wanglab/gogpt-training-data huggingface dataset:
Protein: Myotrophin homolog (Q55FM5)
Organism: Dictyostelium discoideum (Social amoeba)
Function: May regulate NF-kappa-B transcription factor activity. Plays a role in the regulation of the growth of actin filaments. Inhibits the activity of the F-actin-capping protein complex (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- F-actin-capping protein subunit beta
- Myosin-H heavy chain
Sequence:
MEEQNDFTWAVKNGDIANVKKSVEAKKDLISITDGNKRGPCHWAADFNQVEVLEYLISKGAKFDNTDDYGITPLLAAVYEGHTGAVELLVKKGANKSVVGPDGQTAYDAAEKADIKALLK
Protein: Protein CBFA2T2 (ETO homologous on chromosome 20) (MTG8-like protein) (MTG8-related protein 1) (Myeloid translocation-related protein 1) (p85) (O43439)
Organism: Homo sapiens (Human)
Function: Transcriptional corepressor which facilitates transcriptional repression via its association with DNA-binding transcription factors and recruitment of other corepressors and histone-modifying enzymes. Via association with PRDM14 is involved in regulation of embryonic stem cell (ESC) pluripotency. Involved in primordial germ cell (PCG) formation. Stabilizes PRDM14 and OCT4 on chromatin in a homooligomerization-dependent manner (By similarity). Can repress the expression of MMP7 in a ZBTB33-dependent manner. May function as a complex with the chimeric protein RUNX1/AML1-CBFA2T1/MTG8 (AML1-MTG8/ETO fusion protein) which is produced in acute myeloid leukemia with the chromosomal translocation t(8;21). May thus be involved in the repression of AML1-dependent transcription and the induction of G-CSF/CSF3-dependent cell growth. May be a tumor suppressor gene candidate involved in myeloid tumors with the deletion of the 20q11 region. Through heteromerization with CBFA2T3/MTG16 may be involved in regulation of the proliferation and the differentiation of erythroid progenitors by repressing the expression of TAL1 target genes (By similarity). Required for the maintenance of the secretory cell lineage in the small intestine. Can inhibit Notch signaling probably by association with RBPJ and may be involved in GFI1-mediated Paneth cell differentiation (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- PR domain zinc finger protein 14
- Runt-related transcription factor 1
- Protein CBFA2T3
- Protein CBFA2T1
- Putative histone-lysine N-methyltransferase PRDM6
Sequence:
MAKESGISLKEIQVLARQWKVGPEKRVPAMPGSPVEVKIQSRSSPPTMPPLPPINPGGPRPVSFTPTALSNGINHSPPTLNGAPSPPQRFSNGPASSTSSALTNQQLPATCGARQLSKLKRFLTTLQQFGNDISPEIGEKVRTLVLALVNSTVTIEEFHCKLQEATNFPLRPFVIPFLKANLPLLQRELLHCARAAKQTPSQYLAQHEHLLLNTSIASPADSSELLMEVHGNGKRPSPERREENSFDRDTIAPEPPAKRVCTISPAPRHSPALTVPLMNPGGQFHPTPPPLQHYTLEDIATSHLYREPNKMLEHREVRDRHHSLGLNGGYQDELVDHRLTEREWADEWKHLDHALNCIMEMVEKTRRSMAVLRRCQESDREELNYWKRRYNENTELRKTGTELVSRQHSPGSADSLSNDSQREFNSRPGTGYVPVEFWKKTEEAVNKVKIQAMSEVQKAVAEAEQKAFEVIATERARMEQTIADVKRQAAEDAFLVINEQEESTENCWNCGRKASETCSGCNIARYCGSFCQHKDWERHHRLCGQNLHGQSPHGQGRPLLPVGRGSSARSADCSVPSPALDKTSATTSRSSTPASVTAIDTNGL
Protein: AT2G34250 protein (At2g34250/F13P17.9) (SecY protein transport family protein) (O80774)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}. Plastid, chloroplast thylakoid membrane {ECO:0000256|ARBA:ARBA00004454}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004454}.
