	oligomeric_state	In contrast to a previously described SLR motif containing proteins that exist as monomers in solution, SEL1Lcent forms an intimate two-fold homotypic dimer interface (Figs 1B and 2A).	RESULTS
+104	113	SEL1Lcent	structure_element	In contrast to a previously described SLR motif containing proteins that exist as monomers in solution, SEL1Lcent forms an intimate two-fold homotypic dimer interface (Figs 1B and 2A).	RESULTS
+132	166	two-fold homotypic dimer interface	site	In contrast to a previously described SLR motif containing proteins that exist as monomers in solution, SEL1Lcent forms an intimate two-fold homotypic dimer interface (Figs 1B and 2A).	RESULTS
+4	19	concave surface	site	The concave surface of each SEL1L domain comprising helix 5A to 9A encircles its dimer counterpart in an interlocking clasp-like arrangement.	RESULTS
+28	33	SEL1L	protein	The concave surface of each SEL1L domain comprising helix 5A to 9A encircles its dimer counterpart in an interlocking clasp-like arrangement.	RESULTS
+52	66	helix 5A to 9A	structure_element	The concave surface of each SEL1L domain comprising helix 5A to 9A encircles its dimer counterpart in an interlocking clasp-like arrangement.	RESULTS
+81	86	dimer	oligomeric_state	The concave surface of each SEL1L domain comprising helix 5A to 9A encircles its dimer counterpart in an interlocking clasp-like arrangement.	RESULTS
+64	73	protomers	oligomeric_state	However, no interactions were seen between the two-fold-related protomers through the concave inner surfaces themselves.	RESULTS
+86	108	concave inner surfaces	site	However, no interactions were seen between the two-fold-related protomers through the concave inner surfaces themselves.	RESULTS
+32	43	SLR motif 9	structure_element	Rather, the unique structure of SLR motif 9, consisting of two parallel helices (9A and 9B), is located in the space generated by the concave surface and provides an extensive dimerization interface between the two-fold-related molecules (Fig. 2A).	RESULTS
+81	83	9A	structure_element	Rather, the unique structure of SLR motif 9, consisting of two parallel helices (9A and 9B), is located in the space generated by the concave surface and provides an extensive dimerization interface between the two-fold-related molecules (Fig. 2A).	RESULTS
+88	90	9B	structure_element	Rather, the unique structure of SLR motif 9, consisting of two parallel helices (9A and 9B), is located in the space generated by the concave surface and provides an extensive dimerization interface between the two-fold-related molecules (Fig. 2A).	RESULTS
+134	149	concave surface	site	Rather, the unique structure of SLR motif 9, consisting of two parallel helices (9A and 9B), is located in the space generated by the concave surface and provides an extensive dimerization interface between the two-fold-related molecules (Fig. 2A).	RESULTS
+176	198	dimerization interface	site	Rather, the unique structure of SLR motif 9, consisting of two parallel helices (9A and 9B), is located in the space generated by the concave surface and provides an extensive dimerization interface between the two-fold-related molecules (Fig. 2A).	RESULTS
+0	8	Helix 9B	structure_element	Helix 9B from one protomer inserts into the empty space surrounded by the concave region in the other monomer, forming a domain-swapped conformation.	RESULTS
+18	26	protomer	oligomeric_state	Helix 9B from one protomer inserts into the empty space surrounded by the concave region in the other monomer, forming a domain-swapped conformation.	RESULTS
+74	88	concave region	site	Helix 9B from one protomer inserts into the empty space surrounded by the concave region in the other monomer, forming a domain-swapped conformation.	RESULTS
+102	109	monomer	oligomeric_state	Helix 9B from one protomer inserts into the empty space surrounded by the concave region in the other monomer, forming a domain-swapped conformation.	RESULTS
+121	135	domain-swapped	protein_state	Helix 9B from one protomer inserts into the empty space surrounded by the concave region in the other monomer, forming a domain-swapped conformation.	RESULTS
+12	30	contact interfaces	site	Three major contact interfaces are involved in the interactions, and all interfaces are symmetrically related between the dimer subunits (Fig. 2A).	RESULTS
+73	83	interfaces	site	Three major contact interfaces are involved in the interactions, and all interfaces are symmetrically related between the dimer subunits (Fig. 2A).	RESULTS
+122	127	dimer	oligomeric_state	Three major contact interfaces are involved in the interactions, and all interfaces are symmetrically related between the dimer subunits (Fig. 2A).	RESULTS
+0	34	Structure-based sequence alignment	experimental_method	Structure-based sequence alignment of 135 SEL1L phylogenetic sequences using a ConSurf server revealed that the surface residues in the dimer interfaces were highly conserved among the SEL1L orthologs (Fig. 1E).	RESULTS
+42	47	SEL1L	protein	Structure-based sequence alignment of 135 SEL1L phylogenetic sequences using a ConSurf server revealed that the surface residues in the dimer interfaces were highly conserved among the SEL1L orthologs (Fig. 1E).	RESULTS
+79	93	ConSurf server	experimental_method	Structure-based sequence alignment of 135 SEL1L phylogenetic sequences using a ConSurf server revealed that the surface residues in the dimer interfaces were highly conserved among the SEL1L orthologs (Fig. 1E).	RESULTS
+136	152	dimer interfaces	site	Structure-based sequence alignment of 135 SEL1L phylogenetic sequences using a ConSurf server revealed that the surface residues in the dimer interfaces were highly conserved among the SEL1L orthologs (Fig. 1E).	RESULTS
+158	174	highly conserved	protein_state	Structure-based sequence alignment of 135 SEL1L phylogenetic sequences using a ConSurf server revealed that the surface residues in the dimer interfaces were highly conserved among the SEL1L orthologs (Fig. 1E).	RESULTS
+185	190	SEL1L	protein	Structure-based sequence alignment of 135 SEL1L phylogenetic sequences using a ConSurf server revealed that the surface residues in the dimer interfaces were highly conserved among the SEL1L orthologs (Fig. 1E).	RESULTS
+7	15	helix 9B	structure_element	First, helix 9B of each SEL1Lcent subunit interacts with residues lining the inner groove from the SLR α-helices (5B, 6B, 7B, and 8B) from its counterpart.	RESULTS
+24	33	SEL1Lcent	structure_element	First, helix 9B of each SEL1Lcent subunit interacts with residues lining the inner groove from the SLR α-helices (5B, 6B, 7B, and 8B) from its counterpart.	RESULTS
+77	89	inner groove	site	First, helix 9B of each SEL1Lcent subunit interacts with residues lining the inner groove from the SLR α-helices (5B, 6B, 7B, and 8B) from its counterpart.	RESULTS
+99	102	SLR	structure_element	First, helix 9B of each SEL1Lcent subunit interacts with residues lining the inner groove from the SLR α-helices (5B, 6B, 7B, and 8B) from its counterpart.	RESULTS
+103	112	α-helices	structure_element	First, helix 9B of each SEL1Lcent subunit interacts with residues lining the inner groove from the SLR α-helices (5B, 6B, 7B, and 8B) from its counterpart.	RESULTS
+114	116	5B	structure_element	First, helix 9B of each SEL1Lcent subunit interacts with residues lining the inner groove from the SLR α-helices (5B, 6B, 7B, and 8B) from its counterpart.	RESULTS
+118	120	6B	structure_element	First, helix 9B of each SEL1Lcent subunit interacts with residues lining the inner groove from the SLR α-helices (5B, 6B, 7B, and 8B) from its counterpart.	RESULTS
+122	124	7B	structure_element	First, helix 9B of each SEL1Lcent subunit interacts with residues lining the inner groove from the SLR α-helices (5B, 6B, 7B, and 8B) from its counterpart.	RESULTS
+130	132	8B	structure_element	First, helix 9B of each SEL1Lcent subunit interacts with residues lining the inner groove from the SLR α-helices (5B, 6B, 7B, and 8B) from its counterpart.	RESULTS
+8	17	interface	site	In this interface, Leu 516 and Tyr 519 on helix 9B are located in the center, making hydrophobic interactions with Trp 478 on helix 8B, Val 444 on helix 7B, Phe 411 on helix 6B, and Leu 380 on helix 5B from the SEL1Lcent counterpart (Fig. 2A, Interface 1 detail).	RESULTS
+19	26	Leu 516	residue_name_number	In this interface, Leu 516 and Tyr 519 on helix 9B are located in the center, making hydrophobic interactions with Trp 478 on helix 8B, Val 444 on helix 7B, Phe 411 on helix 6B, and Leu 380 on helix 5B from the SEL1Lcent counterpart (Fig. 2A, Interface 1 detail).	RESULTS
+31	38	Tyr 519	residue_name_number	In this interface, Leu 516 and Tyr 519 on helix 9B are located in the center, making hydrophobic interactions with Trp 478 on helix 8B, Val 444 on helix 7B, Phe 411 on helix 6B, and Leu 380 on helix 5B from the SEL1Lcent counterpart (Fig. 2A, Interface 1 detail).	RESULTS
+42	50	helix 9B	structure_element	In this interface, Leu 516 and Tyr 519 on helix 9B are located in the center, making hydrophobic interactions with Trp 478 on helix 8B, Val 444 on helix 7B, Phe 411 on helix 6B, and Leu 380 on helix 5B from the SEL1Lcent counterpart (Fig. 2A, Interface 1 detail).	RESULTS
+85	109	hydrophobic interactions	bond_interaction	In this interface, Leu 516 and Tyr 519 on helix 9B are located in the center, making hydrophobic interactions with Trp 478 on helix 8B, Val 444 on helix 7B, Phe 411 on helix 6B, and Leu 380 on helix 5B from the SEL1Lcent counterpart (Fig. 2A, Interface 1 detail).	RESULTS
+115	122	Trp 478	residue_name_number	In this interface, Leu 516 and Tyr 519 on helix 9B are located in the center, making hydrophobic interactions with Trp 478 on helix 8B, Val 444 on helix 7B, Phe 411 on helix 6B, and Leu 380 on helix 5B from the SEL1Lcent counterpart (Fig. 2A, Interface 1 detail).	RESULTS
+126	134	helix 8B	structure_element	In this interface, Leu 516 and Tyr 519 on helix 9B are located in the center, making hydrophobic interactions with Trp 478 on helix 8B, Val 444 on helix 7B, Phe 411 on helix 6B, and Leu 380 on helix 5B from the SEL1Lcent counterpart (Fig. 2A, Interface 1 detail).	RESULTS
+136	143	Val 444	residue_name_number	In this interface, Leu 516 and Tyr 519 on helix 9B are located in the center, making hydrophobic interactions with Trp 478 on helix 8B, Val 444 on helix 7B, Phe 411 on helix 6B, and Leu 380 on helix 5B from the SEL1Lcent counterpart (Fig. 2A, Interface 1 detail).	RESULTS
+147	155	helix 7B	structure_element	In this interface, Leu 516 and Tyr 519 on helix 9B are located in the center, making hydrophobic interactions with Trp 478 on helix 8B, Val 444 on helix 7B, Phe 411 on helix 6B, and Leu 380 on helix 5B from the SEL1Lcent counterpart (Fig. 2A, Interface 1 detail).	RESULTS
+157	164	Phe 411	residue_name_number	In this interface, Leu 516 and Tyr 519 on helix 9B are located in the center, making hydrophobic interactions with Trp 478 on helix 8B, Val 444 on helix 7B, Phe 411 on helix 6B, and Leu 380 on helix 5B from the SEL1Lcent counterpart (Fig. 2A, Interface 1 detail).	RESULTS
+168	176	helix 6B	structure_element	In this interface, Leu 516 and Tyr 519 on helix 9B are located in the center, making hydrophobic interactions with Trp 478 on helix 8B, Val 444 on helix 7B, Phe 411 on helix 6B, and Leu 380 on helix 5B from the SEL1Lcent counterpart (Fig. 2A, Interface 1 detail).	RESULTS
+182	189	Leu 380	residue_name_number	In this interface, Leu 516 and Tyr 519 on helix 9B are located in the center, making hydrophobic interactions with Trp 478 on helix 8B, Val 444 on helix 7B, Phe 411 on helix 6B, and Leu 380 on helix 5B from the SEL1Lcent counterpart (Fig. 2A, Interface 1 detail).	RESULTS
+193	201	helix 5B	structure_element	In this interface, Leu 516 and Tyr 519 on helix 9B are located in the center, making hydrophobic interactions with Trp 478 on helix 8B, Val 444 on helix 7B, Phe 411 on helix 6B, and Leu 380 on helix 5B from the SEL1Lcent counterpart (Fig. 2A, Interface 1 detail).	RESULTS
+211	220	SEL1Lcent	structure_element	In this interface, Leu 516 and Tyr 519 on helix 9B are located in the center, making hydrophobic interactions with Trp 478 on helix 8B, Val 444 on helix 7B, Phe 411 on helix 6B, and Leu 380 on helix 5B from the SEL1Lcent counterpart (Fig. 2A, Interface 1 detail).	RESULTS
+243	254	Interface 1	site	In this interface, Leu 516 and Tyr 519 on helix 9B are located in the center, making hydrophobic interactions with Trp 478 on helix 8B, Val 444 on helix 7B, Phe 411 on helix 6B, and Leu 380 on helix 5B from the SEL1Lcent counterpart (Fig. 2A, Interface 1 detail).	RESULTS
+15	39	hydrophobic interactions	bond_interaction	In addition to hydrophobic interactions, the side chain hydroxyl group of Tyr 519 and the main-chain oxygen of Ile 515 form H-bonds to the side chain of the conserved Gln 377 and His 381 on helix 5B of the two-fold-related protomer.	RESULTS
+74	81	Tyr 519	residue_name_number	In addition to hydrophobic interactions, the side chain hydroxyl group of Tyr 519 and the main-chain oxygen of Ile 515 form H-bonds to the side chain of the conserved Gln 377 and His 381 on helix 5B of the two-fold-related protomer.	RESULTS
+111	118	Ile 515	residue_name_number	In addition to hydrophobic interactions, the side chain hydroxyl group of Tyr 519 and the main-chain oxygen of Ile 515 form H-bonds to the side chain of the conserved Gln 377 and His 381 on helix 5B of the two-fold-related protomer.	RESULTS
+124	131	H-bonds	bond_interaction	In addition to hydrophobic interactions, the side chain hydroxyl group of Tyr 519 and the main-chain oxygen of Ile 515 form H-bonds to the side chain of the conserved Gln 377 and His 381 on helix 5B of the two-fold-related protomer.	RESULTS
+157	166	conserved	protein_state	In addition to hydrophobic interactions, the side chain hydroxyl group of Tyr 519 and the main-chain oxygen of Ile 515 form H-bonds to the side chain of the conserved Gln 377 and His 381 on helix 5B of the two-fold-related protomer.	RESULTS
+167	174	Gln 377	residue_name_number	In addition to hydrophobic interactions, the side chain hydroxyl group of Tyr 519 and the main-chain oxygen of Ile 515 form H-bonds to the side chain of the conserved Gln 377 and His 381 on helix 5B of the two-fold-related protomer.	RESULTS
+179	186	His 381	residue_name_number	In addition to hydrophobic interactions, the side chain hydroxyl group of Tyr 519 and the main-chain oxygen of Ile 515 form H-bonds to the side chain of the conserved Gln 377 and His 381 on helix 5B of the two-fold-related protomer.	RESULTS
+190	198	helix 5B	structure_element	In addition to hydrophobic interactions, the side chain hydroxyl group of Tyr 519 and the main-chain oxygen of Ile 515 form H-bonds to the side chain of the conserved Gln 377 and His 381 on helix 5B of the two-fold-related protomer.	RESULTS
+223	231	protomer	oligomeric_state	In addition to hydrophobic interactions, the side chain hydroxyl group of Tyr 519 and the main-chain oxygen of Ile 515 form H-bonds to the side chain of the conserved Gln 377 and His 381 on helix 5B of the two-fold-related protomer.	RESULTS
+18	25	Gln 523	residue_name_number	The side chain of Gln 523 forms an H-bond to the side chain of Asp 480 on the two-fold-related protomer (Fig. 2A, Interface 1 detail).	RESULTS
+35	41	H-bond	bond_interaction	The side chain of Gln 523 forms an H-bond to the side chain of Asp 480 on the two-fold-related protomer (Fig. 2A, Interface 1 detail).	RESULTS
+63	70	Asp 480	residue_name_number	The side chain of Gln 523 forms an H-bond to the side chain of Asp 480 on the two-fold-related protomer (Fig. 2A, Interface 1 detail).	RESULTS
+95	103	protomer	oligomeric_state	The side chain of Gln 523 forms an H-bond to the side chain of Asp 480 on the two-fold-related protomer (Fig. 2A, Interface 1 detail).	RESULTS
+114	125	Interface 1	site	The side chain of Gln 523 forms an H-bond to the side chain of Asp 480 on the two-fold-related protomer (Fig. 2A, Interface 1 detail).	RESULTS
+26	34	helix 9A	structure_element	Second, the residues from helix 9A interact with the residues from helix 5A of its counterpart in a head-to-tail orientation.	RESULTS
+67	75	helix 5A	structure_element	Second, the residues from helix 9A interact with the residues from helix 5A of its counterpart in a head-to-tail orientation.	RESULTS
+100	112	head-to-tail	protein_state	Second, the residues from helix 9A interact with the residues from helix 5A of its counterpart in a head-to-tail orientation.	RESULTS
+8	17	interface	site	In this interface, the interacting residues on helix 9A, including Leu 503, Tyr 499, and the aliphatic side chain of Lys 500, form an extensive network of van der Waals contacts with the hydrophobic residues of the counterpart helix 5A, including Tyr 360, Leu 356, Tyr 359, and Leu 363.	RESULTS
+47	55	helix 9A	structure_element	In this interface, the interacting residues on helix 9A, including Leu 503, Tyr 499, and the aliphatic side chain of Lys 500, form an extensive network of van der Waals contacts with the hydrophobic residues of the counterpart helix 5A, including Tyr 360, Leu 356, Tyr 359, and Leu 363.	RESULTS
+67	74	Leu 503	residue_name_number	In this interface, the interacting residues on helix 9A, including Leu 503, Tyr 499, and the aliphatic side chain of Lys 500, form an extensive network of van der Waals contacts with the hydrophobic residues of the counterpart helix 5A, including Tyr 360, Leu 356, Tyr 359, and Leu 363.	RESULTS
+76	83	Tyr 499	residue_name_number	In this interface, the interacting residues on helix 9A, including Leu 503, Tyr 499, and the aliphatic side chain of Lys 500, form an extensive network of van der Waals contacts with the hydrophobic residues of the counterpart helix 5A, including Tyr 360, Leu 356, Tyr 359, and Leu 363.	RESULTS
+117	124	Lys 500	residue_name_number	In this interface, the interacting residues on helix 9A, including Leu 503, Tyr 499, and the aliphatic side chain of Lys 500, form an extensive network of van der Waals contacts with the hydrophobic residues of the counterpart helix 5A, including Tyr 360, Leu 356, Tyr 359, and Leu 363.	RESULTS
+155	177	van der Waals contacts	bond_interaction	In this interface, the interacting residues on helix 9A, including Leu 503, Tyr 499, and the aliphatic side chain of Lys 500, form an extensive network of van der Waals contacts with the hydrophobic residues of the counterpart helix 5A, including Tyr 360, Leu 356, Tyr 359, and Leu 363.	RESULTS
+227	235	helix 5A	structure_element	In this interface, the interacting residues on helix 9A, including Leu 503, Tyr 499, and the aliphatic side chain of Lys 500, form an extensive network of van der Waals contacts with the hydrophobic residues of the counterpart helix 5A, including Tyr 360, Leu 356, Tyr 359, and Leu 363.	RESULTS
+247	254	Tyr 360	residue_name_number	In this interface, the interacting residues on helix 9A, including Leu 503, Tyr 499, and the aliphatic side chain of Lys 500, form an extensive network of van der Waals contacts with the hydrophobic residues of the counterpart helix 5A, including Tyr 360, Leu 356, Tyr 359, and Leu 363.	RESULTS
+256	263	Leu 356	residue_name_number	In this interface, the interacting residues on helix 9A, including Leu 503, Tyr 499, and the aliphatic side chain of Lys 500, form an extensive network of van der Waals contacts with the hydrophobic residues of the counterpart helix 5A, including Tyr 360, Leu 356, Tyr 359, and Leu 363.	RESULTS
+265	272	Tyr 359	residue_name_number	In this interface, the interacting residues on helix 9A, including Leu 503, Tyr 499, and the aliphatic side chain of Lys 500, form an extensive network of van der Waals contacts with the hydrophobic residues of the counterpart helix 5A, including Tyr 360, Leu 356, Tyr 359, and Leu 363.	RESULTS
+278	285	Leu 363	residue_name_number	In this interface, the interacting residues on helix 9A, including Leu 503, Tyr 499, and the aliphatic side chain of Lys 500, form an extensive network of van der Waals contacts with the hydrophobic residues of the counterpart helix 5A, including Tyr 360, Leu 356, Tyr 359, and Leu 363.	RESULTS
+15	39	hydrophobic interactions	bond_interaction	In addition to hydrophobic interactions, the side chains of Asn 507 and Ser 510 on helix 9A make H-bonds with highly conserved Arg 384 in the loop between helix 5B and 6A from the two-fold-related protomer (Fig. 2A, Interface 2 detail).	RESULTS
+60	67	Asn 507	residue_name_number	In addition to hydrophobic interactions, the side chains of Asn 507 and Ser 510 on helix 9A make H-bonds with highly conserved Arg 384 in the loop between helix 5B and 6A from the two-fold-related protomer (Fig. 2A, Interface 2 detail).	RESULTS
+72	79	Ser 510	residue_name_number	In addition to hydrophobic interactions, the side chains of Asn 507 and Ser 510 on helix 9A make H-bonds with highly conserved Arg 384 in the loop between helix 5B and 6A from the two-fold-related protomer (Fig. 2A, Interface 2 detail).	RESULTS
+83	91	helix 9A	structure_element	In addition to hydrophobic interactions, the side chains of Asn 507 and Ser 510 on helix 9A make H-bonds with highly conserved Arg 384 in the loop between helix 5B and 6A from the two-fold-related protomer (Fig. 2A, Interface 2 detail).	RESULTS
+97	104	H-bonds	bond_interaction	In addition to hydrophobic interactions, the side chains of Asn 507 and Ser 510 on helix 9A make H-bonds with highly conserved Arg 384 in the loop between helix 5B and 6A from the two-fold-related protomer (Fig. 2A, Interface 2 detail).	RESULTS
+110	126	highly conserved	protein_state	In addition to hydrophobic interactions, the side chains of Asn 507 and Ser 510 on helix 9A make H-bonds with highly conserved Arg 384 in the loop between helix 5B and 6A from the two-fold-related protomer (Fig. 2A, Interface 2 detail).	RESULTS
+127	134	Arg 384	residue_name_number	In addition to hydrophobic interactions, the side chains of Asn 507 and Ser 510 on helix 9A make H-bonds with highly conserved Arg 384 in the loop between helix 5B and 6A from the two-fold-related protomer (Fig. 2A, Interface 2 detail).	RESULTS
+142	146	loop	structure_element	In addition to hydrophobic interactions, the side chains of Asn 507 and Ser 510 on helix 9A make H-bonds with highly conserved Arg 384 in the loop between helix 5B and 6A from the two-fold-related protomer (Fig. 2A, Interface 2 detail).	RESULTS
+155	163	helix 5B	structure_element	In addition to hydrophobic interactions, the side chains of Asn 507 and Ser 510 on helix 9A make H-bonds with highly conserved Arg 384 in the loop between helix 5B and 6A from the two-fold-related protomer (Fig. 2A, Interface 2 detail).	RESULTS
+168	170	6A	structure_element	In addition to hydrophobic interactions, the side chains of Asn 507 and Ser 510 on helix 9A make H-bonds with highly conserved Arg 384 in the loop between helix 5B and 6A from the two-fold-related protomer (Fig. 2A, Interface 2 detail).	RESULTS
+197	205	protomer	oligomeric_state	In addition to hydrophobic interactions, the side chains of Asn 507 and Ser 510 on helix 9A make H-bonds with highly conserved Arg 384 in the loop between helix 5B and 6A from the two-fold-related protomer (Fig. 2A, Interface 2 detail).	RESULTS
+11	19	helix 9B	structure_element	Third, the helix 9B from each protomer is involved in the dimer interaction by forming a two-fold antiparallel symmetry.	RESULTS
+30	38	protomer	oligomeric_state	Third, the helix 9B from each protomer is involved in the dimer interaction by forming a two-fold antiparallel symmetry.	RESULTS
+58	63	dimer	oligomeric_state	Third, the helix 9B from each protomer is involved in the dimer interaction by forming a two-fold antiparallel symmetry.	RESULTS
+66	73	Phe 518	residue_name_number	In particular, the side chains of hydrophobic residues, including Phe 518, Leu 521, and Met 524, are directed toward each other, where they make both inter- and intramolecular contacts (Fig. 2A, Interface 3 detail).	RESULTS
+75	82	Leu 521	residue_name_number	In particular, the side chains of hydrophobic residues, including Phe 518, Leu 521, and Met 524, are directed toward each other, where they make both inter- and intramolecular contacts (Fig. 2A, Interface 3 detail).	RESULTS
