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