Interaction partners:
- Protein transport protein Sec61 subunit gamma-1
- Protein transport protein Sec61 subunit gamma-3
- Preprotein translocase subunit SCY1, chloroplastic
- Protein transport protein Sec61 subunit beta
- Protein transport protein Sec61 subunit beta
- Preprotein translocase Sec, Sec61-beta subunit protein
- Large ribosomal subunit protein uL18y
- Large ribosomal subunit protein uL23y
- Large ribosomal subunit protein uL23z
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
Sequence:
MGGGFRVLHLVRPFLAFLPEVQSADRKVPFREKVIYTVISLFIFLVCSQLPLYGIHSTTGADPFYWMRVILASNRGTVMELGITPIVTSGLVMQLLAGSKIIEVDNNVREDRALLNGAQKLLGILIAIGEAVAYVLSGMYGPVGQLGVGNAILIILQLFFAGIIVICLDELLQKGYGLGSGISLFIATNICESIIWKAFSPTTINTGRGAEFEGAVIALFHMLITKSNKVAALRQAFYRQNLPNVTNLLATVLIFLIVIYFQGFRVVLPVRSKNARGQQGSYPIKLFYTSNMPIILQSALVSNLYFISQLLYRKFSGNFFVNLLGQWKESEYSGQSIPVSGLAYLITAPASFSDMAAHPFHALFYIVFMLTACALFSKTWIEVSGSSARDVAKQLKEQQMVMPGHRESNLQKELNRYIPTAAAFGGVCIGALTVLADFMGAIGSGTGILLAVTIIYQYFETFEKEKASELGFFGF
Protein: Extracellular glycosidase CRH12 (EC 3.2.-.-) (Congo red hypersensitive protein 12) (Q5AK54)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Extracellular glycosidase which plays an important role in fungal pathogenesis. Involved in cell wall assembly and regeneration, filamentation, and adherence to host cells.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:16455273}. Membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP).
Interaction partners:
Sequence:
MYKQILTFLILFLRYILSEFPDDPYEDDDTSDDNNSDYEGQKCNPYRDKACLVNDEALGKKIFESFAEGTKYFTITSSTRGVRFGSEGLALTIQDEFDNPALVSSFYIMYGKVEAEIKGAAGKGIISSFYLQSDDLDEIDVVEIFGSDPYEFQTNFFIKGNTTTYDRGRYHEMHPSPLSEFHKYGIEWSPDLITWYLDDKPVRMLGRRNKHGLPCSPMFLKFSLWSVEDDDEGTIAWAGGAASFSEGPFTMHIKNLKVQDYSKALTYSYGNLRDGNWLDLRADGGYLYEGHKYCLPPKMLDKLKPTPKQETDDDQVLTSSKSQRVATTISEDKNTVSYYPPSATNSHTTWDRLSEWETEQDETGTDDTENSDNEEEESITAIPISKSRKGSTRRLDISTQLPPLSQNESKIAEIKNITTTKHIHNTTTSLQISKIKSKKVGVTTTIYSSSTPQSTSKSRMPYNIFFNYPGKENSRFKSGVSSILATSFSSVVIAEILVIVVLLL
Protein: Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member) (A0A6H2EEY2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU361195}. Nucleus {ECO:0000256|RuleBase:RU361195}.