+88	95	Met 524	residue_name_number	In particular, the side chains of hydrophobic residues, including Phe 518, Leu 521, and Met 524, are directed toward each other, where they make both inter- and intramolecular contacts (Fig. 2A, Interface 3 detail).	RESULTS
+195	206	Interface 3	site	In particular, the side chains of hydrophobic residues, including Phe 518, Leu 521, and Met 524, are directed toward each other, where they make both inter- and intramolecular contacts (Fig. 2A, Interface 3 detail).	RESULTS
+56	73	crystal structure	evidence	To further investigate the interactions observed in our crystal structure, we generated a C-terminal deletion mutant (SEL1L348–497) lacking SLR motif 9 (helix 9A and 9B) from SEL1Lcent for comparative analysis.	RESULTS
+101	116	deletion mutant	protein_state	To further investigate the interactions observed in our crystal structure, we generated a C-terminal deletion mutant (SEL1L348–497) lacking SLR motif 9 (helix 9A and 9B) from SEL1Lcent for comparative analysis.	RESULTS
+118	130	SEL1L348–497	mutant	To further investigate the interactions observed in our crystal structure, we generated a C-terminal deletion mutant (SEL1L348–497) lacking SLR motif 9 (helix 9A and 9B) from SEL1Lcent for comparative analysis.	RESULTS
+132	139	lacking	protein_state	To further investigate the interactions observed in our crystal structure, we generated a C-terminal deletion mutant (SEL1L348–497) lacking SLR motif 9 (helix 9A and 9B) from SEL1Lcent for comparative analysis.	RESULTS
+140	151	SLR motif 9	structure_element	To further investigate the interactions observed in our crystal structure, we generated a C-terminal deletion mutant (SEL1L348–497) lacking SLR motif 9 (helix 9A and 9B) from SEL1Lcent for comparative analysis.	RESULTS
+153	161	helix 9A	structure_element	To further investigate the interactions observed in our crystal structure, we generated a C-terminal deletion mutant (SEL1L348–497) lacking SLR motif 9 (helix 9A and 9B) from SEL1Lcent for comparative analysis.	RESULTS
+166	168	9B	structure_element	To further investigate the interactions observed in our crystal structure, we generated a C-terminal deletion mutant (SEL1L348–497) lacking SLR motif 9 (helix 9A and 9B) from SEL1Lcent for comparative analysis.	RESULTS
+175	184	SEL1Lcent	structure_element	To further investigate the interactions observed in our crystal structure, we generated a C-terminal deletion mutant (SEL1L348–497) lacking SLR motif 9 (helix 9A and 9B) from SEL1Lcent for comparative analysis.	RESULTS
+4	19	deletion mutant	protein_state	The deletion mutant and the wild-type SEL1Lcent showed no difference in spectra by CD spectroscopy, indicating that the deletion of the SLR motif 9 did not affect the secondary structure of SEL1Lcent (Supplementary Fig. 3).	RESULTS
+28	37	wild-type	protein_state	The deletion mutant and the wild-type SEL1Lcent showed no difference in spectra by CD spectroscopy, indicating that the deletion of the SLR motif 9 did not affect the secondary structure of SEL1Lcent (Supplementary Fig. 3).	RESULTS
+38	47	SEL1Lcent	structure_element	The deletion mutant and the wild-type SEL1Lcent showed no difference in spectra by CD spectroscopy, indicating that the deletion of the SLR motif 9 did not affect the secondary structure of SEL1Lcent (Supplementary Fig. 3).	RESULTS
+72	79	spectra	evidence	The deletion mutant and the wild-type SEL1Lcent showed no difference in spectra by CD spectroscopy, indicating that the deletion of the SLR motif 9 did not affect the secondary structure of SEL1Lcent (Supplementary Fig. 3).	RESULTS
+83	98	CD spectroscopy	experimental_method	The deletion mutant and the wild-type SEL1Lcent showed no difference in spectra by CD spectroscopy, indicating that the deletion of the SLR motif 9 did not affect the secondary structure of SEL1Lcent (Supplementary Fig. 3).	RESULTS
+120	128	deletion	experimental_method	The deletion mutant and the wild-type SEL1Lcent showed no difference in spectra by CD spectroscopy, indicating that the deletion of the SLR motif 9 did not affect the secondary structure of SEL1Lcent (Supplementary Fig. 3).	RESULTS
+136	147	SLR motif 9	structure_element	The deletion mutant and the wild-type SEL1Lcent showed no difference in spectra by CD spectroscopy, indicating that the deletion of the SLR motif 9 did not affect the secondary structure of SEL1Lcent (Supplementary Fig. 3).	RESULTS
+190	199	SEL1Lcent	structure_element	The deletion mutant and the wild-type SEL1Lcent showed no difference in spectra by CD spectroscopy, indicating that the deletion of the SLR motif 9 did not affect the secondary structure of SEL1Lcent (Supplementary Fig. 3).	RESULTS
+13	19	mutant	protein_state	However, the mutant behaved as a monomer in size-exclusion chromatography and analytical ultracentrifugation experiments (Fig. 2B, Supplementary Fig. 2C).	RESULTS
+33	40	monomer	oligomeric_state	However, the mutant behaved as a monomer in size-exclusion chromatography and analytical ultracentrifugation experiments (Fig. 2B, Supplementary Fig. 2C).	RESULTS
+44	73	size-exclusion chromatography	experimental_method	However, the mutant behaved as a monomer in size-exclusion chromatography and analytical ultracentrifugation experiments (Fig. 2B, Supplementary Fig. 2C).	RESULTS
+78	108	analytical ultracentrifugation	experimental_method	However, the mutant behaved as a monomer in size-exclusion chromatography and analytical ultracentrifugation experiments (Fig. 2B, Supplementary Fig. 2C).	RESULTS
+63	68	dimer	oligomeric_state	Additionally, to further validate the key residues involved in dimer formation, we generated a triple point mutant (Interface 1, I515A, L516A, and Y519A) of the hydrophobic residues that are involved in dimerization.	RESULTS
+95	114	triple point mutant	protein_state	Additionally, to further validate the key residues involved in dimer formation, we generated a triple point mutant (Interface 1, I515A, L516A, and Y519A) of the hydrophobic residues that are involved in dimerization.	RESULTS
+116	127	Interface 1	site	Additionally, to further validate the key residues involved in dimer formation, we generated a triple point mutant (Interface 1, I515A, L516A, and Y519A) of the hydrophobic residues that are involved in dimerization.	RESULTS
+129	134	I515A	mutant	Additionally, to further validate the key residues involved in dimer formation, we generated a triple point mutant (Interface 1, I515A, L516A, and Y519A) of the hydrophobic residues that are involved in dimerization.	RESULTS
+136	141	L516A	mutant	Additionally, to further validate the key residues involved in dimer formation, we generated a triple point mutant (Interface 1, I515A, L516A, and Y519A) of the hydrophobic residues that are involved in dimerization.	RESULTS
+147	152	Y519A	mutant	Additionally, to further validate the key residues involved in dimer formation, we generated a triple point mutant (Interface 1, I515A, L516A, and Y519A) of the hydrophobic residues that are involved in dimerization.	RESULTS
+203	215	dimerization	oligomeric_state	Additionally, to further validate the key residues involved in dimer formation, we generated a triple point mutant (Interface 1, I515A, L516A, and Y519A) of the hydrophobic residues that are involved in dimerization.	RESULTS
+4	23	triple point mutant	protein_state	The triple point mutant eluted at the monomer position upon size-exclusion chromatography, while the negative control point mutant (Q460A) eluted at the same position as the wild-type.	RESULTS
+38	45	monomer	oligomeric_state	The triple point mutant eluted at the monomer position upon size-exclusion chromatography, while the negative control point mutant (Q460A) eluted at the same position as the wild-type.	RESULTS
+60	89	size-exclusion chromatography	experimental_method	The triple point mutant eluted at the monomer position upon size-exclusion chromatography, while the negative control point mutant (Q460A) eluted at the same position as the wild-type.	RESULTS
+118	130	point mutant	protein_state	The triple point mutant eluted at the monomer position upon size-exclusion chromatography, while the negative control point mutant (Q460A) eluted at the same position as the wild-type.	RESULTS
+132	137	Q460A	mutant	The triple point mutant eluted at the monomer position upon size-exclusion chromatography, while the negative control point mutant (Q460A) eluted at the same position as the wild-type.	RESULTS
+174	183	wild-type	protein_state	The triple point mutant eluted at the monomer position upon size-exclusion chromatography, while the negative control point mutant (Q460A) eluted at the same position as the wild-type.	RESULTS
+11	34	single-residue mutation	experimental_method	Notably, a single-residue mutation (L521A in interface 3) abolished the dimerization of SEL1Lcent (Fig. 2B).	RESULTS
+36	41	L521A	mutant	Notably, a single-residue mutation (L521A in interface 3) abolished the dimerization of SEL1Lcent (Fig. 2B).	RESULTS
+45	56	interface 3	site	Notably, a single-residue mutation (L521A in interface 3) abolished the dimerization of SEL1Lcent (Fig. 2B).	RESULTS
+58	84	abolished the dimerization	protein_state	Notably, a single-residue mutation (L521A in interface 3) abolished the dimerization of SEL1Lcent (Fig. 2B).	RESULTS
+88	97	SEL1Lcent	structure_element	Notably, a single-residue mutation (L521A in interface 3) abolished the dimerization of SEL1Lcent (Fig. 2B).	RESULTS
+0	7	Leu 521	residue_name_number	Leu 521 is located in the dimerization center of the antiparallel 9B helices in the SEL1Lcent dimer.	RESULTS
+26	45	dimerization center	site	Leu 521 is located in the dimerization center of the antiparallel 9B helices in the SEL1Lcent dimer.	RESULTS
+66	76	9B helices	structure_element	Leu 521 is located in the dimerization center of the antiparallel 9B helices in the SEL1Lcent dimer.	RESULTS
+84	93	SEL1Lcent	structure_element	Leu 521 is located in the dimerization center of the antiparallel 9B helices in the SEL1Lcent dimer.	RESULTS
+94	99	dimer	oligomeric_state	Leu 521 is located in the dimerization center of the antiparallel 9B helices in the SEL1Lcent dimer.	RESULTS
+22	53	structural and biochemical data	evidence	Taken together, these structural and biochemical data demonstrate that SEL1Lcent exists as a dimer in solution and that SLR motif 9 in SEL1Lcent plays an important role in generating a two-fold dimerization interface.	RESULTS
+71	80	SEL1Lcent	structure_element	Taken together, these structural and biochemical data demonstrate that SEL1Lcent exists as a dimer in solution and that SLR motif 9 in SEL1Lcent plays an important role in generating a two-fold dimerization interface.	RESULTS
+93	98	dimer	oligomeric_state	Taken together, these structural and biochemical data demonstrate that SEL1Lcent exists as a dimer in solution and that SLR motif 9 in SEL1Lcent plays an important role in generating a two-fold dimerization interface.	RESULTS
+120	131	SLR motif 9	structure_element	Taken together, these structural and biochemical data demonstrate that SEL1Lcent exists as a dimer in solution and that SLR motif 9 in SEL1Lcent plays an important role in generating a two-fold dimerization interface.	RESULTS
+135	144	SEL1Lcent	structure_element	Taken together, these structural and biochemical data demonstrate that SEL1Lcent exists as a dimer in solution and that SLR motif 9 in SEL1Lcent plays an important role in generating a two-fold dimerization interface.	RESULTS
+194	216	dimerization interface	site	Taken together, these structural and biochemical data demonstrate that SEL1Lcent exists as a dimer in solution and that SLR motif 9 in SEL1Lcent plays an important role in generating a two-fold dimerization interface.	RESULTS
+8	15	Glycine	residue_name	The Two Glycine Residues (G512 and G513) Create a Hinge for Domain Swapping of SLR Motif 9	RESULTS
+26	30	G512	residue_name_number	The Two Glycine Residues (G512 and G513) Create a Hinge for Domain Swapping of SLR Motif 9	RESULTS
+35	39	G513	residue_name_number	The Two Glycine Residues (G512 and G513) Create a Hinge for Domain Swapping of SLR Motif 9	RESULTS
+50	55	Hinge	structure_element	The Two Glycine Residues (G512 and G513) Create a Hinge for Domain Swapping of SLR Motif 9	RESULTS
+79	90	SLR Motif 9	structure_element	The Two Glycine Residues (G512 and G513) Create a Hinge for Domain Swapping of SLR Motif 9	RESULTS
+0	4	SLRs	structure_element	SLRs of mouse SEL1L were predicted using the TPRpred server.	RESULTS
+8	13	mouse	taxonomy_domain	SLRs of mouse SEL1L were predicted using the TPRpred server.	RESULTS
+14	19	SEL1L	protein	SLRs of mouse SEL1L were predicted using the TPRpred server.	RESULTS
+45	59	TPRpred server	experimental_method	SLRs of mouse SEL1L were predicted using the TPRpred server.	RESULTS
+25	36	full-length	protein_state	Based on the prediction, full-length SEL1L contains a total of 11 SLR motifs, and our construct corresponds to SLR motifs 5 through 9.	RESULTS
+37	42	SEL1L	protein	Based on the prediction, full-length SEL1L contains a total of 11 SLR motifs, and our construct corresponds to SLR motifs 5 through 9.	RESULTS
+66	69	SLR	structure_element	Based on the prediction, full-length SEL1L contains a total of 11 SLR motifs, and our construct corresponds to SLR motifs 5 through 9.	RESULTS
+111	133	SLR motifs 5 through 9	structure_element	Based on the prediction, full-length SEL1L contains a total of 11 SLR motifs, and our construct corresponds to SLR motifs 5 through 9.	RESULTS
+35	43	helix 9A	structure_element	Although amino acid sequences from helix 9A and 9B correctly aligned with the regular SLR repeats and corresponded to SLR motif 9 (Fig. 3A), the structural arrangement of the two helices deviated from the common structure for the SLR motif.	RESULTS
+48	50	9B	structure_element	Although amino acid sequences from helix 9A and 9B correctly aligned with the regular SLR repeats and corresponded to SLR motif 9 (Fig. 3A), the structural arrangement of the two helices deviated from the common structure for the SLR motif.	RESULTS
+86	97	SLR repeats	structure_element	Although amino acid sequences from helix 9A and 9B correctly aligned with the regular SLR repeats and corresponded to SLR motif 9 (Fig. 3A), the structural arrangement of the two helices deviated from the common structure for the SLR motif.	RESULTS
+118	129	SLR motif 9	structure_element	Although amino acid sequences from helix 9A and 9B correctly aligned with the regular SLR repeats and corresponded to SLR motif 9 (Fig. 3A), the structural arrangement of the two helices deviated from the common structure for the SLR motif.	RESULTS
+179	186	helices	structure_element	Although amino acid sequences from helix 9A and 9B correctly aligned with the regular SLR repeats and corresponded to SLR motif 9 (Fig. 3A), the structural arrangement of the two helices deviated from the common structure for the SLR motif.	RESULTS
+230	233	SLR	structure_element	Although amino acid sequences from helix 9A and 9B correctly aligned with the regular SLR repeats and corresponded to SLR motif 9 (Fig. 3A), the structural arrangement of the two helices deviated from the common structure for the SLR motif.	RESULTS
+17	34	crystal structure	evidence	According to our crystal structure, the central axis of helix 9B is almost parallel to that of helix 9A (Fig. 3B).	RESULTS
+56	64	helix 9B	structure_element	According to our crystal structure, the central axis of helix 9B is almost parallel to that of helix 9A (Fig. 3B).	RESULTS
+95	103	helix 9A	structure_element	According to our crystal structure, the central axis of helix 9B is almost parallel to that of helix 9A (Fig. 3B).	RESULTS
+38	49	SLR motif 9	structure_element	However, this unusual conformation of SLR motif 9 seems to be essential for dimer formation, as described earlier.	RESULTS
+76	81	dimer	oligomeric_state	However, this unusual conformation of SLR motif 9 seems to be essential for dimer formation, as described earlier.	RESULTS
+53	60	Gly 512	residue_name_number	For this structural geometry, two adjacent residues, Gly 512 and Gly 513, in SEL1L confer flexibility at this position by adopting main-chain dihedral angles that are disallowed for non-glycine residues.	RESULTS
+65	72	Gly 513	residue_name_number	For this structural geometry, two adjacent residues, Gly 512 and Gly 513, in SEL1L confer flexibility at this position by adopting main-chain dihedral angles that are disallowed for non-glycine residues.	RESULTS
+77	82	SEL1L	protein	For this structural geometry, two adjacent residues, Gly 512 and Gly 513, in SEL1L confer flexibility at this position by adopting main-chain dihedral angles that are disallowed for non-glycine residues.	RESULTS
+47	54	Gly 512	residue_name_number	The phi and psi dihedrals are 100° and 20° for Gly 512, and 110° and −20° for Gly 513, respectively (Fig. 3C).	RESULTS
+78	85	Gly 513	residue_name_number	The phi and psi dihedrals are 100° and 20° for Gly 512, and 110° and −20° for Gly 513, respectively (Fig. 3C).	RESULTS
+0	7	Gly 513	residue_name_number	Gly 513 is conserved among other SLR motifs in the SEL1Lcent, but Gly 512 is present only in the SLR motif 9 of SEL1Lcent (Fig. 3A).	RESULTS
+11	20	conserved	protein_state	Gly 513 is conserved among other SLR motifs in the SEL1Lcent, but Gly 512 is present only in the SLR motif 9 of SEL1Lcent (Fig. 3A).	RESULTS
+33	36	SLR	structure_element	Gly 513 is conserved among other SLR motifs in the SEL1Lcent, but Gly 512 is present only in the SLR motif 9 of SEL1Lcent (Fig. 3A).	RESULTS
+51	60	SEL1Lcent	structure_element	Gly 513 is conserved among other SLR motifs in the SEL1Lcent, but Gly 512 is present only in the SLR motif 9 of SEL1Lcent (Fig. 3A).	RESULTS
+66	73	Gly 512	residue_name_number	Gly 513 is conserved among other SLR motifs in the SEL1Lcent, but Gly 512 is present only in the SLR motif 9 of SEL1Lcent (Fig. 3A).	RESULTS
+97	108	SLR motif 9	structure_element	Gly 513 is conserved among other SLR motifs in the SEL1Lcent, but Gly 512 is present only in the SLR motif 9 of SEL1Lcent (Fig. 3A).	RESULTS
+112	121	SEL1Lcent	structure_element	Gly 513 is conserved among other SLR motifs in the SEL1Lcent, but Gly 512 is present only in the SLR motif 9 of SEL1Lcent (Fig. 3A).	RESULTS
+10	17	Gly-Gly	structure_element	Thus, the Gly-Gly residues generate an unusual sharp bend at the C-terminal SLR motif 9.	RESULTS
+76	87	SLR motif 9	structure_element	Thus, the Gly-Gly residues generate an unusual sharp bend at the C-terminal SLR motif 9.	RESULTS
+21	28	glycine	residue_name	The involvement of a glycine residue in forming a hinge for domain swapping has been reported previously.	RESULTS
+50	55	hinge	structure_element	The involvement of a glycine residue in forming a hinge for domain swapping has been reported previously.	RESULTS
+20	27	Gly 513	residue_name_number	The significance of Gly 513 is further highlighted by its absolute conservation among different species, including the budding yeast homolog Hrd3p.	RESULTS
+58	79	absolute conservation	protein_state	The significance of Gly 513 is further highlighted by its absolute conservation among different species, including the budding yeast homolog Hrd3p.	RESULTS
+119	132	budding yeast	taxonomy_domain	The significance of Gly 513 is further highlighted by its absolute conservation among different species, including the budding yeast homolog Hrd3p.	RESULTS
+141	146	Hrd3p	protein	The significance of Gly 513 is further highlighted by its absolute conservation among different species, including the budding yeast homolog Hrd3p.	RESULTS
+41	48	Gly 512	residue_name_number	To further investigate the importance of Gly 512 and Gly 513 in the unusual SLR motif geometry, we generated a point mutation (Gly to Ala), which restricts the flexibility. Although the Gly 512 and Gly 513 residues are closely surrounded by helix 9B from the counter protomer, there is enough space for the side chain of alanine, suggesting that no steric hindrance would be caused by the mutation (Fig. 3C).	RESULTS
+53	60	Gly 513	residue_name_number	To further investigate the importance of Gly 512 and Gly 513 in the unusual SLR motif geometry, we generated a point mutation (Gly to Ala), which restricts the flexibility. Although the Gly 512 and Gly 513 residues are closely surrounded by helix 9B from the counter protomer, there is enough space for the side chain of alanine, suggesting that no steric hindrance would be caused by the mutation (Fig. 3C).	RESULTS
+76	79	SLR	structure_element	To further investigate the importance of Gly 512 and Gly 513 in the unusual SLR motif geometry, we generated a point mutation (Gly to Ala), which restricts the flexibility. Although the Gly 512 and Gly 513 residues are closely surrounded by helix 9B from the counter protomer, there is enough space for the side chain of alanine, suggesting that no steric hindrance would be caused by the mutation (Fig. 3C).	RESULTS
+111	125	point mutation	experimental_method	To further investigate the importance of Gly 512 and Gly 513 in the unusual SLR motif geometry, we generated a point mutation (Gly to Ala), which restricts the flexibility. Although the Gly 512 and Gly 513 residues are closely surrounded by helix 9B from the counter protomer, there is enough space for the side chain of alanine, suggesting that no steric hindrance would be caused by the mutation (Fig. 3C).	RESULTS
+127	137	Gly to Ala	mutant	To further investigate the importance of Gly 512 and Gly 513 in the unusual SLR motif geometry, we generated a point mutation (Gly to Ala), which restricts the flexibility. Although the Gly 512 and Gly 513 residues are closely surrounded by helix 9B from the counter protomer, there is enough space for the side chain of alanine, suggesting that no steric hindrance would be caused by the mutation (Fig. 3C).	RESULTS
+186	193	Gly 512	residue_name_number	To further investigate the importance of Gly 512 and Gly 513 in the unusual SLR motif geometry, we generated a point mutation (Gly to Ala), which restricts the flexibility. Although the Gly 512 and Gly 513 residues are closely surrounded by helix 9B from the counter protomer, there is enough space for the side chain of alanine, suggesting that no steric hindrance would be caused by the mutation (Fig. 3C).	RESULTS
+198	205	Gly 513	residue_name_number	To further investigate the importance of Gly 512 and Gly 513 in the unusual SLR motif geometry, we generated a point mutation (Gly to Ala), which restricts the flexibility. Although the Gly 512 and Gly 513 residues are closely surrounded by helix 9B from the counter protomer, there is enough space for the side chain of alanine, suggesting that no steric hindrance would be caused by the mutation (Fig. 3C).	RESULTS
+241	249	helix 9B	structure_element	To further investigate the importance of Gly 512 and Gly 513 in the unusual SLR motif geometry, we generated a point mutation (Gly to Ala), which restricts the flexibility. Although the Gly 512 and Gly 513 residues are closely surrounded by helix 9B from the counter protomer, there is enough space for the side chain of alanine, suggesting that no steric hindrance would be caused by the mutation (Fig. 3C).	RESULTS
+267	275	protomer	oligomeric_state	To further investigate the importance of Gly 512 and Gly 513 in the unusual SLR motif geometry, we generated a point mutation (Gly to Ala), which restricts the flexibility. Although the Gly 512 and Gly 513 residues are closely surrounded by helix 9B from the counter protomer, there is enough space for the side chain of alanine, suggesting that no steric hindrance would be caused by the mutation (Fig. 3C).	RESULTS
+321	328	alanine	residue_name	To further investigate the importance of Gly 512 and Gly 513 in the unusual SLR motif geometry, we generated a point mutation (Gly to Ala), which restricts the flexibility. Although the Gly 512 and Gly 513 residues are closely surrounded by helix 9B from the counter protomer, there is enough space for the side chain of alanine, suggesting that no steric hindrance would be caused by the mutation (Fig. 3C).	RESULTS