Interaction partners:
Sequence:
MIFPREKKVLWRYASSNNPSNGVSAAPPAQPPRPPPPPHRPRPHQCTPSFGYSCNEEDSLAMRQTPLPPYSSIACGMDCSSSNSSSCGQSLSLSQGQGHNNNNSHPYRRLPNHMDVLPPPPSACDRCCTAPGYSCASSCDDMLIDGSDLDQDRSPDQGQVQPVDRRMISATTFTTMFRKCCGGATESTSGSTLTIPVSTSRATAHPPQTQAQNGKRFREDFEALMKQLKRKQRNELLLAVKSRLDPPTKTQRDVVEPTTTTAPTYLQCILIPCKTQTVWEPHVTASRLFFWRELWNAKELKRLPTCPAARDCIYMCCNPLHWFRILHQPETESPTPPYQRSKMLRLKDADFEEDSQNDAKSAALSTWSAESTSISNIYKPALYESVTTDGKDHNINSQVWCQIAYWEMAHRVGEFFHAKTNAVNIYTDGIVASEVDSMCLRDLTPAGNQIHSVVPKARHTVGLGVTLSLENGDVWIYNRGNTTIFVDSPTLSENLDRVCKVMPGYCLKAFETNRAELLSMRDHGHHPMGPVDYFSIKISFGKGWGRDYKRQDIMGCPCWLEVHFSHLRXQYLMLARSAGPHSASQHLVEPGMGCACDQVSSWRSRQLLQKAQKLLTRLCRQVCALTDYRPARTRWRCLAGRRSSRQLNTKQPIIWNNKGLQKKSF
Protein: Protein O-mannosyl-transferase TMTC1 (EC 2.4.1.109) (Transmembrane O-mannosyltransferase targeting cadherins 1) (Transmembrane and tetratricopeptide repeat-containing 1) (Q8IUR5)
Organism: Homo sapiens (Human)
Function: Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. The 4 members of the TMTC family are O-mannosyl-transferases dedicated primarily to the cadherin superfamily, each member seems to have a distinct role in decorating the cadherin domains with O-linked mannose glycans at specific regions. Also acts as O-mannosyl-transferase on other proteins such as PDIA3.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum {ECO:0000305}.
Interaction partners:
- D
- Guanine nucleotide-binding protein G
- Transcription factor COE1
- Transcription factor COE2
- Transcription factor COE4
- Olfactory marker protein
- Chaperone Ric-8B
- Glyoxylate reductase/hydroxypyruvate reductase
- Adenosine receptor A2a
- Adenylate cyclase type 3
Sequence:
MVVTTSARGGGGDRTPSRRRGCGLAPAGAAALLAGASCLCYGRSLQGEFVHDDVWAIVNNPDVRPGAPLRWGIFTNDFWGKGMAENTSHKSYRPLCVLTFKLNIFLTGMNPFYFHAVNIILHCLVTLVLMYTCDKTVFKNRGLAFVTALLFAVHPIHTEAVAGIVGRADVLACLLFLLAFLSYNRSLDQGCVGGSFPSTVSPFFLLLSLFLGTCAMLVKETGITVFGVCLVYDLFSLSNKQDKSSNGALCPRSPQQPGSPQPSSLPGHPHRENGKQQRFPHKGAWGGCHSPLPPEPKSSGFPVSPRAVWSMMRFLTYSYLLAFNVWLLLAPVTLCYDWQVGSIPLVETIWDMRNLATIFLAVVMALLSLHCLAAFKRLEHKEVLVGLLFLVFPFIPASNLFFRVGFVVAERVLYMPSMGYCILFVHGLSKLCTWLNRCGATTLIVSTVLLLLLFSWKTVKQNEIWLSRESLFRSGVQTLPHNAKVHYNYANFLKDQGRNKEAIYHYRTALKLYPRHASALNNLGTLTRDTAEAKMYYQRALQLHPQHNRALFNLGNLLKSQEKKEEAITLLKDSIKYGPEFADAYSSLASLLAEQERFKEAEEIYQTGIKNCPDSSDLHNNYGVFLVDTGLPEKAVAHYQQAIKLSPSHHVAMVNLGRLYRSLGENSMAEEWYKRALQVAHKAEILSPLGALYYNTGRYEEALQIYQEAAALQPSQRELRLALAQVLAVMGQTKEAEKMTNHIVSEETGCLECYRLLSAIYSKQENHDKALDAIDKALQLKPKDPKVISELFFTKGNQLREQNLLDKAFESYRVAVQLNPDQAQAWMNMGGIQHIKGKYVSARAYYERALQLVPDSKLLKENLAKLDRLEKRLQEVREKDQT
Protein: Zinc finger BED domain-containing protein RICESLEEPER 3 (Transposase-like protein RICESLEEPER 3) (Q75HY5)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transposase-like protein that is essential for plant growth and development. May regulate global gene expression by recruiting other cellular factors.
Subcellular location: Nucleus {ECO:0000269|PubMed:23067104}.
Interaction partners:
Sequence:
MCEPSGSDDAMVHASEMVDGDEMIHGNEMVVHDSVMIDGNEMVQENVMVHGSGEMVQGSEMVHNNEIIQVNDMIQVNEMVNGDKMAHGHELVGVELTTPTASRRRRKKSVVWEHFTIEEMPGGVSRASCNLCKQTFAYSCGSKISGTSHLKRHITLASCPMLKNEDMKLSLPLATVTNNDGEGCAERVAKRHYRSTGYANAMFDQDRTCSNLAKMIILHDYPLHIVEQRGFTAFIGSLQPRFRVIDVDTIEGQVHSVYQKERENLMHVFSTVPGRISLTVRLWATSQTLGYISLAAQFIDTEWRVHRRMVNFMMVSSPHSENSLSEAISTSLSDWNMKDKLFTITLDNDPSSHDIYSANMINYLSNKKDNIMIKGQLFVVRCYAHILNTVAQDVIASVHSVIYHIRESIKFIKASSVHEDKFAEIALQLEIPSAKTLCLDVTTQWNTTYLMLLAALDYQQVFASLETCDGDYNEAPSTEDWKKVEAACSYLSLLYDSAHNIMAAPNPTSNIFFHEAWKLQSELSNAIAHEDPIFRSTAKIMHERFDKYWKDCNLVLAIAVVMDPRFKMKLVEFSYSKIHSVEAAKYVKVVDDAIHELYSEYATQGEANRDAHVTDNSAAVTPPNGDELLDFDIYLSEIATSQPSISELEQYLEEALMPRIQDFEILEWWKLNTIKFPTLSKMARDVLAIPMSMVSSGSSIFSATATGSQMLDDYRSSLRPETVEALFCAKDWLQYPPATTEAPSTALVKMEN
Protein: CCR4-NOT transcription complex subunit 11 (Q38B44)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MHHTGMPNTPPRASQPRYNWLADNRALTQVLTHSDNMGRLPVDIVRDAVCGGVVCAFTDEKNRYDDQVFLPSSCDLTALAFLISEGFFAPFLHRTVGDWFQQYTILTESGFFEPLSIPVLLFPDCFYDASFIDTSLPRVLSPTPSTNGSISSMPSDSISSTAADVLHLHNLRLQVGVLLLKSINEVLRDAEVWKLKANRQKRGQTPPSDVVVANAVIALFYEVKMLLLCCIISTEQAYPKDGSHEETPFKSARSYFESIFSTKELRRIFEERSRPGAEEVMRWFDSTLGALTSTVSGLFSSLQERLQELLNDVSVDGRRVTGTPVQILHRPHDSTSTNVLQLPFVQSKLPHLPLQTGELATLLSPNPGEMLLCDSVPSPLSLLLRRCATVKMSALELRDGVEQLAMNPWWALHYAASQTVQRQLSDTQFIRSAVGKNSCFLIEIVRWLRDVPSDEAKDVAKERGSACSNSEGTKQQNGRTNGESNREQRLLLGLSTSNEIIDHVVHDLPFGTAVAQLIRELVGSNLFTEEQLHRWIGRSLKDVESKPPATIGCFAALLVFVLLHSRWELPADIREMTVQLCSQNKQQQDCVQLINILQRGA
Protein: Deoxyguanosine kinase (D3ZDE4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- 5',3'-nucleotidase, mitochondrial
- Purine nucleoside phosphorylase
- Cytosolic purine 5'-nucleotidase
- 5'-nucleotidase
- 7-methylguanosine phosphate-specific 5'-nucleotidase
- 5'-nucleotidase
- Guanylate kinase
- Inosine triphosphate pyrophosphatase
- 5'-nucleotidase, cytosolic IA
- NADH dehydrogenase flavoprotein 1, mitochondrial
Sequence:
MAAGRFLLRRLRASFRSQPRNALVDAPRARGMHDGGGPRRLCIEGNIAVGKSTFVKLLTKTHPEWQVATEPIATWQNVQAAGTQKDSTSRRLGNLLDMMYQEPARWSYTFQTLSFMSRLKVQLEPTPGRLLQADTSVRVFERSVYSDRYIFAKNLFENGSLSDVEWHIYQDWHSFLLQEFEDRLLLHGFIYLQASPQVCMERLCQRGREEEKGIELAYLKQLHGQHEDWFINKTTKLHFEALRHVPVLVLNISEDFSENAAKQEELMGQQGDSDNRRE
Protein: Minor fimbrium tip subunit Mfa3 (B2RHG3)
Organism: Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561)