+389	397	mutation	experimental_method	To further investigate the importance of Gly 512 and Gly 513 in the unusual SLR motif geometry, we generated a point mutation (Gly to Ala), which restricts the flexibility. Although the Gly 512 and Gly 513 residues are closely surrounded by helix 9B from the counter protomer, there is enough space for the side chain of alanine, suggesting that no steric hindrance would be caused by the mutation (Fig. 3C).	RESULTS
+34	42	mutation	experimental_method	This means that the effect of the mutation is mainly to generate a more restricted geometry at the hinge region.	RESULTS
+99	104	hinge	structure_element	This means that the effect of the mutation is mainly to generate a more restricted geometry at the hinge region.	RESULTS
+0	5	G512A	mutant	G512A or G513A alone showed no differences from wild-type in terms of the size-exclusion chromatography elution profile (Fig. 3D), suggesting that the restriction for single glycine flexibility would not be enough to break the swapped structure of helix 9B.	RESULTS
+9	14	G513A	mutant	G512A or G513A alone showed no differences from wild-type in terms of the size-exclusion chromatography elution profile (Fig. 3D), suggesting that the restriction for single glycine flexibility would not be enough to break the swapped structure of helix 9B.	RESULTS
+48	57	wild-type	protein_state	G512A or G513A alone showed no differences from wild-type in terms of the size-exclusion chromatography elution profile (Fig. 3D), suggesting that the restriction for single glycine flexibility would not be enough to break the swapped structure of helix 9B.	RESULTS
+74	103	size-exclusion chromatography	experimental_method	G512A or G513A alone showed no differences from wild-type in terms of the size-exclusion chromatography elution profile (Fig. 3D), suggesting that the restriction for single glycine flexibility would not be enough to break the swapped structure of helix 9B.	RESULTS
+174	181	glycine	residue_name	G512A or G513A alone showed no differences from wild-type in terms of the size-exclusion chromatography elution profile (Fig. 3D), suggesting that the restriction for single glycine flexibility would not be enough to break the swapped structure of helix 9B.	RESULTS
+248	256	helix 9B	structure_element	G512A or G513A alone showed no differences from wild-type in terms of the size-exclusion chromatography elution profile (Fig. 3D), suggesting that the restriction for single glycine flexibility would not be enough to break the swapped structure of helix 9B.	RESULTS
+13	26	double mutant	protein_state	However, the double mutant (G512A/G513A) eluted over a broad range and much earlier than the wild-type, suggesting that mutation of the residues involved in the hinge linking helix 9A and 9B significantly affected the geometry of helix 9B in generating domain swapping, and eventually altered the overall oligomeric state of SEL1Lcent into a polydisperse pattern (Fig. 3D, Supplementary Fig. 6).	RESULTS
+28	33	G512A	mutant	However, the double mutant (G512A/G513A) eluted over a broad range and much earlier than the wild-type, suggesting that mutation of the residues involved in the hinge linking helix 9A and 9B significantly affected the geometry of helix 9B in generating domain swapping, and eventually altered the overall oligomeric state of SEL1Lcent into a polydisperse pattern (Fig. 3D, Supplementary Fig. 6).	RESULTS
+34	39	G513A	mutant	However, the double mutant (G512A/G513A) eluted over a broad range and much earlier than the wild-type, suggesting that mutation of the residues involved in the hinge linking helix 9A and 9B significantly affected the geometry of helix 9B in generating domain swapping, and eventually altered the overall oligomeric state of SEL1Lcent into a polydisperse pattern (Fig. 3D, Supplementary Fig. 6).	RESULTS
+93	102	wild-type	protein_state	However, the double mutant (G512A/G513A) eluted over a broad range and much earlier than the wild-type, suggesting that mutation of the residues involved in the hinge linking helix 9A and 9B significantly affected the geometry of helix 9B in generating domain swapping, and eventually altered the overall oligomeric state of SEL1Lcent into a polydisperse pattern (Fig. 3D, Supplementary Fig. 6).	RESULTS
+120	128	mutation	experimental_method	However, the double mutant (G512A/G513A) eluted over a broad range and much earlier than the wild-type, suggesting that mutation of the residues involved in the hinge linking helix 9A and 9B significantly affected the geometry of helix 9B in generating domain swapping, and eventually altered the overall oligomeric state of SEL1Lcent into a polydisperse pattern (Fig. 3D, Supplementary Fig. 6).	RESULTS
+161	166	hinge	structure_element	However, the double mutant (G512A/G513A) eluted over a broad range and much earlier than the wild-type, suggesting that mutation of the residues involved in the hinge linking helix 9A and 9B significantly affected the geometry of helix 9B in generating domain swapping, and eventually altered the overall oligomeric state of SEL1Lcent into a polydisperse pattern (Fig. 3D, Supplementary Fig. 6).	RESULTS
+175	183	helix 9A	structure_element	However, the double mutant (G512A/G513A) eluted over a broad range and much earlier than the wild-type, suggesting that mutation of the residues involved in the hinge linking helix 9A and 9B significantly affected the geometry of helix 9B in generating domain swapping, and eventually altered the overall oligomeric state of SEL1Lcent into a polydisperse pattern (Fig. 3D, Supplementary Fig. 6).	RESULTS
+188	190	9B	structure_element	However, the double mutant (G512A/G513A) eluted over a broad range and much earlier than the wild-type, suggesting that mutation of the residues involved in the hinge linking helix 9A and 9B significantly affected the geometry of helix 9B in generating domain swapping, and eventually altered the overall oligomeric state of SEL1Lcent into a polydisperse pattern (Fig. 3D, Supplementary Fig. 6).	RESULTS
+230	238	helix 9B	structure_element	However, the double mutant (G512A/G513A) eluted over a broad range and much earlier than the wild-type, suggesting that mutation of the residues involved in the hinge linking helix 9A and 9B significantly affected the geometry of helix 9B in generating domain swapping, and eventually altered the overall oligomeric state of SEL1Lcent into a polydisperse pattern (Fig. 3D, Supplementary Fig. 6).	RESULTS
+325	334	SEL1Lcent	structure_element	However, the double mutant (G512A/G513A) eluted over a broad range and much earlier than the wild-type, suggesting that mutation of the residues involved in the hinge linking helix 9A and 9B significantly affected the geometry of helix 9B in generating domain swapping, and eventually altered the overall oligomeric state of SEL1Lcent into a polydisperse pattern (Fig. 3D, Supplementary Fig. 6).	RESULTS
+23	33	mutated to	experimental_method	When the residues were mutated to lysine (G512K/G513K), the mutant not only restricted the geometry of residues at the hinge but also generated steric hindrance during interaction with the counter protomer of SEL1Lcent, thereby inhibiting self-association of SEL1Lcent completely.	RESULTS
+34	40	lysine	residue_name	When the residues were mutated to lysine (G512K/G513K), the mutant not only restricted the geometry of residues at the hinge but also generated steric hindrance during interaction with the counter protomer of SEL1Lcent, thereby inhibiting self-association of SEL1Lcent completely.	RESULTS
+42	47	G512K	mutant	When the residues were mutated to lysine (G512K/G513K), the mutant not only restricted the geometry of residues at the hinge but also generated steric hindrance during interaction with the counter protomer of SEL1Lcent, thereby inhibiting self-association of SEL1Lcent completely.	RESULTS
+48	53	G513K	mutant	When the residues were mutated to lysine (G512K/G513K), the mutant not only restricted the geometry of residues at the hinge but also generated steric hindrance during interaction with the counter protomer of SEL1Lcent, thereby inhibiting self-association of SEL1Lcent completely.	RESULTS
+60	66	mutant	protein_state	When the residues were mutated to lysine (G512K/G513K), the mutant not only restricted the geometry of residues at the hinge but also generated steric hindrance during interaction with the counter protomer of SEL1Lcent, thereby inhibiting self-association of SEL1Lcent completely.	RESULTS
+119	124	hinge	structure_element	When the residues were mutated to lysine (G512K/G513K), the mutant not only restricted the geometry of residues at the hinge but also generated steric hindrance during interaction with the counter protomer of SEL1Lcent, thereby inhibiting self-association of SEL1Lcent completely.	RESULTS
+197	205	protomer	oligomeric_state	When the residues were mutated to lysine (G512K/G513K), the mutant not only restricted the geometry of residues at the hinge but also generated steric hindrance during interaction with the counter protomer of SEL1Lcent, thereby inhibiting self-association of SEL1Lcent completely.	RESULTS
+209	218	SEL1Lcent	structure_element	When the residues were mutated to lysine (G512K/G513K), the mutant not only restricted the geometry of residues at the hinge but also generated steric hindrance during interaction with the counter protomer of SEL1Lcent, thereby inhibiting self-association of SEL1Lcent completely.	RESULTS
+259	268	SEL1Lcent	structure_element	When the residues were mutated to lysine (G512K/G513K), the mutant not only restricted the geometry of residues at the hinge but also generated steric hindrance during interaction with the counter protomer of SEL1Lcent, thereby inhibiting self-association of SEL1Lcent completely.	RESULTS
+4	9	G512K	mutant	The G512K/G513K double mutant eluted at the monomer position in size-exclusion chromatography (Fig. 3D).	RESULTS
+10	15	G513K	mutant	The G512K/G513K double mutant eluted at the monomer position in size-exclusion chromatography (Fig. 3D).	RESULTS
+16	29	double mutant	protein_state	The G512K/G513K double mutant eluted at the monomer position in size-exclusion chromatography (Fig. 3D).	RESULTS
+44	51	monomer	oligomeric_state	The G512K/G513K double mutant eluted at the monomer position in size-exclusion chromatography (Fig. 3D).	RESULTS
+64	93	size-exclusion chromatography	experimental_method	The G512K/G513K double mutant eluted at the monomer position in size-exclusion chromatography (Fig. 3D).	RESULTS
+61	69	mutation	experimental_method	A previous study shows that induction of steric hindrance by mutation destabilizes the dimerization interface of a different protein, ClC transporter.	RESULTS
+87	109	dimerization interface	site	A previous study shows that induction of steric hindrance by mutation destabilizes the dimerization interface of a different protein, ClC transporter.	RESULTS
+134	149	ClC transporter	protein_type	A previous study shows that induction of steric hindrance by mutation destabilizes the dimerization interface of a different protein, ClC transporter.	RESULTS
+42	49	Gly 512	residue_name_number	Collectively, these data suggest that the Gly 512 and Gly 513 at the connection between helix 9A and 9B play a crucial role in forming the domain-swapped conformation that enables dimer formation.	RESULTS
+54	61	Gly 513	residue_name_number	Collectively, these data suggest that the Gly 512 and Gly 513 at the connection between helix 9A and 9B play a crucial role in forming the domain-swapped conformation that enables dimer formation.	RESULTS
+88	96	helix 9A	structure_element	Collectively, these data suggest that the Gly 512 and Gly 513 at the connection between helix 9A and 9B play a crucial role in forming the domain-swapped conformation that enables dimer formation.	RESULTS
+101	103	9B	structure_element	Collectively, these data suggest that the Gly 512 and Gly 513 at the connection between helix 9A and 9B play a crucial role in forming the domain-swapped conformation that enables dimer formation.	RESULTS
+139	153	domain-swapped	protein_state	Collectively, these data suggest that the Gly 512 and Gly 513 at the connection between helix 9A and 9B play a crucial role in forming the domain-swapped conformation that enables dimer formation.	RESULTS
+180	185	dimer	oligomeric_state	Collectively, these data suggest that the Gly 512 and Gly 513 at the connection between helix 9A and 9B play a crucial role in forming the domain-swapped conformation that enables dimer formation.	RESULTS
+0	5	SEL1L	protein	SEL1L Forms Self-oligomers through SEL1Lcent domain in vivo	RESULTS
+12	26	Self-oligomers	oligomeric_state	SEL1L Forms Self-oligomers through SEL1Lcent domain in vivo	RESULTS
+35	44	SEL1Lcent	structure_element	SEL1L Forms Self-oligomers through SEL1Lcent domain in vivo	RESULTS
+21	26	SEL1L	protein	Next, we examined if SEL1L also forms self-oligomers in vivo using HEK293T cells.	RESULTS
+38	52	self-oligomers	oligomeric_state	Next, we examined if SEL1L also forms self-oligomers in vivo using HEK293T cells.	RESULTS
+13	24	full-length	protein_state	We generated full-length SEL1L-HA and SEL1L-FLAG fusion constructs and co-transfected the constructs into HEK293T cells.	RESULTS
+25	30	SEL1L	protein	We generated full-length SEL1L-HA and SEL1L-FLAG fusion constructs and co-transfected the constructs into HEK293T cells.	RESULTS
+31	33	HA	experimental_method	We generated full-length SEL1L-HA and SEL1L-FLAG fusion constructs and co-transfected the constructs into HEK293T cells.	RESULTS
+38	43	SEL1L	protein	We generated full-length SEL1L-HA and SEL1L-FLAG fusion constructs and co-transfected the constructs into HEK293T cells.	RESULTS
+44	48	FLAG	experimental_method	We generated full-length SEL1L-HA and SEL1L-FLAG fusion constructs and co-transfected the constructs into HEK293T cells.	RESULTS
+49	66	fusion constructs	experimental_method	We generated full-length SEL1L-HA and SEL1L-FLAG fusion constructs and co-transfected the constructs into HEK293T cells.	RESULTS
+71	85	co-transfected	experimental_method	We generated full-length SEL1L-HA and SEL1L-FLAG fusion constructs and co-transfected the constructs into HEK293T cells.	RESULTS
+2	30	co-immunoprecipitation assay	experimental_method	A co-immunoprecipitation assay using an anti-FLAG antibody followed by Western blot analysis using an anti-HA antibody showed that full-length SEL1L forms self-oligomers in vivo (Fig. 4A).	RESULTS
+45	49	FLAG	experimental_method	A co-immunoprecipitation assay using an anti-FLAG antibody followed by Western blot analysis using an anti-HA antibody showed that full-length SEL1L forms self-oligomers in vivo (Fig. 4A).	RESULTS
+71	83	Western blot	experimental_method	A co-immunoprecipitation assay using an anti-FLAG antibody followed by Western blot analysis using an anti-HA antibody showed that full-length SEL1L forms self-oligomers in vivo (Fig. 4A).	RESULTS
+107	109	HA	experimental_method	A co-immunoprecipitation assay using an anti-FLAG antibody followed by Western blot analysis using an anti-HA antibody showed that full-length SEL1L forms self-oligomers in vivo (Fig. 4A).	RESULTS
+131	142	full-length	protein_state	A co-immunoprecipitation assay using an anti-FLAG antibody followed by Western blot analysis using an anti-HA antibody showed that full-length SEL1L forms self-oligomers in vivo (Fig. 4A).	RESULTS
+143	148	SEL1L	protein	A co-immunoprecipitation assay using an anti-FLAG antibody followed by Western blot analysis using an anti-HA antibody showed that full-length SEL1L forms self-oligomers in vivo (Fig. 4A).	RESULTS
+155	169	self-oligomers	oligomeric_state	A co-immunoprecipitation assay using an anti-FLAG antibody followed by Western blot analysis using an anti-HA antibody showed that full-length SEL1L forms self-oligomers in vivo (Fig. 4A).	RESULTS
+31	40	SEL1Lcent	structure_element	To further examine whether the SEL1Lcent domain is sufficient to physically interact with full-length SEL1L, we generated SEL1Lcent and SLR motif 9 deletion (SEL1L348–497) construct, which were fused to the C-terminus of SEL1L signal peptides.	RESULTS
+90	101	full-length	protein_state	To further examine whether the SEL1Lcent domain is sufficient to physically interact with full-length SEL1L, we generated SEL1Lcent and SLR motif 9 deletion (SEL1L348–497) construct, which were fused to the C-terminus of SEL1L signal peptides.	RESULTS
+102	107	SEL1L	protein	To further examine whether the SEL1Lcent domain is sufficient to physically interact with full-length SEL1L, we generated SEL1Lcent and SLR motif 9 deletion (SEL1L348–497) construct, which were fused to the C-terminus of SEL1L signal peptides.	RESULTS
+122	131	SEL1Lcent	structure_element	To further examine whether the SEL1Lcent domain is sufficient to physically interact with full-length SEL1L, we generated SEL1Lcent and SLR motif 9 deletion (SEL1L348–497) construct, which were fused to the C-terminus of SEL1L signal peptides.	RESULTS
+136	147	SLR motif 9	structure_element	To further examine whether the SEL1Lcent domain is sufficient to physically interact with full-length SEL1L, we generated SEL1Lcent and SLR motif 9 deletion (SEL1L348–497) construct, which were fused to the C-terminus of SEL1L signal peptides.	RESULTS
+148	156	deletion	experimental_method	To further examine whether the SEL1Lcent domain is sufficient to physically interact with full-length SEL1L, we generated SEL1Lcent and SLR motif 9 deletion (SEL1L348–497) construct, which were fused to the C-terminus of SEL1L signal peptides.	RESULTS
+158	170	SEL1L348–497	mutant	To further examine whether the SEL1Lcent domain is sufficient to physically interact with full-length SEL1L, we generated SEL1Lcent and SLR motif 9 deletion (SEL1L348–497) construct, which were fused to the C-terminus of SEL1L signal peptides.	RESULTS
+194	202	fused to	experimental_method	To further examine whether the SEL1Lcent domain is sufficient to physically interact with full-length SEL1L, we generated SEL1Lcent and SLR motif 9 deletion (SEL1L348–497) construct, which were fused to the C-terminus of SEL1L signal peptides.	RESULTS
+221	226	SEL1L	protein	To further examine whether the SEL1Lcent domain is sufficient to physically interact with full-length SEL1L, we generated SEL1Lcent and SLR motif 9 deletion (SEL1L348–497) construct, which were fused to the C-terminus of SEL1L signal peptides.	RESULTS
+227	242	signal peptides	structure_element	To further examine whether the SEL1Lcent domain is sufficient to physically interact with full-length SEL1L, we generated SEL1Lcent and SLR motif 9 deletion (SEL1L348–497) construct, which were fused to the C-terminus of SEL1L signal peptides.	RESULTS
+0	31	Co-immunoprecipitation analysis	experimental_method	Co-immunoprecipitation analysis showed that the SEL1Lcent was sufficient to physically interact with the full-length SEL1L, while SEL1L348–497 failed to do so (Fig. 4A).	RESULTS
+48	57	SEL1Lcent	structure_element	Co-immunoprecipitation analysis showed that the SEL1Lcent was sufficient to physically interact with the full-length SEL1L, while SEL1L348–497 failed to do so (Fig. 4A).	RESULTS
+105	116	full-length	protein_state	Co-immunoprecipitation analysis showed that the SEL1Lcent was sufficient to physically interact with the full-length SEL1L, while SEL1L348–497 failed to do so (Fig. 4A).	RESULTS
+117	122	SEL1L	protein	Co-immunoprecipitation analysis showed that the SEL1Lcent was sufficient to physically interact with the full-length SEL1L, while SEL1L348–497 failed to do so (Fig. 4A).	RESULTS
+130	142	SEL1L348–497	mutant	Co-immunoprecipitation analysis showed that the SEL1Lcent was sufficient to physically interact with the full-length SEL1L, while SEL1L348–497 failed to do so (Fig. 4A).	RESULTS
+48	60	SEL1L348–497	mutant	Interestingly, however, the expression level of SEL1L348–497 was consistently lower than that of SEL1Lcent (Fig. 4A,B).	RESULTS
+97	106	SEL1Lcent	structure_element	Interestingly, however, the expression level of SEL1L348–497 was consistently lower than that of SEL1Lcent (Fig. 4A,B).	RESULTS
+0	24	Semi-quantitative RT-PCR	experimental_method	Semi-quantitative RT-PCR revealed no significant difference in transcriptional levels of the two constructs (data not shown).	RESULTS
+19	31	SEL1L348–497	mutant	We speculated that SEL1L348–497 could be secreted while the SEL1Lcent is retained in the ER by association with the endogenous ERAD complex.	RESULTS
+60	69	SEL1Lcent	structure_element	We speculated that SEL1L348–497 could be secreted while the SEL1Lcent is retained in the ER by association with the endogenous ERAD complex.	RESULTS
+8	27	immunoprecipitation	experimental_method	Indeed, immunoprecipitation followed by western blot analysis using the culture medium detected secreted SEL1L348–497 fragment, but not SEL1Lcent (Fig. 4B).	RESULTS
+40	52	western blot	experimental_method	Indeed, immunoprecipitation followed by western blot analysis using the culture medium detected secreted SEL1L348–497 fragment, but not SEL1Lcent (Fig. 4B).	RESULTS
+105	117	SEL1L348–497	mutant	Indeed, immunoprecipitation followed by western blot analysis using the culture medium detected secreted SEL1L348–497 fragment, but not SEL1Lcent (Fig. 4B).	RESULTS
+136	145	SEL1Lcent	structure_element	Indeed, immunoprecipitation followed by western blot analysis using the culture medium detected secreted SEL1L348–497 fragment, but not SEL1Lcent (Fig. 4B).	RESULTS
+35	47	SEL1L348–497	mutant	We next examined if the reason why SEL1L348–497 failed to bind to the full-length SEL1L may be because of the lower level of SEL1L348–497 in the ER lumen compared to SEL1Lcent fragment.	RESULTS
+70	81	full-length	protein_state	We next examined if the reason why SEL1L348–497 failed to bind to the full-length SEL1L may be because of the lower level of SEL1L348–497 in the ER lumen compared to SEL1Lcent fragment.	RESULTS
+82	87	SEL1L	protein	We next examined if the reason why SEL1L348–497 failed to bind to the full-length SEL1L may be because of the lower level of SEL1L348–497 in the ER lumen compared to SEL1Lcent fragment.	RESULTS
+125	137	SEL1L348–497	mutant	We next examined if the reason why SEL1L348–497 failed to bind to the full-length SEL1L may be because of the lower level of SEL1L348–497 in the ER lumen compared to SEL1Lcent fragment.	RESULTS
+166	175	SEL1Lcent	structure_element	We next examined if the reason why SEL1L348–497 failed to bind to the full-length SEL1L may be because of the lower level of SEL1L348–497 in the ER lumen compared to SEL1Lcent fragment.	RESULTS
+23	28	SEL1L	protein	In order to retain two SEL1L fragments in the ER lumen, we added KDEL ER retention sequence to the C-terminus of both fragments.	RESULTS
+65	69	KDEL	structure_element	In order to retain two SEL1L fragments in the ER lumen, we added KDEL ER retention sequence to the C-terminus of both fragments.	RESULTS
+70	91	ER retention sequence	structure_element	In order to retain two SEL1L fragments in the ER lumen, we added KDEL ER retention sequence to the C-terminus of both fragments.	RESULTS
+24	28	KDEL	structure_element	Indeed, the addition of KDEL peptide increased the level of SEL1L348–497 in the ER lumen (Fig. 4D,E) and the immunostaining analysis showed both constructs were well localized to the ER (Fig. 4C).	RESULTS
+60	72	SEL1L348–497	mutant	Indeed, the addition of KDEL peptide increased the level of SEL1L348–497 in the ER lumen (Fig. 4D,E) and the immunostaining analysis showed both constructs were well localized to the ER (Fig. 4C).	RESULTS
+109	123	immunostaining	experimental_method	Indeed, the addition of KDEL peptide increased the level of SEL1L348–497 in the ER lumen (Fig. 4D,E) and the immunostaining analysis showed both constructs were well localized to the ER (Fig. 4C).	RESULTS
+28	37	SEL1Lcent	structure_element	We further analyzed whether SEL1Lcent may competitively inhibit the self-oligomerization of SEL1L in vivo.	RESULTS
+92	97	SEL1L	protein	We further analyzed whether SEL1Lcent may competitively inhibit the self-oligomerization of SEL1L in vivo.	RESULTS