Function: Tip subunit of the minor fimbriae. These filamentous pili are attached to the cell surface; they mediate biofilm formation, adhesion onto host cells and onto other bacteria that are part of the oral microbiome. They play an important role in invasion of periodontal tissues and are recognized as major virulence factors. Fimbrium subunits from different strains have highly divergent sequences, and this correlates with pathogenicity (Probable).
Subcellular location: Fimbrium {ECO:0000269|PubMed:19589838, ECO:0000269|PubMed:24118823, ECO:0000269|PubMed:26001707}. Cell outer membrane {ECO:0000269|PubMed:24118823, ECO:0000269|PubMed:26437277}. Note=Targeted to the outer membrane as a palmitoylated precursor. The lipid modification is no longer present after proteolytic processing to the mature form (PubMed:26437277). Detected at the tip of the fimbriae (PubMed:24118823). {ECO:0000269|PubMed:24118823, ECO:0000305|PubMed:26437277}.
Interaction partners:
Sequence:
MMQLKKRYFALILLLFLWSGCDRGVDPQPDPLQPDVYLLVNARAAHTNGEESINMDAEDFEDRVHSLAMLVFDSNTGEKVAEHFSSSIGSGTSTYVFTVKLKPGQRDFFFVANIPNMQTAMASIVNKSDMNHFMQVFRDLDPIHYHNATNNNGFPMSRMYSNQTVTIGGTITQPLPFKPDGENNVKLQRVVAKLDVNIVEGVENLQKIELCNANVHYRLVPNQSEPIQFYGPVELRRVGATNQWLGYMPEAIVESTKWWGNTGNAENKPINFFRLTTRGGLVYDVPIITHEGAIPGGQYLPFAKGLLADKPSYTVYRNRHYIYRIKTLPDKIEVKYSICDWNIVTNDTYMGYGYNVGVDEQGNVTITNTMQNCDPHVVRLVAKNGAYFGSQPTDTSVEFTELANGASQTFKVNKDAVAVGSAYLEVYYNPDLNATGVVPDKVFIKK
Protein: SLC15A3 protein (Q05CH4)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MPAPRAREQPRVPGERQPLLPRGARGPRRWRRAAGAAVLLVEMLERAAFFGVTANLVLYLNSTNFNWTGEQATRAALVFLGASYLLAPVGGWLADVYLGRYRAVALSLLLYLAASGLLPATAFPDGRSSFCGEMPASPLGPACPSAGCPRSSPSPYCAPVLYAGLLLLGLAASSVRSNLTSFGADQVMDLGRDATRRFFNWFTGASTWVLCCRCWWWRLFSRTSASCWATASLWAVWAWHFSSSSLPPPSSSPSPRWAAKCPLCLSSLSKTAAPSCGNDTRPETVNVPACWPTRGLPSQGLPRKRTSPTSRCW
Protein: ATP-binding cassette sub-family D member 2 (EC 3.1.2.-) (EC 7.6.2.-) (Adrenoleukodystrophy-related protein) (Q61285)
Organism: Mus musculus (Mouse)
Function: ATP-dependent transporter of the ATP-binding cassette (ABC) family involved in the transport of very long chain fatty acid (VLCFA)-CoA from the cytosol to the peroxisome lumen (By similarity). Like ABCD1 seems to have fatty acyl-CoA thioesterase (ACOT) and ATPase activities, according to this model, VLCFA-CoA as free VLCFA is transpoted in an ATP-dependent manner into peroxisomes after the hydrolysis of VLCFA-CoA mediated by the ACOT activity of ABCD2 (By similarity). Shows overlapping substrate