+16	30	co-transfected	experimental_method	To this end, we co-transfected the differentially tagged full-length SEL1L (SEL1L-HA and SEL1L-FLAG) and increasing doses of SEL1Lcent-KDEL, SEL1L348–497-KDEL or SEL1Lcent (L521A)-KDEL, respectively.	RESULTS
+50	56	tagged	protein_state	To this end, we co-transfected the differentially tagged full-length SEL1L (SEL1L-HA and SEL1L-FLAG) and increasing doses of SEL1Lcent-KDEL, SEL1L348–497-KDEL or SEL1Lcent (L521A)-KDEL, respectively.	RESULTS
+57	68	full-length	protein_state	To this end, we co-transfected the differentially tagged full-length SEL1L (SEL1L-HA and SEL1L-FLAG) and increasing doses of SEL1Lcent-KDEL, SEL1L348–497-KDEL or SEL1Lcent (L521A)-KDEL, respectively.	RESULTS
+69	74	SEL1L	protein	To this end, we co-transfected the differentially tagged full-length SEL1L (SEL1L-HA and SEL1L-FLAG) and increasing doses of SEL1Lcent-KDEL, SEL1L348–497-KDEL or SEL1Lcent (L521A)-KDEL, respectively.	RESULTS
+76	81	SEL1L	protein	To this end, we co-transfected the differentially tagged full-length SEL1L (SEL1L-HA and SEL1L-FLAG) and increasing doses of SEL1Lcent-KDEL, SEL1L348–497-KDEL or SEL1Lcent (L521A)-KDEL, respectively.	RESULTS
+82	84	HA	experimental_method	To this end, we co-transfected the differentially tagged full-length SEL1L (SEL1L-HA and SEL1L-FLAG) and increasing doses of SEL1Lcent-KDEL, SEL1L348–497-KDEL or SEL1Lcent (L521A)-KDEL, respectively.	RESULTS
+89	94	SEL1L	protein	To this end, we co-transfected the differentially tagged full-length SEL1L (SEL1L-HA and SEL1L-FLAG) and increasing doses of SEL1Lcent-KDEL, SEL1L348–497-KDEL or SEL1Lcent (L521A)-KDEL, respectively.	RESULTS
+95	99	FLAG	experimental_method	To this end, we co-transfected the differentially tagged full-length SEL1L (SEL1L-HA and SEL1L-FLAG) and increasing doses of SEL1Lcent-KDEL, SEL1L348–497-KDEL or SEL1Lcent (L521A)-KDEL, respectively.	RESULTS
+105	121	increasing doses	experimental_method	To this end, we co-transfected the differentially tagged full-length SEL1L (SEL1L-HA and SEL1L-FLAG) and increasing doses of SEL1Lcent-KDEL, SEL1L348–497-KDEL or SEL1Lcent (L521A)-KDEL, respectively.	RESULTS
+125	139	SEL1Lcent-KDEL	mutant	To this end, we co-transfected the differentially tagged full-length SEL1L (SEL1L-HA and SEL1L-FLAG) and increasing doses of SEL1Lcent-KDEL, SEL1L348–497-KDEL or SEL1Lcent (L521A)-KDEL, respectively.	RESULTS
+141	158	SEL1L348–497-KDEL	mutant	To this end, we co-transfected the differentially tagged full-length SEL1L (SEL1L-HA and SEL1L-FLAG) and increasing doses of SEL1Lcent-KDEL, SEL1L348–497-KDEL or SEL1Lcent (L521A)-KDEL, respectively.	RESULTS
+162	184	SEL1Lcent (L521A)-KDEL	mutant	To this end, we co-transfected the differentially tagged full-length SEL1L (SEL1L-HA and SEL1L-FLAG) and increasing doses of SEL1Lcent-KDEL, SEL1L348–497-KDEL or SEL1Lcent (L521A)-KDEL, respectively.	RESULTS
+0	28	Co-immunoprecipitation assay	experimental_method	Co-immunoprecipitation assay revealed that wild-type SEL1Lcent-KDEL, indeed, competitively disrupted the self-association of the full-length SEL1L (Fig. 4E).	RESULTS
+43	52	wild-type	protein_state	Co-immunoprecipitation assay revealed that wild-type SEL1Lcent-KDEL, indeed, competitively disrupted the self-association of the full-length SEL1L (Fig. 4E).	RESULTS
+53	67	SEL1Lcent-KDEL	mutant	Co-immunoprecipitation assay revealed that wild-type SEL1Lcent-KDEL, indeed, competitively disrupted the self-association of the full-length SEL1L (Fig. 4E).	RESULTS
+129	140	full-length	protein_state	Co-immunoprecipitation assay revealed that wild-type SEL1Lcent-KDEL, indeed, competitively disrupted the self-association of the full-length SEL1L (Fig. 4E).	RESULTS
+13	30	SEL1L348–497-KDEL	mutant	In contrast, SEL1L348–497-KDEL and the single-residue mutation L521A in SEL1Lcent did not competitively inhibit the self-association of full-length SEL1L (Fig. 4E,F).	RESULTS
+63	68	L521A	mutant	In contrast, SEL1L348–497-KDEL and the single-residue mutation L521A in SEL1Lcent did not competitively inhibit the self-association of full-length SEL1L (Fig. 4E,F).	RESULTS
+72	81	SEL1Lcent	structure_element	In contrast, SEL1L348–497-KDEL and the single-residue mutation L521A in SEL1Lcent did not competitively inhibit the self-association of full-length SEL1L (Fig. 4E,F).	RESULTS
+136	147	full-length	protein_state	In contrast, SEL1L348–497-KDEL and the single-residue mutation L521A in SEL1Lcent did not competitively inhibit the self-association of full-length SEL1L (Fig. 4E,F).	RESULTS
+148	153	SEL1L	protein	In contrast, SEL1L348–497-KDEL and the single-residue mutation L521A in SEL1Lcent did not competitively inhibit the self-association of full-length SEL1L (Fig. 4E,F).	RESULTS
+28	33	SEL1L	protein	These data suggest that the SEL1L forms self-oligomers and the oligomerization is mediated by the SEL1Lcent domain in vivo.	RESULTS
+40	54	self-oligomers	oligomeric_state	These data suggest that the SEL1L forms self-oligomers and the oligomerization is mediated by the SEL1Lcent domain in vivo.	RESULTS
+98	107	SEL1Lcent	structure_element	These data suggest that the SEL1L forms self-oligomers and the oligomerization is mediated by the SEL1Lcent domain in vivo.	RESULTS
+0	21	Structural Comparison	experimental_method	Structural Comparison of SEL1L SLRs with TPRs or SLRs of Other Proteins	RESULTS
+25	30	SEL1L	protein	Structural Comparison of SEL1L SLRs with TPRs or SLRs of Other Proteins	RESULTS
+31	35	SLRs	structure_element	Structural Comparison of SEL1L SLRs with TPRs or SLRs of Other Proteins	RESULTS
+41	45	TPRs	structure_element	Structural Comparison of SEL1L SLRs with TPRs or SLRs of Other Proteins	RESULTS
+49	53	SLRs	structure_element	Structural Comparison of SEL1L SLRs with TPRs or SLRs of Other Proteins	RESULTS
+29	33	TPRs	structure_element	Previous studies reveal that TPRs and SLRs have similar consensus sequences, suggesting that their three-dimensional structures are also similar.	RESULTS
+38	42	SLRs	structure_element	Previous studies reveal that TPRs and SLRs have similar consensus sequences, suggesting that their three-dimensional structures are also similar.	RESULTS
+4	17	superposition	experimental_method	The superposition of isolated TPRs from Cdc23 (S. pombe, cell division cycle 23 homolog, PDB code 3ZN3) and SLRs from HcpC (Helicobacter Cysteine-rich Protein C, PDB code 1OUV) yields RMSDs below 1 Å, confirming that the isolated repeats are indeed similar.	RESULTS
+30	34	TPRs	structure_element	The superposition of isolated TPRs from Cdc23 (S. pombe, cell division cycle 23 homolog, PDB code 3ZN3) and SLRs from HcpC (Helicobacter Cysteine-rich Protein C, PDB code 1OUV) yields RMSDs below 1 Å, confirming that the isolated repeats are indeed similar.	RESULTS
+40	45	Cdc23	protein	The superposition of isolated TPRs from Cdc23 (S. pombe, cell division cycle 23 homolog, PDB code 3ZN3) and SLRs from HcpC (Helicobacter Cysteine-rich Protein C, PDB code 1OUV) yields RMSDs below 1 Å, confirming that the isolated repeats are indeed similar.	RESULTS
+47	55	S. pombe	species	The superposition of isolated TPRs from Cdc23 (S. pombe, cell division cycle 23 homolog, PDB code 3ZN3) and SLRs from HcpC (Helicobacter Cysteine-rich Protein C, PDB code 1OUV) yields RMSDs below 1 Å, confirming that the isolated repeats are indeed similar.	RESULTS
+57	79	cell division cycle 23	protein	The superposition of isolated TPRs from Cdc23 (S. pombe, cell division cycle 23 homolog, PDB code 3ZN3) and SLRs from HcpC (Helicobacter Cysteine-rich Protein C, PDB code 1OUV) yields RMSDs below 1 Å, confirming that the isolated repeats are indeed similar.	RESULTS
+108	112	SLRs	structure_element	The superposition of isolated TPRs from Cdc23 (S. pombe, cell division cycle 23 homolog, PDB code 3ZN3) and SLRs from HcpC (Helicobacter Cysteine-rich Protein C, PDB code 1OUV) yields RMSDs below 1 Å, confirming that the isolated repeats are indeed similar.	RESULTS
+118	122	HcpC	protein	The superposition of isolated TPRs from Cdc23 (S. pombe, cell division cycle 23 homolog, PDB code 3ZN3) and SLRs from HcpC (Helicobacter Cysteine-rich Protein C, PDB code 1OUV) yields RMSDs below 1 Å, confirming that the isolated repeats are indeed similar.	RESULTS
+124	160	Helicobacter Cysteine-rich Protein C	protein	The superposition of isolated TPRs from Cdc23 (S. pombe, cell division cycle 23 homolog, PDB code 3ZN3) and SLRs from HcpC (Helicobacter Cysteine-rich Protein C, PDB code 1OUV) yields RMSDs below 1 Å, confirming that the isolated repeats are indeed similar.	RESULTS
+184	189	RMSDs	evidence	The superposition of isolated TPRs from Cdc23 (S. pombe, cell division cycle 23 homolog, PDB code 3ZN3) and SLRs from HcpC (Helicobacter Cysteine-rich Protein C, PDB code 1OUV) yields RMSDs below 1 Å, confirming that the isolated repeats are indeed similar.	RESULTS
+20	23	SLR	structure_element	This is relevant to SLR motifs in SEL1L, as isolated SLR motifs from SEL1Lcent showed good structural alignment with isolated TPRs (RMSD 1.6 Å for all Cα chains) from Cdc23N-term and SLRs (RMSD 0.6 Å for all Cα chains) from HcpC (Fig. 5A).	RESULTS
+34	39	SEL1L	protein	This is relevant to SLR motifs in SEL1L, as isolated SLR motifs from SEL1Lcent showed good structural alignment with isolated TPRs (RMSD 1.6 Å for all Cα chains) from Cdc23N-term and SLRs (RMSD 0.6 Å for all Cα chains) from HcpC (Fig. 5A).	RESULTS
+53	56	SLR	structure_element	This is relevant to SLR motifs in SEL1L, as isolated SLR motifs from SEL1Lcent showed good structural alignment with isolated TPRs (RMSD 1.6 Å for all Cα chains) from Cdc23N-term and SLRs (RMSD 0.6 Å for all Cα chains) from HcpC (Fig. 5A).	RESULTS
+69	78	SEL1Lcent	structure_element	This is relevant to SLR motifs in SEL1L, as isolated SLR motifs from SEL1Lcent showed good structural alignment with isolated TPRs (RMSD 1.6 Å for all Cα chains) from Cdc23N-term and SLRs (RMSD 0.6 Å for all Cα chains) from HcpC (Fig. 5A).	RESULTS
+91	111	structural alignment	experimental_method	This is relevant to SLR motifs in SEL1L, as isolated SLR motifs from SEL1Lcent showed good structural alignment with isolated TPRs (RMSD 1.6 Å for all Cα chains) from Cdc23N-term and SLRs (RMSD 0.6 Å for all Cα chains) from HcpC (Fig. 5A).	RESULTS
+126	130	TPRs	structure_element	This is relevant to SLR motifs in SEL1L, as isolated SLR motifs from SEL1Lcent showed good structural alignment with isolated TPRs (RMSD 1.6 Å for all Cα chains) from Cdc23N-term and SLRs (RMSD 0.6 Å for all Cα chains) from HcpC (Fig. 5A).	RESULTS
+132	136	RMSD	evidence	This is relevant to SLR motifs in SEL1L, as isolated SLR motifs from SEL1Lcent showed good structural alignment with isolated TPRs (RMSD 1.6 Å for all Cα chains) from Cdc23N-term and SLRs (RMSD 0.6 Å for all Cα chains) from HcpC (Fig. 5A).	RESULTS
+167	172	Cdc23	protein	This is relevant to SLR motifs in SEL1L, as isolated SLR motifs from SEL1Lcent showed good structural alignment with isolated TPRs (RMSD 1.6 Å for all Cα chains) from Cdc23N-term and SLRs (RMSD 0.6 Å for all Cα chains) from HcpC (Fig. 5A).	RESULTS
+183	187	SLRs	structure_element	This is relevant to SLR motifs in SEL1L, as isolated SLR motifs from SEL1Lcent showed good structural alignment with isolated TPRs (RMSD 1.6 Å for all Cα chains) from Cdc23N-term and SLRs (RMSD 0.6 Å for all Cα chains) from HcpC (Fig. 5A).	RESULTS
+189	193	RMSD	evidence	This is relevant to SLR motifs in SEL1L, as isolated SLR motifs from SEL1Lcent showed good structural alignment with isolated TPRs (RMSD 1.6 Å for all Cα chains) from Cdc23N-term and SLRs (RMSD 0.6 Å for all Cα chains) from HcpC (Fig. 5A).	RESULTS
+224	228	HcpC	protein	This is relevant to SLR motifs in SEL1L, as isolated SLR motifs from SEL1Lcent showed good structural alignment with isolated TPRs (RMSD 1.6 Å for all Cα chains) from Cdc23N-term and SLRs (RMSD 0.6 Å for all Cα chains) from HcpC (Fig. 5A).	RESULTS
+9	22	superimposing	experimental_method	However, superimposing the structure of SLR motifs 5 to 9 from SEL1Lcent onto the overall Cdc23N-term or full-length HcpC structures revealed that SLR motifs 5 to 9 in SEL1Lcent have a different superhelical structure than either Cdc23 or HcpC (RMSD values of >2.5 Å for Cα atoms) (Fig. 5B).	RESULTS
+27	36	structure	evidence	However, superimposing the structure of SLR motifs 5 to 9 from SEL1Lcent onto the overall Cdc23N-term or full-length HcpC structures revealed that SLR motifs 5 to 9 in SEL1Lcent have a different superhelical structure than either Cdc23 or HcpC (RMSD values of >2.5 Å for Cα atoms) (Fig. 5B).	RESULTS
+40	57	SLR motifs 5 to 9	structure_element	However, superimposing the structure of SLR motifs 5 to 9 from SEL1Lcent onto the overall Cdc23N-term or full-length HcpC structures revealed that SLR motifs 5 to 9 in SEL1Lcent have a different superhelical structure than either Cdc23 or HcpC (RMSD values of >2.5 Å for Cα atoms) (Fig. 5B).	RESULTS
+63	72	SEL1Lcent	structure_element	However, superimposing the structure of SLR motifs 5 to 9 from SEL1Lcent onto the overall Cdc23N-term or full-length HcpC structures revealed that SLR motifs 5 to 9 in SEL1Lcent have a different superhelical structure than either Cdc23 or HcpC (RMSD values of >2.5 Å for Cα atoms) (Fig. 5B).	RESULTS
+90	95	Cdc23	protein	However, superimposing the structure of SLR motifs 5 to 9 from SEL1Lcent onto the overall Cdc23N-term or full-length HcpC structures revealed that SLR motifs 5 to 9 in SEL1Lcent have a different superhelical structure than either Cdc23 or HcpC (RMSD values of >2.5 Å for Cα atoms) (Fig. 5B).	RESULTS
+105	116	full-length	protein_state	However, superimposing the structure of SLR motifs 5 to 9 from SEL1Lcent onto the overall Cdc23N-term or full-length HcpC structures revealed that SLR motifs 5 to 9 in SEL1Lcent have a different superhelical structure than either Cdc23 or HcpC (RMSD values of >2.5 Å for Cα atoms) (Fig. 5B).	RESULTS
+117	121	HcpC	protein	However, superimposing the structure of SLR motifs 5 to 9 from SEL1Lcent onto the overall Cdc23N-term or full-length HcpC structures revealed that SLR motifs 5 to 9 in SEL1Lcent have a different superhelical structure than either Cdc23 or HcpC (RMSD values of >2.5 Å for Cα atoms) (Fig. 5B).	RESULTS
+122	132	structures	evidence	However, superimposing the structure of SLR motifs 5 to 9 from SEL1Lcent onto the overall Cdc23N-term or full-length HcpC structures revealed that SLR motifs 5 to 9 in SEL1Lcent have a different superhelical structure than either Cdc23 or HcpC (RMSD values of >2.5 Å for Cα atoms) (Fig. 5B).	RESULTS
+147	164	SLR motifs 5 to 9	structure_element	However, superimposing the structure of SLR motifs 5 to 9 from SEL1Lcent onto the overall Cdc23N-term or full-length HcpC structures revealed that SLR motifs 5 to 9 in SEL1Lcent have a different superhelical structure than either Cdc23 or HcpC (RMSD values of >2.5 Å for Cα atoms) (Fig. 5B).	RESULTS
+168	177	SEL1Lcent	structure_element	However, superimposing the structure of SLR motifs 5 to 9 from SEL1Lcent onto the overall Cdc23N-term or full-length HcpC structures revealed that SLR motifs 5 to 9 in SEL1Lcent have a different superhelical structure than either Cdc23 or HcpC (RMSD values of >2.5 Å for Cα atoms) (Fig. 5B).	RESULTS
+230	235	Cdc23	protein	However, superimposing the structure of SLR motifs 5 to 9 from SEL1Lcent onto the overall Cdc23N-term or full-length HcpC structures revealed that SLR motifs 5 to 9 in SEL1Lcent have a different superhelical structure than either Cdc23 or HcpC (RMSD values of >2.5 Å for Cα atoms) (Fig. 5B).	RESULTS
+239	243	HcpC	protein	However, superimposing the structure of SLR motifs 5 to 9 from SEL1Lcent onto the overall Cdc23N-term or full-length HcpC structures revealed that SLR motifs 5 to 9 in SEL1Lcent have a different superhelical structure than either Cdc23 or HcpC (RMSD values of >2.5 Å for Cα atoms) (Fig. 5B).	RESULTS
+245	249	RMSD	evidence	However, superimposing the structure of SLR motifs 5 to 9 from SEL1Lcent onto the overall Cdc23N-term or full-length HcpC structures revealed that SLR motifs 5 to 9 in SEL1Lcent have a different superhelical structure than either Cdc23 or HcpC (RMSD values of >2.5 Å for Cα atoms) (Fig. 5B).	RESULTS
+73	78	loops	structure_element	The differences may result from the differing numbers of residues in the loops and differences in antiparallel helix packing.	RESULTS
+98	116	antiparallel helix	structure_element	The differences may result from the differing numbers of residues in the loops and differences in antiparallel helix packing.	RESULTS
+20	29	conserved	protein_state	Moreover, there are conserved disulfide bonds in the SLR motifs of HcpC and HcpB, but no such bonds are observed in SEL1Lcent.	RESULTS
+30	45	disulfide bonds	ptm	Moreover, there are conserved disulfide bonds in the SLR motifs of HcpC and HcpB, but no such bonds are observed in SEL1Lcent.	RESULTS
+53	56	SLR	structure_element	Moreover, there are conserved disulfide bonds in the SLR motifs of HcpC and HcpB, but no such bonds are observed in SEL1Lcent.	RESULTS
+67	71	HcpC	protein	Moreover, there are conserved disulfide bonds in the SLR motifs of HcpC and HcpB, but no such bonds are observed in SEL1Lcent.	RESULTS
+76	80	HcpB	protein	Moreover, there are conserved disulfide bonds in the SLR motifs of HcpC and HcpB, but no such bonds are observed in SEL1Lcent.	RESULTS
+116	125	SEL1Lcent	structure_element	Moreover, there are conserved disulfide bonds in the SLR motifs of HcpC and HcpB, but no such bonds are observed in SEL1Lcent.	RESULTS
+79	82	SLR	structure_element	These factors contribute to the differences in the overall conformation of the SLR motifs in SEL1L and other SLR or TPR motif-containing proteins.	RESULTS
+93	98	SEL1L	protein	These factors contribute to the differences in the overall conformation of the SLR motifs in SEL1L and other SLR or TPR motif-containing proteins.	RESULTS
+109	145	SLR or TPR motif-containing proteins	protein_type	These factors contribute to the differences in the overall conformation of the SLR motifs in SEL1L and other SLR or TPR motif-containing proteins.	RESULTS
+32	41	structure	evidence	Another major difference in the structure of SLR motifs between SEL1L and HcpC is the oligomeric state of proteins.	RESULTS
+45	48	SLR	structure_element	Another major difference in the structure of SLR motifs between SEL1L and HcpC is the oligomeric state of proteins.	RESULTS
+64	69	SEL1L	protein	Another major difference in the structure of SLR motifs between SEL1L and HcpC is the oligomeric state of proteins.	RESULTS
+74	78	HcpC	protein	Another major difference in the structure of SLR motifs between SEL1L and HcpC is the oligomeric state of proteins.	RESULTS
+4	7	TPR	structure_element	The TPR motif is involved in the dimerization of proteins such as Cdc23, Cdc16, and Cdc27.	RESULTS
+33	45	dimerization	oligomeric_state	The TPR motif is involved in the dimerization of proteins such as Cdc23, Cdc16, and Cdc27.	RESULTS
+66	71	Cdc23	protein	The TPR motif is involved in the dimerization of proteins such as Cdc23, Cdc16, and Cdc27.	RESULTS
+73	78	Cdc16	protein	The TPR motif is involved in the dimerization of proteins such as Cdc23, Cdc16, and Cdc27.	RESULTS
+84	89	Cdc27	protein	The TPR motif is involved in the dimerization of proteins such as Cdc23, Cdc16, and Cdc27.	RESULTS
+40	45	Cdc23	protein	In particular, the N-terminal domain of Cdc23 (Cdc23N-term) has a TPR-motif organization similar to that of the SLR motif in SEL1Lcent.	RESULTS
+47	52	Cdc23	protein	In particular, the N-terminal domain of Cdc23 (Cdc23N-term) has a TPR-motif organization similar to that of the SLR motif in SEL1Lcent.	RESULTS
+66	69	TPR	structure_element	In particular, the N-terminal domain of Cdc23 (Cdc23N-term) has a TPR-motif organization similar to that of the SLR motif in SEL1Lcent.	RESULTS
+112	115	SLR	structure_element	In particular, the N-terminal domain of Cdc23 (Cdc23N-term) has a TPR-motif organization similar to that of the SLR motif in SEL1Lcent.	RESULTS
+125	134	SEL1Lcent	structure_element	In particular, the N-terminal domain of Cdc23 (Cdc23N-term) has a TPR-motif organization similar to that of the SLR motif in SEL1Lcent.	RESULTS
+10	13	TPR	structure_element	The seven TPR motifs of Cdc23N-term are assembled into a superhelical structure, generating a hollow surface and encircling its dimer counterpart in an interlocking clasp-like arrangement (Fig. 5C).	RESULTS
+24	29	Cdc23	protein	The seven TPR motifs of Cdc23N-term are assembled into a superhelical structure, generating a hollow surface and encircling its dimer counterpart in an interlocking clasp-like arrangement (Fig. 5C).	RESULTS
+57	79	superhelical structure	structure_element	The seven TPR motifs of Cdc23N-term are assembled into a superhelical structure, generating a hollow surface and encircling its dimer counterpart in an interlocking clasp-like arrangement (Fig. 5C).	RESULTS
+128	133	dimer	oligomeric_state	The seven TPR motifs of Cdc23N-term are assembled into a superhelical structure, generating a hollow surface and encircling its dimer counterpart in an interlocking clasp-like arrangement (Fig. 5C).	RESULTS
+4	15	TPR motif 1	structure_element	The TPR motif 1 (TPR1) of each Cdc23N-term subunit is located in the hollow surface of the counter subunit and interacts with residues lining the inner groove TPR α-helices, generating two-fold symmetry homotype interactions.	RESULTS
+17	21	TPR1	structure_element	The TPR motif 1 (TPR1) of each Cdc23N-term subunit is located in the hollow surface of the counter subunit and interacts with residues lining the inner groove TPR α-helices, generating two-fold symmetry homotype interactions.	RESULTS
+31	36	Cdc23	protein	The TPR motif 1 (TPR1) of each Cdc23N-term subunit is located in the hollow surface of the counter subunit and interacts with residues lining the inner groove TPR α-helices, generating two-fold symmetry homotype interactions.	RESULTS
+146	158	inner groove	site	The TPR motif 1 (TPR1) of each Cdc23N-term subunit is located in the hollow surface of the counter subunit and interacts with residues lining the inner groove TPR α-helices, generating two-fold symmetry homotype interactions.	RESULTS
+159	162	TPR	structure_element	The TPR motif 1 (TPR1) of each Cdc23N-term subunit is located in the hollow surface of the counter subunit and interacts with residues lining the inner groove TPR α-helices, generating two-fold symmetry homotype interactions.	RESULTS
+163	172	α-helices	structure_element	The TPR motif 1 (TPR1) of each Cdc23N-term subunit is located in the hollow surface of the counter subunit and interacts with residues lining the inner groove TPR α-helices, generating two-fold symmetry homotype interactions.	RESULTS
+17	26	structure	evidence	However, in this structure, a conformational change in the TPR motif itself is not observed.	RESULTS
+59	62	TPR	structure_element	However, in this structure, a conformational change in the TPR motif itself is not observed.	RESULTS
+20	24	HcpC	protein	Self-association of HcpC has not been reported, and there is no domain-swapped structure in the SLR motifs of HcpC, in contrast to that observed in SEL1Lcent.	RESULTS
+64	78	domain-swapped	protein_state	Self-association of HcpC has not been reported, and there is no domain-swapped structure in the SLR motifs of HcpC, in contrast to that observed in SEL1Lcent.	RESULTS
+96	99	SLR	structure_element	Self-association of HcpC has not been reported, and there is no domain-swapped structure in the SLR motifs of HcpC, in contrast to that observed in SEL1Lcent.	RESULTS
+110	114	HcpC	protein	Self-association of HcpC has not been reported, and there is no domain-swapped structure in the SLR motifs of HcpC, in contrast to that observed in SEL1Lcent.	RESULTS
+148	157	SEL1Lcent	structure_element	Self-association of HcpC has not been reported, and there is no domain-swapped structure in the SLR motifs of HcpC, in contrast to that observed in SEL1Lcent.	RESULTS
+9	14	SEL1L	protein	Although SEL1L contains a number of SLR motifs comparable to HcpC, the SLR motifs in SEL1L are interrupted by other sequences, making three SLR motif clusters (Fig. 1A).	RESULTS