specificities with ABCD1 toward saturated fatty acids (FA) and monounsaturated FA (MUFA) but has a distinct substrate preference for shorter VLCFA (C22:0) and polyunsaturated fatty acid (PUFA) such as C22:6-CoA and C24:6-CoA (in vitro) (By similarity). Thus, may play a role in regulation of VLCFAs and energy metabolism namely, in the degradation and biosynthesis of fatty acids by beta-oxidation.
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:8577752}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- ATP-binding cassette sub-family D member 3
- ATP-binding cassette sub-family D member 1
- Peroxisomal biogenesis factor 19
- Peroxisomal membrane protein 11B
- Peroxisomal membrane protein PMP34
- Peroxisomal membrane protein PEX13
- Peroxisomal membrane protein 4
- Peroxisomal membrane protein PEX16
- Peroxisome assembly protein 12
Sequence:
MIHMLNAAAYRVKWTRSGAAKRAACLVAAAYALKTLYPIIGKRLKQPGHRKAKAEAYSPAENREILHCTEIICKKPAPGLNAAFFKQLLELRKILFPKLVTTETGWLCLHSVALISRTFLSIYVAGLDGKIVKSIVEKKPRTFIIKLIKWLMIAIPATFVNSAIRYLECKLALAFRTRLVDHAYETYFANQTYYKVINMDGRLANPDQSLTEDIMMFSQSVAHLYSNLTKPILDVILTSYTLIRTATSRGASPIGPTLLAGLVVYATAKVLKACSPKFGSLVAEEAHRKGYLRYVHSRIIANVEEIAFYRGHKVEMKQLQKCYKALAYQMNLILSKRLWYIMIEQFLMKYVWSSCGLIMVAIPIITATGFADGDLEDGPKQAMVSDRTEAFTTARNLLASGADAIERIMSSYKEITELAGYTARVYNMFWVFDEVKRGIYKRTVTQEPENHSKRGGNLELPLSDTLAIKGTVIDVDHGIICENVPIITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQRPYMSLGSLRDQVIYPDSADDMREKGYTDQDLERILHSVHLYHIVQREGGWDAVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKIFQAAIGAGISLLSITHRPSLWKYHTHLLQFDGEGGWRFEQLDTAIRLTLSEEKQKLESQLAGIPKMQQRLNELCKILGEDSVLKTIQTAEKTS
Protein: N-fatty-acyl-amino acid synthase/hydrolase PM20D1 (EC 3.5.1.114) (EC 3.5.1.14) (Peptidase M20 domain-containing protein 1) (PM20D1) (Q8C165)
Organism: Mus musculus (Mouse)
Function: Secreted enzyme that regulates the endogenous N-fatty acyl amino acid (NAAs) tissue and circulating levels by functioning as a bidirectional NAA synthase/hydrolase. It condenses free fatty acids and free amino acids to generate NAAs and bidirectionally catalyzes the reverse hydrolysis reaction (Probable). Some of these NAAs stimulate oxidative metabolism via mitochondrial uncoupling, increasing energy expenditure in a UPC1-independent manner. Thereby, this secreted protein may indirectly regulate whole body energy expenditure. PM20D1 circulates in tight association with both low- and high-density (LDL and HDL,respectively) lipoprotein particles.