+36	39	SLR	structure_element	Although SEL1L contains a number of SLR motifs comparable to HcpC, the SLR motifs in SEL1L are interrupted by other sequences, making three SLR motif clusters (Fig. 1A).	RESULTS
+61	65	HcpC	protein	Although SEL1L contains a number of SLR motifs comparable to HcpC, the SLR motifs in SEL1L are interrupted by other sequences, making three SLR motif clusters (Fig. 1A).	RESULTS
+71	74	SLR	structure_element	Although SEL1L contains a number of SLR motifs comparable to HcpC, the SLR motifs in SEL1L are interrupted by other sequences, making three SLR motif clusters (Fig. 1A).	RESULTS
+85	90	SEL1L	protein	Although SEL1L contains a number of SLR motifs comparable to HcpC, the SLR motifs in SEL1L are interrupted by other sequences, making three SLR motif clusters (Fig. 1A).	RESULTS
+140	143	SLR	structure_element	Although SEL1L contains a number of SLR motifs comparable to HcpC, the SLR motifs in SEL1L are interrupted by other sequences, making three SLR motif clusters (Fig. 1A).	RESULTS
+16	19	SLR	structure_element	The interrupted SLR motifs may be required for dimerization of SEL1Lcent, as five SLR motifs are more than enough to form the semicircle of the yin-yang symbol (Fig. 1B).	RESULTS
+47	59	dimerization	oligomeric_state	The interrupted SLR motifs may be required for dimerization of SEL1Lcent, as five SLR motifs are more than enough to form the semicircle of the yin-yang symbol (Fig. 1B).	RESULTS
+63	72	SEL1Lcent	structure_element	The interrupted SLR motifs may be required for dimerization of SEL1Lcent, as five SLR motifs are more than enough to form the semicircle of the yin-yang symbol (Fig. 1B).	RESULTS
+82	85	SLR	structure_element	The interrupted SLR motifs may be required for dimerization of SEL1Lcent, as five SLR motifs are more than enough to form the semicircle of the yin-yang symbol (Fig. 1B).	RESULTS
+126	152	semicircle of the yin-yang	structure_element	The interrupted SLR motifs may be required for dimerization of SEL1Lcent, as five SLR motifs are more than enough to form the semicircle of the yin-yang symbol (Fig. 1B).	RESULTS
+0	8	Helix 5A	structure_element	Helix 5A from SLR motif 5 meets helix 9A from SLR motif 9 of the counterpart SEL1L.	RESULTS
+14	25	SLR motif 5	structure_element	Helix 5A from SLR motif 5 meets helix 9A from SLR motif 9 of the counterpart SEL1L.	RESULTS
+32	40	helix 9A	structure_element	Helix 5A from SLR motif 5 meets helix 9A from SLR motif 9 of the counterpart SEL1L.	RESULTS
+46	57	SLR motif 9	structure_element	Helix 5A from SLR motif 5 meets helix 9A from SLR motif 9 of the counterpart SEL1L.	RESULTS
+77	82	SEL1L	protein	Helix 5A from SLR motif 5 meets helix 9A from SLR motif 9 of the counterpart SEL1L.	RESULTS
+7	24	SLR motifs 5 to 9	structure_element	If the SLR motifs 5 to 9 were not isolated from other SLR motifs, steric hindrance could interfere with dimerization of SEL1L.	RESULTS
+54	57	SLR	structure_element	If the SLR motifs 5 to 9 were not isolated from other SLR motifs, steric hindrance could interfere with dimerization of SEL1L.	RESULTS
+104	116	dimerization	oligomeric_state	If the SLR motifs 5 to 9 were not isolated from other SLR motifs, steric hindrance could interfere with dimerization of SEL1L.	RESULTS
+120	125	SEL1L	protein	If the SLR motifs 5 to 9 were not isolated from other SLR motifs, steric hindrance could interfere with dimerization of SEL1L.	RESULTS
+44	48	TPRs	structure_element	This is one of the biggest differences from TPRs in Cdc23 and from the SLRs in HcpC, where the motifs exist in tandem.	RESULTS
+52	57	Cdc23	protein	This is one of the biggest differences from TPRs in Cdc23 and from the SLRs in HcpC, where the motifs exist in tandem.	RESULTS
+71	75	SLRs	structure_element	This is one of the biggest differences from TPRs in Cdc23 and from the SLRs in HcpC, where the motifs exist in tandem.	RESULTS
+79	83	HcpC	protein	This is one of the biggest differences from TPRs in Cdc23 and from the SLRs in HcpC, where the motifs exist in tandem.	RESULTS
+0	3	TPR	structure_element	TPR and SLR motifs are generally involved in protein-protein interaction modules, and the sequences between the SLR motifs of SEL1L might actually facilitate the self-association of this protein.	RESULTS
+8	11	SLR	structure_element	TPR and SLR motifs are generally involved in protein-protein interaction modules, and the sequences between the SLR motifs of SEL1L might actually facilitate the self-association of this protein.	RESULTS
+112	115	SLR	structure_element	TPR and SLR motifs are generally involved in protein-protein interaction modules, and the sequences between the SLR motifs of SEL1L might actually facilitate the self-association of this protein.	RESULTS
+126	131	SEL1L	protein	TPR and SLR motifs are generally involved in protein-protein interaction modules, and the sequences between the SLR motifs of SEL1L might actually facilitate the self-association of this protein.	RESULTS
+0	5	SLR-C	structure_element	SLR-C of SEL1L Binds HRD1 N-terminus Luminal Loop	RESULTS
+9	14	SEL1L	protein	SLR-C of SEL1L Binds HRD1 N-terminus Luminal Loop	RESULTS
+21	25	HRD1	protein	SLR-C of SEL1L Binds HRD1 N-terminus Luminal Loop	RESULTS
+37	49	Luminal Loop	structure_element	SLR-C of SEL1L Binds HRD1 N-terminus Luminal Loop	RESULTS
+13	28	structural data	evidence	Based on the structural data presented herein, a possible arrangement of membrane-associated ERAD components in mammals, highlighting the molecular functions of SLR domains in SEL1L, is shown in Fig. 6C.	RESULTS
+112	119	mammals	taxonomy_domain	Based on the structural data presented herein, a possible arrangement of membrane-associated ERAD components in mammals, highlighting the molecular functions of SLR domains in SEL1L, is shown in Fig. 6C.	RESULTS
+161	164	SLR	structure_element	Based on the structural data presented herein, a possible arrangement of membrane-associated ERAD components in mammals, highlighting the molecular functions of SLR domains in SEL1L, is shown in Fig. 6C.	RESULTS
+176	181	SEL1L	protein	Based on the structural data presented herein, a possible arrangement of membrane-associated ERAD components in mammals, highlighting the molecular functions of SLR domains in SEL1L, is shown in Fig. 6C.	RESULTS
+27	30	SLR	structure_element	We suggest that the middle SLR domains are involved in the dimerization of SEL1L based on the crystal structure and biochemical data.	RESULTS
+59	71	dimerization	oligomeric_state	We suggest that the middle SLR domains are involved in the dimerization of SEL1L based on the crystal structure and biochemical data.	RESULTS
+75	80	SEL1L	protein	We suggest that the middle SLR domains are involved in the dimerization of SEL1L based on the crystal structure and biochemical data.	RESULTS
+94	111	crystal structure	evidence	We suggest that the middle SLR domains are involved in the dimerization of SEL1L based on the crystal structure and biochemical data.	RESULTS
+0	5	SLR-C	structure_element	SLR-C, which contains SLR motifs 10 to 11, might be involved in the interaction with HRD1.	RESULTS
+22	41	SLR motifs 10 to 11	structure_element	SLR-C, which contains SLR motifs 10 to 11, might be involved in the interaction with HRD1.	RESULTS
+85	89	HRD1	protein	SLR-C, which contains SLR motifs 10 to 11, might be involved in the interaction with HRD1.	RESULTS
+34	39	yeast	taxonomy_domain	Indirect evidence from a previous yeast study shows that the circumscribed region of C-terminal Hrd3p, specifically residues 664–695, forms contacts with the Hrd1 luminal loops.	RESULTS
+96	101	Hrd3p	protein	Indirect evidence from a previous yeast study shows that the circumscribed region of C-terminal Hrd3p, specifically residues 664–695, forms contacts with the Hrd1 luminal loops.	RESULTS
+125	132	664–695	residue_range	Indirect evidence from a previous yeast study shows that the circumscribed region of C-terminal Hrd3p, specifically residues 664–695, forms contacts with the Hrd1 luminal loops.	RESULTS
+158	162	Hrd1	protein	Indirect evidence from a previous yeast study shows that the circumscribed region of C-terminal Hrd3p, specifically residues 664–695, forms contacts with the Hrd1 luminal loops.	RESULTS
+163	176	luminal loops	structure_element	Indirect evidence from a previous yeast study shows that the circumscribed region of C-terminal Hrd3p, specifically residues 664–695, forms contacts with the Hrd1 luminal loops.	RESULTS
+4	9	Hrd3p	protein	The Hrd3p residues 664–695 correspond to mouse SEL1L residues 696–727, which include the entire helix 11B (residue 697–709) of SLR motif 11 and a well-conserved adjacent region (Supplementary Fig. 4).	RESULTS
+19	26	664–695	residue_range	The Hrd3p residues 664–695 correspond to mouse SEL1L residues 696–727, which include the entire helix 11B (residue 697–709) of SLR motif 11 and a well-conserved adjacent region (Supplementary Fig. 4).	RESULTS
+41	46	mouse	taxonomy_domain	The Hrd3p residues 664–695 correspond to mouse SEL1L residues 696–727, which include the entire helix 11B (residue 697–709) of SLR motif 11 and a well-conserved adjacent region (Supplementary Fig. 4).	RESULTS
+47	52	SEL1L	protein	The Hrd3p residues 664–695 correspond to mouse SEL1L residues 696–727, which include the entire helix 11B (residue 697–709) of SLR motif 11 and a well-conserved adjacent region (Supplementary Fig. 4).	RESULTS
+62	69	696–727	residue_range	The Hrd3p residues 664–695 correspond to mouse SEL1L residues 696–727, which include the entire helix 11B (residue 697–709) of SLR motif 11 and a well-conserved adjacent region (Supplementary Fig. 4).	RESULTS
+96	105	helix 11B	structure_element	The Hrd3p residues 664–695 correspond to mouse SEL1L residues 696–727, which include the entire helix 11B (residue 697–709) of SLR motif 11 and a well-conserved adjacent region (Supplementary Fig. 4).	RESULTS
+115	122	697–709	residue_range	The Hrd3p residues 664–695 correspond to mouse SEL1L residues 696–727, which include the entire helix 11B (residue 697–709) of SLR motif 11 and a well-conserved adjacent region (Supplementary Fig. 4).	RESULTS
+127	139	SLR motif 11	structure_element	The Hrd3p residues 664–695 correspond to mouse SEL1L residues 696–727, which include the entire helix 11B (residue 697–709) of SLR motif 11 and a well-conserved adjacent region (Supplementary Fig. 4).	RESULTS
+146	160	well-conserved	protein_state	The Hrd3p residues 664–695 correspond to mouse SEL1L residues 696–727, which include the entire helix 11B (residue 697–709) of SLR motif 11 and a well-conserved adjacent region (Supplementary Fig. 4).	RESULTS
+76	94	SLR motif 10 to 11	structure_element	This observation is supported by the following: (1) the meticulous range of SLR motif 10 to 11 is newly established from a structure-guided SLR motif alignment, based on the present structure study, and (2) the relatively high sequence conservation between mammalian SEL1L and yeast Hrd3p around SLR motifs 10 to 11, which contain contact regions with HRD1 (Hrd1p) (Supplementary Figs. 4 and 5).	RESULTS
+123	159	structure-guided SLR motif alignment	experimental_method	This observation is supported by the following: (1) the meticulous range of SLR motif 10 to 11 is newly established from a structure-guided SLR motif alignment, based on the present structure study, and (2) the relatively high sequence conservation between mammalian SEL1L and yeast Hrd3p around SLR motifs 10 to 11, which contain contact regions with HRD1 (Hrd1p) (Supplementary Figs. 4 and 5).	RESULTS
+182	197	structure study	experimental_method	This observation is supported by the following: (1) the meticulous range of SLR motif 10 to 11 is newly established from a structure-guided SLR motif alignment, based on the present structure study, and (2) the relatively high sequence conservation between mammalian SEL1L and yeast Hrd3p around SLR motifs 10 to 11, which contain contact regions with HRD1 (Hrd1p) (Supplementary Figs. 4 and 5).	RESULTS
+227	248	sequence conservation	protein_state	This observation is supported by the following: (1) the meticulous range of SLR motif 10 to 11 is newly established from a structure-guided SLR motif alignment, based on the present structure study, and (2) the relatively high sequence conservation between mammalian SEL1L and yeast Hrd3p around SLR motifs 10 to 11, which contain contact regions with HRD1 (Hrd1p) (Supplementary Figs. 4 and 5).	RESULTS
+257	266	mammalian	taxonomy_domain	This observation is supported by the following: (1) the meticulous range of SLR motif 10 to 11 is newly established from a structure-guided SLR motif alignment, based on the present structure study, and (2) the relatively high sequence conservation between mammalian SEL1L and yeast Hrd3p around SLR motifs 10 to 11, which contain contact regions with HRD1 (Hrd1p) (Supplementary Figs. 4 and 5).	RESULTS
+267	272	SEL1L	protein	This observation is supported by the following: (1) the meticulous range of SLR motif 10 to 11 is newly established from a structure-guided SLR motif alignment, based on the present structure study, and (2) the relatively high sequence conservation between mammalian SEL1L and yeast Hrd3p around SLR motifs 10 to 11, which contain contact regions with HRD1 (Hrd1p) (Supplementary Figs. 4 and 5).	RESULTS
+277	282	yeast	taxonomy_domain	This observation is supported by the following: (1) the meticulous range of SLR motif 10 to 11 is newly established from a structure-guided SLR motif alignment, based on the present structure study, and (2) the relatively high sequence conservation between mammalian SEL1L and yeast Hrd3p around SLR motifs 10 to 11, which contain contact regions with HRD1 (Hrd1p) (Supplementary Figs. 4 and 5).	RESULTS
+283	288	Hrd3p	protein	This observation is supported by the following: (1) the meticulous range of SLR motif 10 to 11 is newly established from a structure-guided SLR motif alignment, based on the present structure study, and (2) the relatively high sequence conservation between mammalian SEL1L and yeast Hrd3p around SLR motifs 10 to 11, which contain contact regions with HRD1 (Hrd1p) (Supplementary Figs. 4 and 5).	RESULTS
+296	315	SLR motifs 10 to 11	structure_element	This observation is supported by the following: (1) the meticulous range of SLR motif 10 to 11 is newly established from a structure-guided SLR motif alignment, based on the present structure study, and (2) the relatively high sequence conservation between mammalian SEL1L and yeast Hrd3p around SLR motifs 10 to 11, which contain contact regions with HRD1 (Hrd1p) (Supplementary Figs. 4 and 5).	RESULTS
+352	356	HRD1	protein	This observation is supported by the following: (1) the meticulous range of SLR motif 10 to 11 is newly established from a structure-guided SLR motif alignment, based on the present structure study, and (2) the relatively high sequence conservation between mammalian SEL1L and yeast Hrd3p around SLR motifs 10 to 11, which contain contact regions with HRD1 (Hrd1p) (Supplementary Figs. 4 and 5).	RESULTS
+358	363	Hrd1p	protein	This observation is supported by the following: (1) the meticulous range of SLR motif 10 to 11 is newly established from a structure-guided SLR motif alignment, based on the present structure study, and (2) the relatively high sequence conservation between mammalian SEL1L and yeast Hrd3p around SLR motifs 10 to 11, which contain contact regions with HRD1 (Hrd1p) (Supplementary Figs. 4 and 5).	RESULTS
+60	65	mouse	taxonomy_domain	To address this hypothesis, we prepared constructs encoding mouse HRD1 luminal fragments fused to GST as shown in Fig. 6A, and tested their ability to bind certain SLR motifs in SEL1L.	RESULTS
+66	70	HRD1	protein	To address this hypothesis, we prepared constructs encoding mouse HRD1 luminal fragments fused to GST as shown in Fig. 6A, and tested their ability to bind certain SLR motifs in SEL1L.	RESULTS
+89	101	fused to GST	experimental_method	To address this hypothesis, we prepared constructs encoding mouse HRD1 luminal fragments fused to GST as shown in Fig. 6A, and tested their ability to bind certain SLR motifs in SEL1L.	RESULTS
+164	167	SLR	structure_element	To address this hypothesis, we prepared constructs encoding mouse HRD1 luminal fragments fused to GST as shown in Fig. 6A, and tested their ability to bind certain SLR motifs in SEL1L.	RESULTS
+178	183	SEL1L	protein	To address this hypothesis, we prepared constructs encoding mouse HRD1 luminal fragments fused to GST as shown in Fig. 6A, and tested their ability to bind certain SLR motifs in SEL1L.	RESULTS
+94	99	SLR-N	structure_element	The fusion proteins were immobilized on glutathione-Sepharose beads and probed for binding to SLR-N, SLR-M, SLR-C, and monomer form of SLR-M (SLR-ML521A).	RESULTS
+101	106	SLR-M	structure_element	The fusion proteins were immobilized on glutathione-Sepharose beads and probed for binding to SLR-N, SLR-M, SLR-C, and monomer form of SLR-M (SLR-ML521A).	RESULTS
+108	113	SLR-C	structure_element	The fusion proteins were immobilized on glutathione-Sepharose beads and probed for binding to SLR-N, SLR-M, SLR-C, and monomer form of SLR-M (SLR-ML521A).	RESULTS
+119	126	monomer	oligomeric_state	The fusion proteins were immobilized on glutathione-Sepharose beads and probed for binding to SLR-N, SLR-M, SLR-C, and monomer form of SLR-M (SLR-ML521A).	RESULTS
+135	140	SLR-M	structure_element	The fusion proteins were immobilized on glutathione-Sepharose beads and probed for binding to SLR-N, SLR-M, SLR-C, and monomer form of SLR-M (SLR-ML521A).	RESULTS
+142	152	SLR-ML521A	mutant	The fusion proteins were immobilized on glutathione-Sepharose beads and probed for binding to SLR-N, SLR-M, SLR-C, and monomer form of SLR-M (SLR-ML521A).	RESULTS
+25	30	SLR-C	structure_element	Figure 6B shows that the SLR-C, consisting of SLR motifs 10 and 11, exclusively interacts with N-terminal luminal loop (residues 21–42) of HRD1.	RESULTS
+46	66	SLR motifs 10 and 11	structure_element	Figure 6B shows that the SLR-C, consisting of SLR motifs 10 and 11, exclusively interacts with N-terminal luminal loop (residues 21–42) of HRD1.	RESULTS
+106	118	luminal loop	structure_element	Figure 6B shows that the SLR-C, consisting of SLR motifs 10 and 11, exclusively interacts with N-terminal luminal loop (residues 21–42) of HRD1.	RESULTS
+129	134	21–42	residue_range	Figure 6B shows that the SLR-C, consisting of SLR motifs 10 and 11, exclusively interacts with N-terminal luminal loop (residues 21–42) of HRD1.	RESULTS
+139	143	HRD1	protein	Figure 6B shows that the SLR-C, consisting of SLR motifs 10 and 11, exclusively interacts with N-terminal luminal loop (residues 21–42) of HRD1.	RESULTS
+27	32	SLR-N	structure_element	The molecular functions of SLR-N are unclear.	RESULTS
+24	29	SLR-N	structure_element	One possibility is that SLR-N contributes to substrate recognition of proteins to be degraded because there are a couple of putative glycosylation sites within the SLR-N domain (Fig. 1A).	RESULTS
+133	152	glycosylation sites	site	One possibility is that SLR-N contributes to substrate recognition of proteins to be degraded because there are a couple of putative glycosylation sites within the SLR-N domain (Fig. 1A).	RESULTS
+164	169	SLR-N	structure_element	One possibility is that SLR-N contributes to substrate recognition of proteins to be degraded because there are a couple of putative glycosylation sites within the SLR-N domain (Fig. 1A).	RESULTS
+0	9	SEL1Lcent	structure_element	SEL1Lcent contains a putative N-glycosylation site, Asn 427, which is highly conserved among different species and structurally exposed to the surface of the SEL1L dimer according to the crystal structure (Fig. 6C).	RESULTS
+30	50	N-glycosylation site	site	SEL1Lcent contains a putative N-glycosylation site, Asn 427, which is highly conserved among different species and structurally exposed to the surface of the SEL1L dimer according to the crystal structure (Fig. 6C).	RESULTS
+52	59	Asn 427	residue_name_number	SEL1Lcent contains a putative N-glycosylation site, Asn 427, which is highly conserved among different species and structurally exposed to the surface of the SEL1L dimer according to the crystal structure (Fig. 6C).	RESULTS
+70	86	highly conserved	protein_state	SEL1Lcent contains a putative N-glycosylation site, Asn 427, which is highly conserved among different species and structurally exposed to the surface of the SEL1L dimer according to the crystal structure (Fig. 6C).	RESULTS
+158	163	SEL1L	protein	SEL1Lcent contains a putative N-glycosylation site, Asn 427, which is highly conserved among different species and structurally exposed to the surface of the SEL1L dimer according to the crystal structure (Fig. 6C).	RESULTS
+164	169	dimer	oligomeric_state	SEL1Lcent contains a putative N-glycosylation site, Asn 427, which is highly conserved among different species and structurally exposed to the surface of the SEL1L dimer according to the crystal structure (Fig. 6C).	RESULTS
+187	204	crystal structure	evidence	SEL1Lcent contains a putative N-glycosylation site, Asn 427, which is highly conserved among different species and structurally exposed to the surface of the SEL1L dimer according to the crystal structure (Fig. 6C).	RESULTS
+72	77	yeast	taxonomy_domain	Many reports demonstrate that membrane-bound ERAD machinery proteins in yeast, such as Hrd1p, Der1p, and Usa1p, are involved in oligomerization of ERAD components.	DISCUSS
+87	92	Hrd1p	protein	Many reports demonstrate that membrane-bound ERAD machinery proteins in yeast, such as Hrd1p, Der1p, and Usa1p, are involved in oligomerization of ERAD components.	DISCUSS
+94	99	Der1p	protein	Many reports demonstrate that membrane-bound ERAD machinery proteins in yeast, such as Hrd1p, Der1p, and Usa1p, are involved in oligomerization of ERAD components.	DISCUSS
+105	110	Usa1p	protein	Many reports demonstrate that membrane-bound ERAD machinery proteins in yeast, such as Hrd1p, Der1p, and Usa1p, are involved in oligomerization of ERAD components.	DISCUSS
+4	9	Hrd1p	protein	The Hrd1p complex forms dimers upon sucrose gradient sedimentation and size-exclusion chromatography.	DISCUSS
+24	30	dimers	oligomeric_state	The Hrd1p complex forms dimers upon sucrose gradient sedimentation and size-exclusion chromatography.	DISCUSS
+36	66	sucrose gradient sedimentation	experimental_method	The Hrd1p complex forms dimers upon sucrose gradient sedimentation and size-exclusion chromatography.	DISCUSS
+71	100	size-exclusion chromatography	experimental_method	The Hrd1p complex forms dimers upon sucrose gradient sedimentation and size-exclusion chromatography.	DISCUSS
+24	41	HA-epitope-tagged	protein_state	Previous data show that HA-epitope-tagged Hrd3p or Hrd1p efficiently co-precipitate with unmodified Hrd3p and Hrd1p, respectively, suggesting that both Hrd1p and Hrd3p homodimers are involved in self-association of the Hrd complex.	DISCUSS
+42	47	Hrd3p	protein	Previous data show that HA-epitope-tagged Hrd3p or Hrd1p efficiently co-precipitate with unmodified Hrd3p and Hrd1p, respectively, suggesting that both Hrd1p and Hrd3p homodimers are involved in self-association of the Hrd complex.	DISCUSS
+51	56	Hrd1p	protein	Previous data show that HA-epitope-tagged Hrd3p or Hrd1p efficiently co-precipitate with unmodified Hrd3p and Hrd1p, respectively, suggesting that both Hrd1p and Hrd3p homodimers are involved in self-association of the Hrd complex.	DISCUSS
+89	99	unmodified	protein_state	Previous data show that HA-epitope-tagged Hrd3p or Hrd1p efficiently co-precipitate with unmodified Hrd3p and Hrd1p, respectively, suggesting that both Hrd1p and Hrd3p homodimers are involved in self-association of the Hrd complex.	DISCUSS
+100	105	Hrd3p	protein	Previous data show that HA-epitope-tagged Hrd3p or Hrd1p efficiently co-precipitate with unmodified Hrd3p and Hrd1p, respectively, suggesting that both Hrd1p and Hrd3p homodimers are involved in self-association of the Hrd complex.	DISCUSS
+110	115	Hrd1p	protein	Previous data show that HA-epitope-tagged Hrd3p or Hrd1p efficiently co-precipitate with unmodified Hrd3p and Hrd1p, respectively, suggesting that both Hrd1p and Hrd3p homodimers are involved in self-association of the Hrd complex.	DISCUSS
+152	157	Hrd1p	protein	Previous data show that HA-epitope-tagged Hrd3p or Hrd1p efficiently co-precipitate with unmodified Hrd3p and Hrd1p, respectively, suggesting that both Hrd1p and Hrd3p homodimers are involved in self-association of the Hrd complex.	DISCUSS
+162	167	Hrd3p	protein	Previous data show that HA-epitope-tagged Hrd3p or Hrd1p efficiently co-precipitate with unmodified Hrd3p and Hrd1p, respectively, suggesting that both Hrd1p and Hrd3p homodimers are involved in self-association of the Hrd complex.	DISCUSS
+168	178	homodimers	oligomeric_state	Previous data show that HA-epitope-tagged Hrd3p or Hrd1p efficiently co-precipitate with unmodified Hrd3p and Hrd1p, respectively, suggesting that both Hrd1p and Hrd3p homodimers are involved in self-association of the Hrd complex.	DISCUSS
+219	222	Hrd	complex_assembly	Previous data show that HA-epitope-tagged Hrd3p or Hrd1p efficiently co-precipitate with unmodified Hrd3p and Hrd1p, respectively, suggesting that both Hrd1p and Hrd3p homodimers are involved in self-association of the Hrd complex.	DISCUSS
+100	105	yeast	taxonomy_domain	Considering that the functional and structural composition of ERAD components are conserved in both yeast and mammals, we propose that the mammalian ERAD components also form self-associating oligomers.	DISCUSS
+110	117	mammals	taxonomy_domain	Considering that the functional and structural composition of ERAD components are conserved in both yeast and mammals, we propose that the mammalian ERAD components also form self-associating oligomers.	DISCUSS
+139	148	mammalian	taxonomy_domain	Considering that the functional and structural composition of ERAD components are conserved in both yeast and mammals, we propose that the mammalian ERAD components also form self-associating oligomers.	DISCUSS
+192	201	oligomers	oligomeric_state	Considering that the functional and structural composition of ERAD components are conserved in both yeast and mammals, we propose that the mammalian ERAD components also form self-associating oligomers.	DISCUSS
+32	50	cross-linking data	experimental_method	This hypothesis is supported by cross-linking data suggesting that human HRD1 forms a homodimer.	DISCUSS
+67	72	human	species	This hypothesis is supported by cross-linking data suggesting that human HRD1 forms a homodimer.	DISCUSS
+73	77	HRD1	protein	This hypothesis is supported by cross-linking data suggesting that human HRD1 forms a homodimer.	DISCUSS
+86	95	homodimer	oligomeric_state	This hypothesis is supported by cross-linking data suggesting that human HRD1 forms a homodimer.	DISCUSS
+39	56	crystal structure	evidence	Consistent with the previous data, our crystal structure and biochemical data demonstrate that mouse SEL1Lcent exists as a homodimer in the ER lumen via domain swapping of SLR motif 9.	DISCUSS
+61	77	biochemical data	evidence	Consistent with the previous data, our crystal structure and biochemical data demonstrate that mouse SEL1Lcent exists as a homodimer in the ER lumen via domain swapping of SLR motif 9.	DISCUSS
+95	100	mouse	taxonomy_domain	Consistent with the previous data, our crystal structure and biochemical data demonstrate that mouse SEL1Lcent exists as a homodimer in the ER lumen via domain swapping of SLR motif 9.	DISCUSS
+101	110	SEL1Lcent	structure_element	Consistent with the previous data, our crystal structure and biochemical data demonstrate that mouse SEL1Lcent exists as a homodimer in the ER lumen via domain swapping of SLR motif 9.	DISCUSS
+123	132	homodimer	oligomeric_state	Consistent with the previous data, our crystal structure and biochemical data demonstrate that mouse SEL1Lcent exists as a homodimer in the ER lumen via domain swapping of SLR motif 9.	DISCUSS
+172	183	SLR motif 9	structure_element	Consistent with the previous data, our crystal structure and biochemical data demonstrate that mouse SEL1Lcent exists as a homodimer in the ER lumen via domain swapping of SLR motif 9.	DISCUSS
+63	68	dimer	oligomeric_state	We need to further test whether there are contacts involved in dimer formation in SEL1L in addition to those in the SLR-M region.	DISCUSS
+82	87	SEL1L	protein	We need to further test whether there are contacts involved in dimer formation in SEL1L in addition to those in the SLR-M region.	DISCUSS
+116	121	SLR-M	structure_element	We need to further test whether there are contacts involved in dimer formation in SEL1L in addition to those in the SLR-M region.	DISCUSS
+3	8	yeast	taxonomy_domain	In yeast, Usa1p acts as a scaffold for Hrd1p and Der1p, in which the N-terminus of Usa1p interacts with the C-terminal 34 amino acids of Hrd1p in the cytosol to induce oligomerization of Hrd1p, which is essential for its activity.	DISCUSS
+10	15	Usa1p	protein	In yeast, Usa1p acts as a scaffold for Hrd1p and Der1p, in which the N-terminus of Usa1p interacts with the C-terminal 34 amino acids of Hrd1p in the cytosol to induce oligomerization of Hrd1p, which is essential for its activity.	DISCUSS
+39	44	Hrd1p	protein	In yeast, Usa1p acts as a scaffold for Hrd1p and Der1p, in which the N-terminus of Usa1p interacts with the C-terminal 34 amino acids of Hrd1p in the cytosol to induce oligomerization of Hrd1p, which is essential for its activity.	DISCUSS
+49	54	Der1p	protein	In yeast, Usa1p acts as a scaffold for Hrd1p and Der1p, in which the N-terminus of Usa1p interacts with the C-terminal 34 amino acids of Hrd1p in the cytosol to induce oligomerization of Hrd1p, which is essential for its activity.	DISCUSS
+83	88	Usa1p	protein	In yeast, Usa1p acts as a scaffold for Hrd1p and Der1p, in which the N-terminus of Usa1p interacts with the C-terminal 34 amino acids of Hrd1p in the cytosol to induce oligomerization of Hrd1p, which is essential for its activity.	DISCUSS
+137	142	Hrd1p	protein	In yeast, Usa1p acts as a scaffold for Hrd1p and Der1p, in which the N-terminus of Usa1p interacts with the C-terminal 34 amino acids of Hrd1p in the cytosol to induce oligomerization of Hrd1p, which is essential for its activity.	DISCUSS
+187	192	Hrd1p	protein	In yeast, Usa1p acts as a scaffold for Hrd1p and Der1p, in which the N-terminus of Usa1p interacts with the C-terminal 34 amino acids of Hrd1p in the cytosol to induce oligomerization of Hrd1p, which is essential for its activity.	DISCUSS
+9	18	metazoans	taxonomy_domain	However, metazoans lack a clear Usa1p homolog.	DISCUSS
+32	37	Usa1p	protein	However, metazoans lack a clear Usa1p homolog.	DISCUSS
+9	18	mammalian	taxonomy_domain	Although mammalian HERP has sequences and domains that are conserved in Usa1p, the molecular function of HERP is not clearly related to that of Usa1p.	DISCUSS
+19	23	HERP	protein_type	Although mammalian HERP has sequences and domains that are conserved in Usa1p, the molecular function of HERP is not clearly related to that of Usa1p.	DISCUSS
+59	71	conserved in	protein_state	Although mammalian HERP has sequences and domains that are conserved in Usa1p, the molecular function of HERP is not clearly related to that of Usa1p.	DISCUSS
+72	77	Usa1p	protein	Although mammalian HERP has sequences and domains that are conserved in Usa1p, the molecular function of HERP is not clearly related to that of Usa1p.	DISCUSS
+105	109	HERP	protein_type	Although mammalian HERP has sequences and domains that are conserved in Usa1p, the molecular function of HERP is not clearly related to that of Usa1p.	DISCUSS
+144	149	Usa1p	protein	Although mammalian HERP has sequences and domains that are conserved in Usa1p, the molecular function of HERP is not clearly related to that of Usa1p.	DISCUSS
+37	58	transiently expressed	protein_state	Rather, recent research shows that a transiently expressed HRD1-SEL1L complex alone associates with the ERAD lectins OS9 or XTP-B and is sufficient to facilitate the retrotranslocation and degradation of the model ERAD substrate α-antitrypsin null Hong-Kong (NHK) and its variant, NHK-QQQ, which lacks the N-glycosylation sites.	DISCUSS
+59	69	HRD1-SEL1L	complex_assembly	Rather, recent research shows that a transiently expressed HRD1-SEL1L complex alone associates with the ERAD lectins OS9 or XTP-B and is sufficient to facilitate the retrotranslocation and degradation of the model ERAD substrate α-antitrypsin null Hong-Kong (NHK) and its variant, NHK-QQQ, which lacks the N-glycosylation sites.	DISCUSS
+109	116	lectins	protein_type	Rather, recent research shows that a transiently expressed HRD1-SEL1L complex alone associates with the ERAD lectins OS9 or XTP-B and is sufficient to facilitate the retrotranslocation and degradation of the model ERAD substrate α-antitrypsin null Hong-Kong (NHK) and its variant, NHK-QQQ, which lacks the N-glycosylation sites.	DISCUSS
+117	120	OS9	protein	Rather, recent research shows that a transiently expressed HRD1-SEL1L complex alone associates with the ERAD lectins OS9 or XTP-B and is sufficient to facilitate the retrotranslocation and degradation of the model ERAD substrate α-antitrypsin null Hong-Kong (NHK) and its variant, NHK-QQQ, which lacks the N-glycosylation sites.	DISCUSS
+124	129	XTP-B	protein	Rather, recent research shows that a transiently expressed HRD1-SEL1L complex alone associates with the ERAD lectins OS9 or XTP-B and is sufficient to facilitate the retrotranslocation and degradation of the model ERAD substrate α-antitrypsin null Hong-Kong (NHK) and its variant, NHK-QQQ, which lacks the N-glycosylation sites.	DISCUSS
+229	257	α-antitrypsin null Hong-Kong	protein	Rather, recent research shows that a transiently expressed HRD1-SEL1L complex alone associates with the ERAD lectins OS9 or XTP-B and is sufficient to facilitate the retrotranslocation and degradation of the model ERAD substrate α-antitrypsin null Hong-Kong (NHK) and its variant, NHK-QQQ, which lacks the N-glycosylation sites.	DISCUSS
+259	262	NHK	protein	Rather, recent research shows that a transiently expressed HRD1-SEL1L complex alone associates with the ERAD lectins OS9 or XTP-B and is sufficient to facilitate the retrotranslocation and degradation of the model ERAD substrate α-antitrypsin null Hong-Kong (NHK) and its variant, NHK-QQQ, which lacks the N-glycosylation sites.	DISCUSS
+281	288	NHK-QQQ	mutant	Rather, recent research shows that a transiently expressed HRD1-SEL1L complex alone associates with the ERAD lectins OS9 or XTP-B and is sufficient to facilitate the retrotranslocation and degradation of the model ERAD substrate α-antitrypsin null Hong-Kong (NHK) and its variant, NHK-QQQ, which lacks the N-glycosylation sites.	DISCUSS
+296	301	lacks	protein_state	Rather, recent research shows that a transiently expressed HRD1-SEL1L complex alone associates with the ERAD lectins OS9 or XTP-B and is sufficient to facilitate the retrotranslocation and degradation of the model ERAD substrate α-antitrypsin null Hong-Kong (NHK) and its variant, NHK-QQQ, which lacks the N-glycosylation sites.	DISCUSS
+306	327	N-glycosylation sites	site	Rather, recent research shows that a transiently expressed HRD1-SEL1L complex alone associates with the ERAD lectins OS9 or XTP-B and is sufficient to facilitate the retrotranslocation and degradation of the model ERAD substrate α-antitrypsin null Hong-Kong (NHK) and its variant, NHK-QQQ, which lacks the N-glycosylation sites.	DISCUSS
+117	126	homodimer	oligomeric_state	Assuming that the correct oligomerization of ERAD components may be critical for their function, we hypothesize that homodimer formation of SEL1L in the ER lumen may stabilize oligomerization of the HRD complex, given that SEL1L forms a stoichiometric complex with HRD1.	DISCUSS
+140	145	SEL1L	protein	Assuming that the correct oligomerization of ERAD components may be critical for their function, we hypothesize that homodimer formation of SEL1L in the ER lumen may stabilize oligomerization of the HRD complex, given that SEL1L forms a stoichiometric complex with HRD1.	DISCUSS
+199	202	HRD	complex_assembly	Assuming that the correct oligomerization of ERAD components may be critical for their function, we hypothesize that homodimer formation of SEL1L in the ER lumen may stabilize oligomerization of the HRD complex, given that SEL1L forms a stoichiometric complex with HRD1.	DISCUSS
+223	228	SEL1L	protein	Assuming that the correct oligomerization of ERAD components may be critical for their function, we hypothesize that homodimer formation of SEL1L in the ER lumen may stabilize oligomerization of the HRD complex, given that SEL1L forms a stoichiometric complex with HRD1.	DISCUSS
+252	264	complex with	protein_state	Assuming that the correct oligomerization of ERAD components may be critical for their function, we hypothesize that homodimer formation of SEL1L in the ER lumen may stabilize oligomerization of the HRD complex, given that SEL1L forms a stoichiometric complex with HRD1.	DISCUSS
+265	269	HRD1	protein	Assuming that the correct oligomerization of ERAD components may be critical for their function, we hypothesize that homodimer formation of SEL1L in the ER lumen may stabilize oligomerization of the HRD complex, given that SEL1L forms a stoichiometric complex with HRD1.	DISCUSS
+55	60	SLR-C	structure_element	This is further supported by our data showing that the SLR-C of SEL1L directly interacts with the luminal fragment of HRD1 in the ER lumen.	DISCUSS
+64	69	SEL1L	protein	This is further supported by our data showing that the SLR-C of SEL1L directly interacts with the luminal fragment of HRD1 in the ER lumen.	DISCUSS
+118	122	HRD1	protein	This is further supported by our data showing that the SLR-C of SEL1L directly interacts with the luminal fragment of HRD1 in the ER lumen.	DISCUSS
+44	47	HRD	complex_assembly	Although the organization of membrane-bound HRD complex components may be very similar between metazoans and yeast, the molecular details of interactions between the components may not necessarily be conserved.	DISCUSS
+95	104	metazoans	taxonomy_domain	Although the organization of membrane-bound HRD complex components may be very similar between metazoans and yeast, the molecular details of interactions between the components may not necessarily be conserved.	DISCUSS
+109	114	yeast	taxonomy_domain	Although the organization of membrane-bound HRD complex components may be very similar between metazoans and yeast, the molecular details of interactions between the components may not necessarily be conserved.	DISCUSS
+3	8	yeast	taxonomy_domain	In yeast, it is unclear whether self-association of Hrd3p is due to SLR motifs because the sequence of Hrd3p does not align precisely with the SLR motifs in SEL1L.	DISCUSS
+52	57	Hrd3p	protein	In yeast, it is unclear whether self-association of Hrd3p is due to SLR motifs because the sequence of Hrd3p does not align precisely with the SLR motifs in SEL1L.	DISCUSS
+68	71	SLR	structure_element	In yeast, it is unclear whether self-association of Hrd3p is due to SLR motifs because the sequence of Hrd3p does not align precisely with the SLR motifs in SEL1L.	DISCUSS
+103	108	Hrd3p	protein	In yeast, it is unclear whether self-association of Hrd3p is due to SLR motifs because the sequence of Hrd3p does not align precisely with the SLR motifs in SEL1L.	DISCUSS
+143	146	SLR	structure_element	In yeast, it is unclear whether self-association of Hrd3p is due to SLR motifs because the sequence of Hrd3p does not align precisely with the SLR motifs in SEL1L.	DISCUSS
+157	162	SEL1L	protein	In yeast, it is unclear whether self-association of Hrd3p is due to SLR motifs because the sequence of Hrd3p does not align precisely with the SLR motifs in SEL1L.	DISCUSS
+58	63	Hrd3p	protein	Furthermore, we are uncertain whether self-association of Hrd3p contributes to formation of the active form of the Hrd1p complex.	DISCUSS
+96	102	active	protein_state	Furthermore, we are uncertain whether self-association of Hrd3p contributes to formation of the active form of the Hrd1p complex.	DISCUSS
+115	120	Hrd1p	protein	Furthermore, we are uncertain whether self-association of Hrd3p contributes to formation of the active form of the Hrd1p complex.	DISCUSS
+12	21	truncated	protein_state	Recently, a truncated version of Yos9 was shown to form a dimer in the ER lumen and to contribute to the dimeric state of the Hrd1p complex.	DISCUSS
+33	37	Yos9	protein	Recently, a truncated version of Yos9 was shown to form a dimer in the ER lumen and to contribute to the dimeric state of the Hrd1p complex.	DISCUSS
+58	63	dimer	oligomeric_state	Recently, a truncated version of Yos9 was shown to form a dimer in the ER lumen and to contribute to the dimeric state of the Hrd1p complex.	DISCUSS
+105	112	dimeric	oligomeric_state	Recently, a truncated version of Yos9 was shown to form a dimer in the ER lumen and to contribute to the dimeric state of the Hrd1p complex.	DISCUSS
+126	131	Hrd1p	protein	Recently, a truncated version of Yos9 was shown to form a dimer in the ER lumen and to contribute to the dimeric state of the Hrd1p complex.	DISCUSS
+49	53	Yos9	protein	This interaction seems to be weak because direct Yos9-Yos9 interactions were not detected in immunoprecipitation experiments from yeast cell extracts containing different epitope-tagged variants of Yos9.	DISCUSS
+54	58	Yos9	protein	This interaction seems to be weak because direct Yos9-Yos9 interactions were not detected in immunoprecipitation experiments from yeast cell extracts containing different epitope-tagged variants of Yos9.	DISCUSS
+93	124	immunoprecipitation experiments	experimental_method	This interaction seems to be weak because direct Yos9-Yos9 interactions were not detected in immunoprecipitation experiments from yeast cell extracts containing different epitope-tagged variants of Yos9.	DISCUSS
+130	135	yeast	taxonomy_domain	This interaction seems to be weak because direct Yos9-Yos9 interactions were not detected in immunoprecipitation experiments from yeast cell extracts containing different epitope-tagged variants of Yos9.	DISCUSS
+171	185	epitope-tagged	protein_state	This interaction seems to be weak because direct Yos9-Yos9 interactions were not detected in immunoprecipitation experiments from yeast cell extracts containing different epitope-tagged variants of Yos9.	DISCUSS
+198	202	Yos9	protein	This interaction seems to be weak because direct Yos9-Yos9 interactions were not detected in immunoprecipitation experiments from yeast cell extracts containing different epitope-tagged variants of Yos9.	DISCUSS
+13	25	dimerization	oligomeric_state	However, the dimerization of Yos9 could provide a higher stability for the Hrd1p complex oligomer.	DISCUSS
+29	33	Yos9	protein	However, the dimerization of Yos9 could provide a higher stability for the Hrd1p complex oligomer.	DISCUSS
+75	80	Hrd1p	protein	However, the dimerization of Yos9 could provide a higher stability for the Hrd1p complex oligomer.	DISCUSS
+89	97	oligomer	oligomeric_state	However, the dimerization of Yos9 could provide a higher stability for the Hrd1p complex oligomer.	DISCUSS
+14	26	dimerization	oligomeric_state	Likewise, the dimerization of SEL1L might provide stability for the mammalian HRD oligomer complex.	DISCUSS
+30	35	SEL1L	protein	Likewise, the dimerization of SEL1L might provide stability for the mammalian HRD oligomer complex.	DISCUSS
+68	77	mammalian	taxonomy_domain	Likewise, the dimerization of SEL1L might provide stability for the mammalian HRD oligomer complex.	DISCUSS
+78	81	HRD	complex_assembly	Likewise, the dimerization of SEL1L might provide stability for the mammalian HRD oligomer complex.	DISCUSS
+82	90	oligomer	oligomeric_state	Likewise, the dimerization of SEL1L might provide stability for the mammalian HRD oligomer complex.	DISCUSS
+64	69	SEL1L	protein	Further cell biological studies are required to clarify whether SEL1L (Hrd3p) dimerization could be cooperative with the oligomerization of the HRD complex.	DISCUSS
+71	76	Hrd3p	protein	Further cell biological studies are required to clarify whether SEL1L (Hrd3p) dimerization could be cooperative with the oligomerization of the HRD complex.	DISCUSS
+78	90	dimerization	oligomeric_state	Further cell biological studies are required to clarify whether SEL1L (Hrd3p) dimerization could be cooperative with the oligomerization of the HRD complex.	DISCUSS
+144	147	HRD	complex_assembly	Further cell biological studies are required to clarify whether SEL1L (Hrd3p) dimerization could be cooperative with the oligomerization of the HRD complex.	DISCUSS
+62	65	HRD	complex_assembly	Considering that it is very important for the function of the HRD complex that the components assemble as oligomers, we believe that the self-association of SEL1L strongly contributes to generating active forms of the HRD complex, even in the absence of Usa1p, in metazoans.	DISCUSS
+106	115	oligomers	oligomeric_state	Considering that it is very important for the function of the HRD complex that the components assemble as oligomers, we believe that the self-association of SEL1L strongly contributes to generating active forms of the HRD complex, even in the absence of Usa1p, in metazoans.	DISCUSS
+157	162	SEL1L	protein	Considering that it is very important for the function of the HRD complex that the components assemble as oligomers, we believe that the self-association of SEL1L strongly contributes to generating active forms of the HRD complex, even in the absence of Usa1p, in metazoans.	DISCUSS
+198	204	active	protein_state	Considering that it is very important for the function of the HRD complex that the components assemble as oligomers, we believe that the self-association of SEL1L strongly contributes to generating active forms of the HRD complex, even in the absence of Usa1p, in metazoans.	DISCUSS
+218	221	HRD	complex_assembly	Considering that it is very important for the function of the HRD complex that the components assemble as oligomers, we believe that the self-association of SEL1L strongly contributes to generating active forms of the HRD complex, even in the absence of Usa1p, in metazoans.	DISCUSS
+243	253	absence of	protein_state	Considering that it is very important for the function of the HRD complex that the components assemble as oligomers, we believe that the self-association of SEL1L strongly contributes to generating active forms of the HRD complex, even in the absence of Usa1p, in metazoans.	DISCUSS
+254	259	Usa1p	protein	Considering that it is very important for the function of the HRD complex that the components assemble as oligomers, we believe that the self-association of SEL1L strongly contributes to generating active forms of the HRD complex, even in the absence of Usa1p, in metazoans.	DISCUSS
+264	273	metazoans	taxonomy_domain	Considering that it is very important for the function of the HRD complex that the components assemble as oligomers, we believe that the self-association of SEL1L strongly contributes to generating active forms of the HRD complex, even in the absence of Usa1p, in metazoans.	DISCUSS
+109	112	HRD	complex_assembly	These findings should provide a foundation for molecular-level studies to understand the membrane-associated HRD complex assembly in ERAD.	DISCUSS
+0	17	Crystal Structure	evidence	Crystal Structure of SEL1Lcent.	FIG
+21	30	SEL1Lcent	structure_element	Crystal Structure of SEL1Lcent.	FIG
+46	58	Mus musculus	species	(A) The diagram shows the domain structure of Mus musculus SEL1L, as defined by proteolytic mapping and sequence/structure analysis.	FIG
+59	64	SEL1L	protein	(A) The diagram shows the domain structure of Mus musculus SEL1L, as defined by proteolytic mapping and sequence/structure analysis.	FIG
+80	99	proteolytic mapping	experimental_method	(A) The diagram shows the domain structure of Mus musculus SEL1L, as defined by proteolytic mapping and sequence/structure analysis.	FIG
+104	131	sequence/structure analysis	experimental_method	(A) The diagram shows the domain structure of Mus musculus SEL1L, as defined by proteolytic mapping and sequence/structure analysis.	FIG
+7	10	SLR	structure_element	The 11 SLR motifs were divided into three groups (SLR-N, SLR-M, and SLR-C) due to the presence of linker sequences that are not predicted SLR motifs.	FIG
+50	55	SLR-N	structure_element	The 11 SLR motifs were divided into three groups (SLR-N, SLR-M, and SLR-C) due to the presence of linker sequences that are not predicted SLR motifs.	FIG
+57	62	SLR-M	structure_element	The 11 SLR motifs were divided into three groups (SLR-N, SLR-M, and SLR-C) due to the presence of linker sequences that are not predicted SLR motifs.	FIG
+68	73	SLR-C	structure_element	The 11 SLR motifs were divided into three groups (SLR-N, SLR-M, and SLR-C) due to the presence of linker sequences that are not predicted SLR motifs.	FIG
+98	114	linker sequences	structure_element	The 11 SLR motifs were divided into three groups (SLR-N, SLR-M, and SLR-C) due to the presence of linker sequences that are not predicted SLR motifs.	FIG
+138	141	SLR	structure_element	The 11 SLR motifs were divided into three groups (SLR-N, SLR-M, and SLR-C) due to the presence of linker sequences that are not predicted SLR motifs.	FIG
+9	30	N-glycosylation sites	site	Putative N-glycosylation sites are indicated by black triangles.	FIG
+18	35	crystal structure	evidence	We determined the crystal structure of the SLR-M, residues 348–533. (B) Ribbon diagram of the biological unit of the SEL1Lcent, viewed along the two-fold NCS axis.	FIG
+43	48	SLR-M	structure_element	We determined the crystal structure of the SLR-M, residues 348–533. (B) Ribbon diagram of the biological unit of the SEL1Lcent, viewed along the two-fold NCS axis.	FIG
+59	66	348–533	residue_range	We determined the crystal structure of the SLR-M, residues 348–533. (B) Ribbon diagram of the biological unit of the SEL1Lcent, viewed along the two-fold NCS axis.	FIG
+117	126	SEL1Lcent	structure_element	We determined the crystal structure of the SLR-M, residues 348–533. (B) Ribbon diagram of the biological unit of the SEL1Lcent, viewed along the two-fold NCS axis.	FIG
+4	21	crystal structure	evidence	The crystal structure was determined by SAD phasing using selenium as the anomalous scatterer and refined to 2.6 Å resolution (Table 1).	FIG
+40	51	SAD phasing	experimental_method	The crystal structure was determined by SAD phasing using selenium as the anomalous scatterer and refined to 2.6 Å resolution (Table 1).	FIG
+58	66	selenium	chemical	The crystal structure was determined by SAD phasing using selenium as the anomalous scatterer and refined to 2.6 Å resolution (Table 1).	FIG
+4	13	SEL1Lcent	structure_element	(C) SEL1Lcent ribbon diagram rotated 90° around a horizontal axis relative to (B).	FIG
+8	16	protomer	oligomeric_state	(D) One protomer of the SEL1Lcent dimer.	FIG
+24	33	SEL1Lcent	structure_element	(D) One protomer of the SEL1Lcent dimer.	FIG
+34	39	dimer	oligomeric_state	(D) One protomer of the SEL1Lcent dimer.	FIG
+30	39	SEL1Lcent	structure_element	Starting from the N-terminus, SEL1Lcent has five SLR motifs comprising ten α helices.	FIG
+49	52	SLR	structure_element	Starting from the N-terminus, SEL1Lcent has five SLR motifs comprising ten α helices.	FIG
+75	84	α helices	structure_element	Starting from the N-terminus, SEL1Lcent has five SLR motifs comprising ten α helices.	FIG
+5	8	SLR	structure_element	Each SLR motif (from 5 to 9) is indicated in a different color. (E) Evolutionary conservation of surface residues in SEL1Lcent, calculated using ConSurf, from a structure-based alignment of 135 SEL1L sequences.	FIG
+117	126	SEL1Lcent	structure_element	Each SLR motif (from 5 to 9) is indicated in a different color. (E) Evolutionary conservation of surface residues in SEL1Lcent, calculated using ConSurf, from a structure-based alignment of 135 SEL1L sequences.	FIG
+145	152	ConSurf	experimental_method	Each SLR motif (from 5 to 9) is indicated in a different color. (E) Evolutionary conservation of surface residues in SEL1Lcent, calculated using ConSurf, from a structure-based alignment of 135 SEL1L sequences.	FIG
+161	186	structure-based alignment	experimental_method	Each SLR motif (from 5 to 9) is indicated in a different color. (E) Evolutionary conservation of surface residues in SEL1Lcent, calculated using ConSurf, from a structure-based alignment of 135 SEL1L sequences.	FIG
+194	199	SEL1L	protein	Each SLR motif (from 5 to 9) is indicated in a different color. (E) Evolutionary conservation of surface residues in SEL1Lcent, calculated using ConSurf, from a structure-based alignment of 135 SEL1L sequences.	FIG
+102	107	SEL1L	protein	The surface is colored from red (high) to white (poor) according to the degree of conservation in the SEL1L phylogenetic orthologs.	FIG
+38	46	protomer	oligomeric_state	The ribbon diagram of the counterpart protomer is drawn to show the orientation of the SEL1Lcent dimer.	FIG
+87	96	SEL1Lcent	structure_element	The ribbon diagram of the counterpart protomer is drawn to show the orientation of the SEL1Lcent dimer.	FIG
+97	102	dimer	oligomeric_state	The ribbon diagram of the counterpart protomer is drawn to show the orientation of the SEL1Lcent dimer.	FIG
+0	15	Dimer Interface	site	Dimer Interface of SEL1Lcent.	FIG
+19	28	SEL1Lcent	structure_element	Dimer Interface of SEL1Lcent.	FIG
+38	47	SEL1Lcent	structure_element	(A) The diagram on the left shows the SEL1Lcent dimer viewed along the two-fold symmetry axis.	FIG
+48	53	dimer	oligomeric_state	(A) The diagram on the left shows the SEL1Lcent dimer viewed along the two-fold symmetry axis.	FIG
+15	30	contact regions	site	Three distinct contact regions are indicated with labeled boxes.	FIG
+53	62	SEL1Lcent	structure_element	The close-up view on the right shows the residues of SEL1Lcent that contribute to dimer formation via the three contact interfaces.	FIG
+82	87	dimer	oligomeric_state	The close-up view on the right shows the residues of SEL1Lcent that contribute to dimer formation via the three contact interfaces.	FIG
+112	130	contact interfaces	site	The close-up view on the right shows the residues of SEL1Lcent that contribute to dimer formation via the three contact interfaces.	FIG
+48	62	hydrogen bonds	bond_interaction	The yellow dotted lines indicate intermolecular hydrogen bonds between two protomers of SEL1Lcent. (B) Size-exclusion chromatography (SEC) analysis of the wild-type and dimeric interface SEL1Lcent mutants to compare the oligomeric states of the proteins.	FIG
+75	84	protomers	oligomeric_state	The yellow dotted lines indicate intermolecular hydrogen bonds between two protomers of SEL1Lcent. (B) Size-exclusion chromatography (SEC) analysis of the wild-type and dimeric interface SEL1Lcent mutants to compare the oligomeric states of the proteins.	FIG
+88	97	SEL1Lcent	structure_element	The yellow dotted lines indicate intermolecular hydrogen bonds between two protomers of SEL1Lcent. (B) Size-exclusion chromatography (SEC) analysis of the wild-type and dimeric interface SEL1Lcent mutants to compare the oligomeric states of the proteins.	FIG
+103	132	Size-exclusion chromatography	experimental_method	The yellow dotted lines indicate intermolecular hydrogen bonds between two protomers of SEL1Lcent. (B) Size-exclusion chromatography (SEC) analysis of the wild-type and dimeric interface SEL1Lcent mutants to compare the oligomeric states of the proteins.	FIG
+134	137	SEC	experimental_method	The yellow dotted lines indicate intermolecular hydrogen bonds between two protomers of SEL1Lcent. (B) Size-exclusion chromatography (SEC) analysis of the wild-type and dimeric interface SEL1Lcent mutants to compare the oligomeric states of the proteins.	FIG
+155	164	wild-type	protein_state	The yellow dotted lines indicate intermolecular hydrogen bonds between two protomers of SEL1Lcent. (B) Size-exclusion chromatography (SEC) analysis of the wild-type and dimeric interface SEL1Lcent mutants to compare the oligomeric states of the proteins.	FIG
+169	186	dimeric interface	site	The yellow dotted lines indicate intermolecular hydrogen bonds between two protomers of SEL1Lcent. (B) Size-exclusion chromatography (SEC) analysis of the wild-type and dimeric interface SEL1Lcent mutants to compare the oligomeric states of the proteins.	FIG
+187	196	SEL1Lcent	structure_element	The yellow dotted lines indicate intermolecular hydrogen bonds between two protomers of SEL1Lcent. (B) Size-exclusion chromatography (SEC) analysis of the wild-type and dimeric interface SEL1Lcent mutants to compare the oligomeric states of the proteins.	FIG
+197	204	mutants	protein_state	The yellow dotted lines indicate intermolecular hydrogen bonds between two protomers of SEL1Lcent. (B) Size-exclusion chromatography (SEC) analysis of the wild-type and dimeric interface SEL1Lcent mutants to compare the oligomeric states of the proteins.	FIG
+38	41	SEC	experimental_method	The standard molecular masses for the SEC experiments (top) were obtained from the following proteins: aldolase, 158 kDa; cobalbumin, 75 kDa; ovalbumin, 44 kDa; and carbonic anhydrase, 29 kDa.	FIG
+66	74	SDS-PAGE	experimental_method	The elution fractions, indicated by the gray shading, were run on SDS-PAGE and are shown below the gel-filtration elution profile.	FIG
+99	129	gel-filtration elution profile	evidence	The elution fractions, indicated by the gray shading, were run on SDS-PAGE and are shown below the gel-filtration elution profile.	FIG
+71	74	SEC	experimental_method	The schematic diagrams representing the protein constructs used in the SEC are shown on the left of each SDS-PAGE profile.	FIG
+105	113	SDS-PAGE	experimental_method	The schematic diagrams representing the protein constructs used in the SEC are shown on the left of each SDS-PAGE profile.	FIG
+20	32	Dimerization	oligomeric_state	Domain Swapping for Dimerization of SEL1Lcent.	FIG
+36	45	SEL1Lcent	structure_element	Domain Swapping for Dimerization of SEL1Lcent.	FIG
+4	22	Sequence alignment	experimental_method	(A) Sequence alignment of the SLR motifs in SEL1L.	FIG
+30	33	SLR	structure_element	(A) Sequence alignment of the SLR motifs in SEL1L.	FIG
+44	49	SEL1L	protein	(A) Sequence alignment of the SLR motifs in SEL1L.	FIG
+7	10	SLR	structure_element	The 11 SLR motifs were aligned based on the present crystal structure of SEL1Lcent.	FIG
+23	30	aligned	experimental_method	The 11 SLR motifs were aligned based on the present crystal structure of SEL1Lcent.	FIG
+52	69	crystal structure	evidence	The 11 SLR motifs were aligned based on the present crystal structure of SEL1Lcent.	FIG
+73	82	SEL1Lcent	structure_element	The 11 SLR motifs were aligned based on the present crystal structure of SEL1Lcent.	FIG
+17	26	SEL1Lcent	structure_element	The sequences of SEL1Lcent included in the crystal structure are highlighted by the blue box.	FIG
+43	60	crystal structure	evidence	The sequences of SEL1Lcent included in the crystal structure are highlighted by the blue box.	FIG
+73	80	helices	structure_element	The secondary structure elements are indicated above the sequences, with helices depicted as cylinders.	FIG
+4	6	GG	structure_element	The GG sequence in SLR motif 9, which creates the hinge for domain swapping (see text), is shaded yellow.	FIG
+19	30	SLR motif 9	structure_element	The GG sequence in SLR motif 9, which creates the hinge for domain swapping (see text), is shaded yellow.	FIG
+50	55	hinge	structure_element	The GG sequence in SLR motif 9, which creates the hinge for domain swapping (see text), is shaded yellow.	FIG
+81	85	SLRs	structure_element	Stars below the sequences indicate the specific residues that commonly appear in SLRs.	FIG
+4	23	Structure alignment	experimental_method	(B) Structure alignment of five SLR motifs in SEL1Lcent is shown to highlight the unusual geometry of SLR motif 9.	FIG
+32	35	SLR	structure_element	(B) Structure alignment of five SLR motifs in SEL1Lcent is shown to highlight the unusual geometry of SLR motif 9.	FIG
+46	55	SEL1Lcent	structure_element	(B) Structure alignment of five SLR motifs in SEL1Lcent is shown to highlight the unusual geometry of SLR motif 9.	FIG
+102	113	SLR motif 9	structure_element	(B) Structure alignment of five SLR motifs in SEL1Lcent is shown to highlight the unusual geometry of SLR motif 9.	FIG
+5	8	SLR	structure_element	Each SLR motif is shown in a different color.	FIG
+3	14	SLR motif 9	structure_element	In SLR motif 9, the axes for the two helices are almost parallel, while the other SLR motifs adopt an α-hairpin structure. (C) Stereo view shows that the Gly 512 and Gly 513 residues are surrounded by neighboring residues from helix 9B from the counterpart dimer.	FIG
+37	44	helices	structure_element	In SLR motif 9, the axes for the two helices are almost parallel, while the other SLR motifs adopt an α-hairpin structure. (C) Stereo view shows that the Gly 512 and Gly 513 residues are surrounded by neighboring residues from helix 9B from the counterpart dimer.	FIG
+82	85	SLR	structure_element	In SLR motif 9, the axes for the two helices are almost parallel, while the other SLR motifs adopt an α-hairpin structure. (C) Stereo view shows that the Gly 512 and Gly 513 residues are surrounded by neighboring residues from helix 9B from the counterpart dimer.	FIG
+102	111	α-hairpin	structure_element	In SLR motif 9, the axes for the two helices are almost parallel, while the other SLR motifs adopt an α-hairpin structure. (C) Stereo view shows that the Gly 512 and Gly 513 residues are surrounded by neighboring residues from helix 9B from the counterpart dimer.	FIG
+154	161	Gly 512	residue_name_number	In SLR motif 9, the axes for the two helices are almost parallel, while the other SLR motifs adopt an α-hairpin structure. (C) Stereo view shows that the Gly 512 and Gly 513 residues are surrounded by neighboring residues from helix 9B from the counterpart dimer.	FIG
+166	173	Gly 513	residue_name_number	In SLR motif 9, the axes for the two helices are almost parallel, while the other SLR motifs adopt an α-hairpin structure. (C) Stereo view shows that the Gly 512 and Gly 513 residues are surrounded by neighboring residues from helix 9B from the counterpart dimer.	FIG
+227	235	helix 9B	structure_element	In SLR motif 9, the axes for the two helices are almost parallel, while the other SLR motifs adopt an α-hairpin structure. (C) Stereo view shows that the Gly 512 and Gly 513 residues are surrounded by neighboring residues from helix 9B from the counterpart dimer.	FIG
+257	262	dimer	oligomeric_state	In SLR motif 9, the axes for the two helices are almost parallel, while the other SLR motifs adopt an α-hairpin structure. (C) Stereo view shows that the Gly 512 and Gly 513 residues are surrounded by neighboring residues from helix 9B from the counterpart dimer.	FIG
+4	11	Gly 512	residue_name_number	The Gly 512 and Gly 513 residues are colored green and red, respectively. (D) The following point mutations were generated to check the effect of the Gly 512 and Gly 513 residues in terms of generating the hinge of SLR motif 9: G512A, G513A, G512A/G513A, and G512K/G513K.	FIG
+16	23	Gly 513	residue_name_number	The Gly 512 and Gly 513 residues are colored green and red, respectively. (D) The following point mutations were generated to check the effect of the Gly 512 and Gly 513 residues in terms of generating the hinge of SLR motif 9: G512A, G513A, G512A/G513A, and G512K/G513K.	FIG
+92	107	point mutations	experimental_method	The Gly 512 and Gly 513 residues are colored green and red, respectively. (D) The following point mutations were generated to check the effect of the Gly 512 and Gly 513 residues in terms of generating the hinge of SLR motif 9: G512A, G513A, G512A/G513A, and G512K/G513K.	FIG
+150	157	Gly 512	residue_name_number	The Gly 512 and Gly 513 residues are colored green and red, respectively. (D) The following point mutations were generated to check the effect of the Gly 512 and Gly 513 residues in terms of generating the hinge of SLR motif 9: G512A, G513A, G512A/G513A, and G512K/G513K.	FIG
+162	169	Gly 513	residue_name_number	The Gly 512 and Gly 513 residues are colored green and red, respectively. (D) The following point mutations were generated to check the effect of the Gly 512 and Gly 513 residues in terms of generating the hinge of SLR motif 9: G512A, G513A, G512A/G513A, and G512K/G513K.	FIG
+206	211	hinge	structure_element	The Gly 512 and Gly 513 residues are colored green and red, respectively. (D) The following point mutations were generated to check the effect of the Gly 512 and Gly 513 residues in terms of generating the hinge of SLR motif 9: G512A, G513A, G512A/G513A, and G512K/G513K.	FIG
+215	226	SLR motif 9	structure_element	The Gly 512 and Gly 513 residues are colored green and red, respectively. (D) The following point mutations were generated to check the effect of the Gly 512 and Gly 513 residues in terms of generating the hinge of SLR motif 9: G512A, G513A, G512A/G513A, and G512K/G513K.	FIG
+228	233	G512A	mutant	The Gly 512 and Gly 513 residues are colored green and red, respectively. (D) The following point mutations were generated to check the effect of the Gly 512 and Gly 513 residues in terms of generating the hinge of SLR motif 9: G512A, G513A, G512A/G513A, and G512K/G513K.	FIG
+235	240	G513A	mutant	The Gly 512 and Gly 513 residues are colored green and red, respectively. (D) The following point mutations were generated to check the effect of the Gly 512 and Gly 513 residues in terms of generating the hinge of SLR motif 9: G512A, G513A, G512A/G513A, and G512K/G513K.	FIG
+242	247	G512A	mutant	The Gly 512 and Gly 513 residues are colored green and red, respectively. (D) The following point mutations were generated to check the effect of the Gly 512 and Gly 513 residues in terms of generating the hinge of SLR motif 9: G512A, G513A, G512A/G513A, and G512K/G513K.	FIG
+248	253	G513A	mutant	The Gly 512 and Gly 513 residues are colored green and red, respectively. (D) The following point mutations were generated to check the effect of the Gly 512 and Gly 513 residues in terms of generating the hinge of SLR motif 9: G512A, G513A, G512A/G513A, and G512K/G513K.	FIG
+259	264	G512K	mutant	The Gly 512 and Gly 513 residues are colored green and red, respectively. (D) The following point mutations were generated to check the effect of the Gly 512 and Gly 513 residues in terms of generating the hinge of SLR motif 9: G512A, G513A, G512A/G513A, and G512K/G513K.	FIG
+265	270	G513K	mutant	The Gly 512 and Gly 513 residues are colored green and red, respectively. (D) The following point mutations were generated to check the effect of the Gly 512 and Gly 513 residues in terms of generating the hinge of SLR motif 9: G512A, G513A, G512A/G513A, and G512K/G513K.	FIG
+0	29	Size-exclusion chromatography	experimental_method	Size-exclusion chromatography was conducted as described in Fig. 2B.	FIG
+0	5	SEL1L	protein	SEL1L forms self-oligomer mediated by the SEL1Lcent domain in vivo.	FIG
+12	25	self-oligomer	oligomeric_state	SEL1L forms self-oligomer mediated by the SEL1Lcent domain in vivo.	FIG
+42	51	SEL1Lcent	structure_element	SEL1L forms self-oligomer mediated by the SEL1Lcent domain in vivo.	FIG
+94	112	immunoprecipitated	experimental_method	(A) HEK293T cells were transfected with the indicated plasmid constructs and the lysates were immunoprecipitated with an anti-FLAG antibody followed by western blot analysis using an anti-HA antibody.	FIG
+126	130	FLAG	experimental_method	(A) HEK293T cells were transfected with the indicated plasmid constructs and the lysates were immunoprecipitated with an anti-FLAG antibody followed by western blot analysis using an anti-HA antibody.	FIG
+152	164	western blot	experimental_method	(A) HEK293T cells were transfected with the indicated plasmid constructs and the lysates were immunoprecipitated with an anti-FLAG antibody followed by western blot analysis using an anti-HA antibody.	FIG
+188	190	HA	experimental_method	(A) HEK293T cells were transfected with the indicated plasmid constructs and the lysates were immunoprecipitated with an anti-FLAG antibody followed by western blot analysis using an anti-HA antibody.	FIG
+4	15	full-length	protein_state	The full-length SEL1L-FLAG was co-immunoprecipitated with the full-length SEL1L-HA.	FIG
+16	21	SEL1L	protein	The full-length SEL1L-FLAG was co-immunoprecipitated with the full-length SEL1L-HA.	FIG
+22	26	FLAG	experimental_method	The full-length SEL1L-FLAG was co-immunoprecipitated with the full-length SEL1L-HA.	FIG
+31	52	co-immunoprecipitated	experimental_method	The full-length SEL1L-FLAG was co-immunoprecipitated with the full-length SEL1L-HA.	FIG
+62	73	full-length	protein_state	The full-length SEL1L-FLAG was co-immunoprecipitated with the full-length SEL1L-HA.	FIG
+74	79	SEL1L	protein	The full-length SEL1L-FLAG was co-immunoprecipitated with the full-length SEL1L-HA.	FIG
+80	82	HA	experimental_method	The full-length SEL1L-FLAG was co-immunoprecipitated with the full-length SEL1L-HA.	FIG
+6	15	SEL1Lcent	structure_element	Also, SEL1Lcent was co-immunoprecipitated with the full-length SEL1L while the SLR motif 9 deletion failed to do so. (B) The HEK293T cells were transfected with the indicated plasmid constructs and the cell lysate and culture media were analyzed by western blot analysis and immunoprecipitation respectively.	FIG
+20	41	co-immunoprecipitated	experimental_method	Also, SEL1Lcent was co-immunoprecipitated with the full-length SEL1L while the SLR motif 9 deletion failed to do so. (B) The HEK293T cells were transfected with the indicated plasmid constructs and the cell lysate and culture media were analyzed by western blot analysis and immunoprecipitation respectively.	FIG
+51	62	full-length	protein_state	Also, SEL1Lcent was co-immunoprecipitated with the full-length SEL1L while the SLR motif 9 deletion failed to do so. (B) The HEK293T cells were transfected with the indicated plasmid constructs and the cell lysate and culture media were analyzed by western blot analysis and immunoprecipitation respectively.	FIG
+63	68	SEL1L	protein	Also, SEL1Lcent was co-immunoprecipitated with the full-length SEL1L while the SLR motif 9 deletion failed to do so. (B) The HEK293T cells were transfected with the indicated plasmid constructs and the cell lysate and culture media were analyzed by western blot analysis and immunoprecipitation respectively.	FIG
+79	90	SLR motif 9	structure_element	Also, SEL1Lcent was co-immunoprecipitated with the full-length SEL1L while the SLR motif 9 deletion failed to do so. (B) The HEK293T cells were transfected with the indicated plasmid constructs and the cell lysate and culture media were analyzed by western blot analysis and immunoprecipitation respectively.	FIG
+91	99	deletion	experimental_method	Also, SEL1Lcent was co-immunoprecipitated with the full-length SEL1L while the SLR motif 9 deletion failed to do so. (B) The HEK293T cells were transfected with the indicated plasmid constructs and the cell lysate and culture media were analyzed by western blot analysis and immunoprecipitation respectively.	FIG
+249	261	western blot	experimental_method	Also, SEL1Lcent was co-immunoprecipitated with the full-length SEL1L while the SLR motif 9 deletion failed to do so. (B) The HEK293T cells were transfected with the indicated plasmid constructs and the cell lysate and culture media were analyzed by western blot analysis and immunoprecipitation respectively.	FIG
+275	294	immunoprecipitation	experimental_method	Also, SEL1Lcent was co-immunoprecipitated with the full-length SEL1L while the SLR motif 9 deletion failed to do so. (B) The HEK293T cells were transfected with the indicated plasmid constructs and the cell lysate and culture media were analyzed by western blot analysis and immunoprecipitation respectively.	FIG
+4	16	SEL1L348–497	mutant	The SEL1L348–497 fragment was secreted to the culture media but the SEL1Lcent was retained in the ER. (C) SEL1Lcent-FLAG-KDEL and SEL1L348–497-FLAG-KDEL localized to the ER.	FIG
+68	77	SEL1Lcent	structure_element	The SEL1L348–497 fragment was secreted to the culture media but the SEL1Lcent was retained in the ER. (C) SEL1Lcent-FLAG-KDEL and SEL1L348–497-FLAG-KDEL localized to the ER.	FIG
+106	125	SEL1Lcent-FLAG-KDEL	mutant	The SEL1L348–497 fragment was secreted to the culture media but the SEL1Lcent was retained in the ER. (C) SEL1Lcent-FLAG-KDEL and SEL1L348–497-FLAG-KDEL localized to the ER.	FIG
+130	152	SEL1L348–497-FLAG-KDEL	mutant	The SEL1L348–497 fragment was secreted to the culture media but the SEL1Lcent was retained in the ER. (C) SEL1Lcent-FLAG-KDEL and SEL1L348–497-FLAG-KDEL localized to the ER.	FIG
+4	9	SEL1L	protein	The SEL1L fragments were stained in red. (D) HEK293T cells were transfected with the indicated plasmid constructs and the lysates were immunoprecipitated with an anti-HA antibody followed by Western blot analysis using an anti-FLAG antibody.	FIG
+135	153	immunoprecipitated	experimental_method	The SEL1L fragments were stained in red. (D) HEK293T cells were transfected with the indicated plasmid constructs and the lysates were immunoprecipitated with an anti-HA antibody followed by Western blot analysis using an anti-FLAG antibody.	FIG
+167	169	HA	experimental_method	The SEL1L fragments were stained in red. (D) HEK293T cells were transfected with the indicated plasmid constructs and the lysates were immunoprecipitated with an anti-HA antibody followed by Western blot analysis using an anti-FLAG antibody.	FIG
+191	203	Western blot	experimental_method	The SEL1L fragments were stained in red. (D) HEK293T cells were transfected with the indicated plasmid constructs and the lysates were immunoprecipitated with an anti-HA antibody followed by Western blot analysis using an anti-FLAG antibody.	FIG
+227	231	FLAG	experimental_method	The SEL1L fragments were stained in red. (D) HEK293T cells were transfected with the indicated plasmid constructs and the lysates were immunoprecipitated with an anti-HA antibody followed by Western blot analysis using an anti-FLAG antibody.	FIG
+4	15	full-length	protein_state	The full-length SEL1L forms self-oligomers and the SEL1Lcent-FLAG-KDEL was co-immunoprecipitated with full-length SEL1L-HA.	FIG
+16	21	SEL1L	protein	The full-length SEL1L forms self-oligomers and the SEL1Lcent-FLAG-KDEL was co-immunoprecipitated with full-length SEL1L-HA.	FIG
+28	42	self-oligomers	oligomeric_state	The full-length SEL1L forms self-oligomers and the SEL1Lcent-FLAG-KDEL was co-immunoprecipitated with full-length SEL1L-HA.	FIG
+51	70	SEL1Lcent-FLAG-KDEL	mutant	The full-length SEL1L forms self-oligomers and the SEL1Lcent-FLAG-KDEL was co-immunoprecipitated with full-length SEL1L-HA.	FIG
+75	96	co-immunoprecipitated	experimental_method	The full-length SEL1L forms self-oligomers and the SEL1Lcent-FLAG-KDEL was co-immunoprecipitated with full-length SEL1L-HA.	FIG
+102	113	full-length	protein_state	The full-length SEL1L forms self-oligomers and the SEL1Lcent-FLAG-KDEL was co-immunoprecipitated with full-length SEL1L-HA.	FIG
+114	119	SEL1L	protein	The full-length SEL1L forms self-oligomers and the SEL1Lcent-FLAG-KDEL was co-immunoprecipitated with full-length SEL1L-HA.	FIG
+120	122	HA	experimental_method	The full-length SEL1L forms self-oligomers and the SEL1Lcent-FLAG-KDEL was co-immunoprecipitated with full-length SEL1L-HA.	FIG
+51	73	SEL1L348–497-FLAG-KDEL	mutant	The red asterisk indicates the expected signal for SEL1L348–497-FLAG-KDEL.	FIG
+0	22	SEL1L348–497-FLAG-KDEL	mutant	SEL1L348–497-FLAG-KDEL did not co-immunoprecipitate with full-length SEL1L-HA.	FIG
+57	68	full-length	protein_state	SEL1L348–497-FLAG-KDEL did not co-immunoprecipitate with full-length SEL1L-HA.	FIG
+69	74	SEL1L	protein	SEL1L348–497-FLAG-KDEL did not co-immunoprecipitate with full-length SEL1L-HA.	FIG
+75	77	HA	experimental_method	SEL1L348–497-FLAG-KDEL did not co-immunoprecipitate with full-length SEL1L-HA.	FIG
+53	70	SEL1Lcent-HA-KDEL	mutant	The white asterisks indicate non-specific bands. (E) SEL1Lcent-HA-KDEL competitively inhibited self-oligomerization of full-length SEL1L.	FIG
+119	130	full-length	protein_state	The white asterisks indicate non-specific bands. (E) SEL1Lcent-HA-KDEL competitively inhibited self-oligomerization of full-length SEL1L.	FIG
+131	136	SEL1L	protein	The white asterisks indicate non-specific bands. (E) SEL1Lcent-HA-KDEL competitively inhibited self-oligomerization of full-length SEL1L.	FIG
+54	79	immunoprecipitation assay	experimental_method	The indicated plasmid constructs were transfected and immunoprecipitation assay was performed using an anti-FLAG antibody followed by western blot analysis using an anti-HA antibody.	FIG
+108	112	FLAG	experimental_method	The indicated plasmid constructs were transfected and immunoprecipitation assay was performed using an anti-FLAG antibody followed by western blot analysis using an anti-HA antibody.	FIG
+134	146	western blot	experimental_method	The indicated plasmid constructs were transfected and immunoprecipitation assay was performed using an anti-FLAG antibody followed by western blot analysis using an anti-HA antibody.	FIG
+170	172	HA	experimental_method	The indicated plasmid constructs were transfected and immunoprecipitation assay was performed using an anti-FLAG antibody followed by western blot analysis using an anti-HA antibody.	FIG
+52	57	SEL1L	protein	The red rectangle indicates competitively inhibited SEL1L self-oligomer formation by the increasing doses of SEL1Lcent-HA-KDEL. (F) L521A point mutant in SEL1Lcent did not inhibit the self-association of SEL1L.	FIG
+63	71	oligomer	oligomeric_state	The red rectangle indicates competitively inhibited SEL1L self-oligomer formation by the increasing doses of SEL1Lcent-HA-KDEL. (F) L521A point mutant in SEL1Lcent did not inhibit the self-association of SEL1L.	FIG
+109	126	SEL1Lcent-HA-KDEL	mutant	The red rectangle indicates competitively inhibited SEL1L self-oligomer formation by the increasing doses of SEL1Lcent-HA-KDEL. (F) L521A point mutant in SEL1Lcent did not inhibit the self-association of SEL1L.	FIG
+132	137	L521A	mutant	The red rectangle indicates competitively inhibited SEL1L self-oligomer formation by the increasing doses of SEL1Lcent-HA-KDEL. (F) L521A point mutant in SEL1Lcent did not inhibit the self-association of SEL1L.	FIG
+138	150	point mutant	protein_state	The red rectangle indicates competitively inhibited SEL1L self-oligomer formation by the increasing doses of SEL1Lcent-HA-KDEL. (F) L521A point mutant in SEL1Lcent did not inhibit the self-association of SEL1L.	FIG
+154	163	SEL1Lcent	structure_element	The red rectangle indicates competitively inhibited SEL1L self-oligomer formation by the increasing doses of SEL1Lcent-HA-KDEL. (F) L521A point mutant in SEL1Lcent did not inhibit the self-association of SEL1L.	FIG
+204	209	SEL1L	protein	The red rectangle indicates competitively inhibited SEL1L self-oligomer formation by the increasing doses of SEL1Lcent-HA-KDEL. (F) L521A point mutant in SEL1Lcent did not inhibit the self-association of SEL1L.	FIG
+14	17	SLR	structure_element	Comparison of SLR in SEL1L with TPR or Other SLR-Containing Proteins.	FIG
+21	26	SEL1L	protein	Comparison of SLR in SEL1L with TPR or Other SLR-Containing Proteins.	FIG
+32	35	TPR	structure_element	Comparison of SLR in SEL1L with TPR or Other SLR-Containing Proteins.	FIG
+45	68	SLR-Containing Proteins	protein_type	Comparison of SLR in SEL1L with TPR or Other SLR-Containing Proteins.	FIG
+27	42	superimposition	experimental_method	(A) Ribbon diagram showing superimposition of an isolated TPR motif from Cdc23 and an SLR motif from SEL1Lcent (left), and SLR motifs in HcpC and SEL1Lcent (right).	FIG
+58	61	TPR	structure_element	(A) Ribbon diagram showing superimposition of an isolated TPR motif from Cdc23 and an SLR motif from SEL1Lcent (left), and SLR motifs in HcpC and SEL1Lcent (right).	FIG
+73	78	Cdc23	protein	(A) Ribbon diagram showing superimposition of an isolated TPR motif from Cdc23 and an SLR motif from SEL1Lcent (left), and SLR motifs in HcpC and SEL1Lcent (right).	FIG
+86	89	SLR	structure_element	(A) Ribbon diagram showing superimposition of an isolated TPR motif from Cdc23 and an SLR motif from SEL1Lcent (left), and SLR motifs in HcpC and SEL1Lcent (right).	FIG
+101	110	SEL1Lcent	structure_element	(A) Ribbon diagram showing superimposition of an isolated TPR motif from Cdc23 and an SLR motif from SEL1Lcent (left), and SLR motifs in HcpC and SEL1Lcent (right).	FIG
+123	126	SLR	structure_element	(A) Ribbon diagram showing superimposition of an isolated TPR motif from Cdc23 and an SLR motif from SEL1Lcent (left), and SLR motifs in HcpC and SEL1Lcent (right).	FIG
+137	141	HcpC	protein	(A) Ribbon diagram showing superimposition of an isolated TPR motif from Cdc23 and an SLR motif from SEL1Lcent (left), and SLR motifs in HcpC and SEL1Lcent (right).	FIG
+146	155	SEL1Lcent	structure_element	(A) Ribbon diagram showing superimposition of an isolated TPR motif from Cdc23 and an SLR motif from SEL1Lcent (left), and SLR motifs in HcpC and SEL1Lcent (right).	FIG
+4	9	SEL1L	protein	The SEL1L, Cdc23, and HcpC are colored magenta, green and cyan, respectively.	FIG
+11	16	Cdc23	protein	The SEL1L, Cdc23, and HcpC are colored magenta, green and cyan, respectively.	FIG
+22	26	HcpC	protein	The SEL1L, Cdc23, and HcpC are colored magenta, green and cyan, respectively.	FIG
+24	39	disulfide bonds	ptm	The red arrow indicates disulfide bonds in the HcpC, and Cys residues involved in disulfide bonding are shown by a yellow line. (B) Ribbon representation showing superimposition of Cdc23 and SEL1Lcent (left) or HcpC and SEL1Lcent (right) to compare the overall organization of the α-solenoid domain.	FIG
+47	51	HcpC	protein	The red arrow indicates disulfide bonds in the HcpC, and Cys residues involved in disulfide bonding are shown by a yellow line. (B) Ribbon representation showing superimposition of Cdc23 and SEL1Lcent (left) or HcpC and SEL1Lcent (right) to compare the overall organization of the α-solenoid domain.	FIG
+57	60	Cys	residue_name	The red arrow indicates disulfide bonds in the HcpC, and Cys residues involved in disulfide bonding are shown by a yellow line. (B) Ribbon representation showing superimposition of Cdc23 and SEL1Lcent (left) or HcpC and SEL1Lcent (right) to compare the overall organization of the α-solenoid domain.	FIG
+82	99	disulfide bonding	ptm	The red arrow indicates disulfide bonds in the HcpC, and Cys residues involved in disulfide bonding are shown by a yellow line. (B) Ribbon representation showing superimposition of Cdc23 and SEL1Lcent (left) or HcpC and SEL1Lcent (right) to compare the overall organization of the α-solenoid domain.	FIG
+162	177	superimposition	experimental_method	The red arrow indicates disulfide bonds in the HcpC, and Cys residues involved in disulfide bonding are shown by a yellow line. (B) Ribbon representation showing superimposition of Cdc23 and SEL1Lcent (left) or HcpC and SEL1Lcent (right) to compare the overall organization of the α-solenoid domain.	FIG
+181	186	Cdc23	protein	The red arrow indicates disulfide bonds in the HcpC, and Cys residues involved in disulfide bonding are shown by a yellow line. (B) Ribbon representation showing superimposition of Cdc23 and SEL1Lcent (left) or HcpC and SEL1Lcent (right) to compare the overall organization of the α-solenoid domain.	FIG
+191	200	SEL1Lcent	structure_element	The red arrow indicates disulfide bonds in the HcpC, and Cys residues involved in disulfide bonding are shown by a yellow line. (B) Ribbon representation showing superimposition of Cdc23 and SEL1Lcent (left) or HcpC and SEL1Lcent (right) to compare the overall organization of the α-solenoid domain.	FIG
+211	215	HcpC	protein	The red arrow indicates disulfide bonds in the HcpC, and Cys residues involved in disulfide bonding are shown by a yellow line. (B) Ribbon representation showing superimposition of Cdc23 and SEL1Lcent (left) or HcpC and SEL1Lcent (right) to compare the overall organization of the α-solenoid domain.	FIG
+220	229	SEL1Lcent	structure_element	The red arrow indicates disulfide bonds in the HcpC, and Cys residues involved in disulfide bonding are shown by a yellow line. (B) Ribbon representation showing superimposition of Cdc23 and SEL1Lcent (left) or HcpC and SEL1Lcent (right) to compare the overall organization of the α-solenoid domain.	FIG
+281	298	α-solenoid domain	structure_element	The red arrow indicates disulfide bonds in the HcpC, and Cys residues involved in disulfide bonding are shown by a yellow line. (B) Ribbon representation showing superimposition of Cdc23 and SEL1Lcent (left) or HcpC and SEL1Lcent (right) to compare the overall organization of the α-solenoid domain.	FIG
+5	14	SEL1Lcent	structure_element	Both SEL1Lcent schematics are identically oriented for comparison.	FIG
+37	54	α-solenoid domain	structure_element	The Cα atoms of the residues in each α-solenoid domain are superimposed with a root-mean-squared deviation of 3.3 Å for Cdc23 and SEL1Lcent (left), and 2.5 Å for HcpC and SEL1Lcent (right).	FIG
+59	71	superimposed	experimental_method	The Cα atoms of the residues in each α-solenoid domain are superimposed with a root-mean-squared deviation of 3.3 Å for Cdc23 and SEL1Lcent (left), and 2.5 Å for HcpC and SEL1Lcent (right).	FIG
+79	106	root-mean-squared deviation	evidence	The Cα atoms of the residues in each α-solenoid domain are superimposed with a root-mean-squared deviation of 3.3 Å for Cdc23 and SEL1Lcent (left), and 2.5 Å for HcpC and SEL1Lcent (right).	FIG
+120	125	Cdc23	protein	The Cα atoms of the residues in each α-solenoid domain are superimposed with a root-mean-squared deviation of 3.3 Å for Cdc23 and SEL1Lcent (left), and 2.5 Å for HcpC and SEL1Lcent (right).	FIG
+130	139	SEL1Lcent	structure_element	The Cα atoms of the residues in each α-solenoid domain are superimposed with a root-mean-squared deviation of 3.3 Å for Cdc23 and SEL1Lcent (left), and 2.5 Å for HcpC and SEL1Lcent (right).	FIG
+162	166	HcpC	protein	The Cα atoms of the residues in each α-solenoid domain are superimposed with a root-mean-squared deviation of 3.3 Å for Cdc23 and SEL1Lcent (left), and 2.5 Å for HcpC and SEL1Lcent (right).	FIG
+171	180	SEL1Lcent	structure_element	The Cα atoms of the residues in each α-solenoid domain are superimposed with a root-mean-squared deviation of 3.3 Å for Cdc23 and SEL1Lcent (left), and 2.5 Å for HcpC and SEL1Lcent (right).	FIG
+0	9	SEL1Lcent	structure_element	SEL1Lcent, Cdc23, and HcpC are colored as in (A). (C) Ribbon diagram showing the overall structure of Cdc23N-term (left) and SEL1Lcent (right) to compare their similarities regarding dimer formation through domain swapping.	FIG
+11	16	Cdc23	protein	SEL1Lcent, Cdc23, and HcpC are colored as in (A). (C) Ribbon diagram showing the overall structure of Cdc23N-term (left) and SEL1Lcent (right) to compare their similarities regarding dimer formation through domain swapping.	FIG
+22	26	HcpC	protein	SEL1Lcent, Cdc23, and HcpC are colored as in (A). (C) Ribbon diagram showing the overall structure of Cdc23N-term (left) and SEL1Lcent (right) to compare their similarities regarding dimer formation through domain swapping.	FIG
+89	98	structure	evidence	SEL1Lcent, Cdc23, and HcpC are colored as in (A). (C) Ribbon diagram showing the overall structure of Cdc23N-term (left) and SEL1Lcent (right) to compare their similarities regarding dimer formation through domain swapping.	FIG
+102	107	Cdc23	protein	SEL1Lcent, Cdc23, and HcpC are colored as in (A). (C) Ribbon diagram showing the overall structure of Cdc23N-term (left) and SEL1Lcent (right) to compare their similarities regarding dimer formation through domain swapping.	FIG
+125	134	SEL1Lcent	structure_element	SEL1Lcent, Cdc23, and HcpC are colored as in (A). (C) Ribbon diagram showing the overall structure of Cdc23N-term (left) and SEL1Lcent (right) to compare their similarities regarding dimer formation through domain swapping.	FIG
+183	188	dimer	oligomeric_state	SEL1Lcent, Cdc23, and HcpC are colored as in (A). (C) Ribbon diagram showing the overall structure of Cdc23N-term (left) and SEL1Lcent (right) to compare their similarities regarding dimer formation through domain swapping.	FIG
+12	17	SLR-C	structure_element	The Role of SLR-C in ERAD machinery and Model for the Organization of Proteins in Membrane-Associated ERAD Components.	FIG
+34	38	HRD1	protein	(A) Schematic diagram shows three HRD1 fragment constructs used in the GST pull-down experiment. (B) Pull-down experiments to examine the interactions between HRD luminal loops and certain SLR motifs of SEL1L.	FIG
+71	84	GST pull-down	experimental_method	(A) Schematic diagram shows three HRD1 fragment constructs used in the GST pull-down experiment. (B) Pull-down experiments to examine the interactions between HRD luminal loops and certain SLR motifs of SEL1L.	FIG
+101	122	Pull-down experiments	experimental_method	(A) Schematic diagram shows three HRD1 fragment constructs used in the GST pull-down experiment. (B) Pull-down experiments to examine the interactions between HRD luminal loops and certain SLR motifs of SEL1L.	FIG
+159	162	HRD	complex_assembly	(A) Schematic diagram shows three HRD1 fragment constructs used in the GST pull-down experiment. (B) Pull-down experiments to examine the interactions between HRD luminal loops and certain SLR motifs of SEL1L.	FIG
+163	176	luminal loops	structure_element	(A) Schematic diagram shows three HRD1 fragment constructs used in the GST pull-down experiment. (B) Pull-down experiments to examine the interactions between HRD luminal loops and certain SLR motifs of SEL1L.	FIG
+189	192	SLR	structure_element	(A) Schematic diagram shows three HRD1 fragment constructs used in the GST pull-down experiment. (B) Pull-down experiments to examine the interactions between HRD luminal loops and certain SLR motifs of SEL1L.	FIG
+203	208	SEL1L	protein	(A) Schematic diagram shows three HRD1 fragment constructs used in the GST pull-down experiment. (B) Pull-down experiments to examine the interactions between HRD luminal loops and certain SLR motifs of SEL1L.	FIG
+17	29	luminal loop	structure_element	Fragments of the luminal loop of HRD1 fused to GST were immobilized on glutathione sepharose beads and incubated with purified three clusters of SLR motifs and monomer form of SLR-M (SLR-ML521A, right panel) in SEL1L.	FIG
+33	37	HRD1	protein	Fragments of the luminal loop of HRD1 fused to GST were immobilized on glutathione sepharose beads and incubated with purified three clusters of SLR motifs and monomer form of SLR-M (SLR-ML521A, right panel) in SEL1L.	FIG
+47	50	GST	chemical	Fragments of the luminal loop of HRD1 fused to GST were immobilized on glutathione sepharose beads and incubated with purified three clusters of SLR motifs and monomer form of SLR-M (SLR-ML521A, right panel) in SEL1L.	FIG
+145	148	SLR	structure_element	Fragments of the luminal loop of HRD1 fused to GST were immobilized on glutathione sepharose beads and incubated with purified three clusters of SLR motifs and monomer form of SLR-M (SLR-ML521A, right panel) in SEL1L.	FIG
+160	167	monomer	oligomeric_state	Fragments of the luminal loop of HRD1 fused to GST were immobilized on glutathione sepharose beads and incubated with purified three clusters of SLR motifs and monomer form of SLR-M (SLR-ML521A, right panel) in SEL1L.	FIG
+176	181	SLR-M	structure_element	Fragments of the luminal loop of HRD1 fused to GST were immobilized on glutathione sepharose beads and incubated with purified three clusters of SLR motifs and monomer form of SLR-M (SLR-ML521A, right panel) in SEL1L.	FIG
+183	193	SLR-ML521A	mutant	Fragments of the luminal loop of HRD1 fused to GST were immobilized on glutathione sepharose beads and incubated with purified three clusters of SLR motifs and monomer form of SLR-M (SLR-ML521A, right panel) in SEL1L.	FIG
+211	216	SEL1L	protein	Fragments of the luminal loop of HRD1 fused to GST were immobilized on glutathione sepharose beads and incubated with purified three clusters of SLR motifs and monomer form of SLR-M (SLR-ML521A, right panel) in SEL1L.	FIG
+30	38	SDS-PAGE	experimental_method	Proteins were analyzed by 12% SDS-PAGE and Coomassie blue staining.	FIG
+52	60	metazoan	taxonomy_domain	(C) Schematic representation of the organization of metazoan ERAD components in the ER membrane.	FIG
+7	10	SLR	structure_element	The 11 SLR motifs of SEL1L were expressed with red cylinders and grouped into three parts (SLR-N, SLR-M, and SLR-C) based on the sequence alignment across the motifs and the crystal structure presented herein.	FIG
+21	26	SEL1L	protein	The 11 SLR motifs of SEL1L were expressed with red cylinders and grouped into three parts (SLR-N, SLR-M, and SLR-C) based on the sequence alignment across the motifs and the crystal structure presented herein.	FIG
+91	96	SLR-N	structure_element	The 11 SLR motifs of SEL1L were expressed with red cylinders and grouped into three parts (SLR-N, SLR-M, and SLR-C) based on the sequence alignment across the motifs and the crystal structure presented herein.	FIG
+98	103	SLR-M	structure_element	The 11 SLR motifs of SEL1L were expressed with red cylinders and grouped into three parts (SLR-N, SLR-M, and SLR-C) based on the sequence alignment across the motifs and the crystal structure presented herein.	FIG
+109	114	SLR-C	structure_element	The 11 SLR motifs of SEL1L were expressed with red cylinders and grouped into three parts (SLR-N, SLR-M, and SLR-C) based on the sequence alignment across the motifs and the crystal structure presented herein.	FIG
+129	147	sequence alignment	experimental_method	The 11 SLR motifs of SEL1L were expressed with red cylinders and grouped into three parts (SLR-N, SLR-M, and SLR-C) based on the sequence alignment across the motifs and the crystal structure presented herein.	FIG
+174	191	crystal structure	evidence	The 11 SLR motifs of SEL1L were expressed with red cylinders and grouped into three parts (SLR-N, SLR-M, and SLR-C) based on the sequence alignment across the motifs and the crystal structure presented herein.	FIG
+37	40	SLR	structure_element	We hypothesized that the interrupted SLR motifs of SEL1L have distinct functions such that the SLR-M is important for dimer formation of the protein, and SLR-C is involved in the interaction with HRD1 in the ER lumen.	FIG
+51	56	SEL1L	protein	We hypothesized that the interrupted SLR motifs of SEL1L have distinct functions such that the SLR-M is important for dimer formation of the protein, and SLR-C is involved in the interaction with HRD1 in the ER lumen.	FIG
+95	100	SLR-M	structure_element	We hypothesized that the interrupted SLR motifs of SEL1L have distinct functions such that the SLR-M is important for dimer formation of the protein, and SLR-C is involved in the interaction with HRD1 in the ER lumen.	FIG
+118	123	dimer	oligomeric_state	We hypothesized that the interrupted SLR motifs of SEL1L have distinct functions such that the SLR-M is important for dimer formation of the protein, and SLR-C is involved in the interaction with HRD1 in the ER lumen.	FIG
+154	159	SLR-C	structure_element	We hypothesized that the interrupted SLR motifs of SEL1L have distinct functions such that the SLR-M is important for dimer formation of the protein, and SLR-C is involved in the interaction with HRD1 in the ER lumen.	FIG
+196	200	HRD1	protein	We hypothesized that the interrupted SLR motifs of SEL1L have distinct functions such that the SLR-M is important for dimer formation of the protein, and SLR-C is involved in the interaction with HRD1 in the ER lumen.	FIG
+30	39	SEL1Lcent	structure_element	The surface representation of SEL1Lcent is placed in the same orientation as that shown in the schematic model to show that the putative N-glycosylation site, residue N427 (indicated in yellow), is exposed on the surface of the protein.	FIG
+137	157	N-glycosylation site	site	The surface representation of SEL1Lcent is placed in the same orientation as that shown in the schematic model to show that the putative N-glycosylation site, residue N427 (indicated in yellow), is exposed on the surface of the protein.	FIG
+167	171	N427	residue_name_number	The surface representation of SEL1Lcent is placed in the same orientation as that shown in the schematic model to show that the putative N-glycosylation site, residue N427 (indicated in yellow), is exposed on the surface of the protein.	FIG