Subcellular location: Secreted {ECO:0000269|PubMed:27374330, ECO:0000269|PubMed:32271712, ECO:0000269|PubMed:32402239}.
Interaction partners:
- Nuclear ubiquitous casein and cyclin-dependent kinase substrate 1
Sequence:
MAELLASLPAWAAVLLLFFATVSGSTGPRSRENRGASRIPSQFSEEERVAIKEALKGAIQIPTVSFSHEESNTTALAEFGEYIRKAFPTVFHSSLVQHEVVAKYSHLFTIQGSDPSLQPYMLMAHIDVVPAPEEGWEVPPFSGLERNGFIYGRGALDNKNSVMAILHALELLLIRNYSPKRSFFIALGHDEEVSGEKGAQKISALLQARGVQLAFLVDEGSFILEGFIPNLEKPVAMISVTEKGALDLMLQVNMTPGHSSAPPKETSIGILSAAVSRLEQTPMPNMFGGGPLKKTMKLLANEFSFPINIVLRNLWLFHPIVSRIMERNPITNALVRTTTALTMFNAGIKVNVIPPLAQATINCRIHPSQTVHEVLELVKNTVADDRVQLHVLRSFEPLPISPSDDQAMGYQLLQETIRSVFPEVDIVVPGICIANTDTRHYANITNGMYRFNPLPLNPQDFSGVHGINEKVSVQNYQNQVKFIFEFIQNADTYKEPVPHLHEL
Protein: Lectin, mannose-binding 2-like a (Lectin, mannose-binding 2-like a precursor) (Q4QRF6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MIWASALIFITALSSGVCDDGHEMEEFLKREYTLSKPYQDVGVSGSSHWELMGDALVSSDYVRLTPDQQSKQGAIWSRMPCHLSDWELQVHFRVHGQGKKNLNGDGLAVWYTKERMQRGPVFGNRDFFTGLGVFVDTYPNEEKLLEAQKKRYTPRTQRIFPYVLAMVGNGSISYDHDRDGRPTELGGCNAMVRNQKHETFLFIRYVRRRLTVMMDIDGQHEWRDCLDVPGVRLPQGFYFGASAVTGDLSDNHDLISMKLYQLTILRSKQEDEEQEEVLVPSVDNIDLLRPPVDEESVSSVGIFFSVLFTLLGVFLLVVVGLVLYEHWSESRRKRFY
Protein: Cytoskeletal signaling protein slm1 (O94447)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Effector of the TORC2- and calcineurin-signaling pathways. Mediates actin polarization via inhibition of calcineurin-dependent transcription (By similarity).
Subcellular location: Cell tip {ECO:0000269|PubMed:21900489}.
Interaction partners:
- Probable sphingolipid long chain base-responsive protein pil1
- Large ribosomal subunit protein uL22m
- Large ribosomal subunit protein uL15m
- Small ribosomal subunit protein uS15m
- Translation initiation factor IF-2, mitochondrial
- Small ribosomal subunit protein uS14m
- Meiotically up-regulated gene 33 protein
- Large ribosomal subunit protein uL3m
- Target of rapamycin complex 2 subunit bit61
- Large ribosomal subunit protein uL11m
Sequence:
MELSGKSEFPTRTEIPNQASNGDAVPNTDAYMGLCNSLTYRFEGWRHLVENLIAFFKQLESTSKNNAKEYMKLSKVIVHPYKDANVFEEHGIQDIFAALRDQTAAIASDSEQISIQLPGTIINILELLREDLREHCKKIAAEGTKGVKVVEKQRAETQKYLSLLDRALLPWRASSPPTVNIKNDPFIVDRQVLNCLARQVQEENNHSVAVAQLQEFSFRFEQNLIAKIKDTVKQFEGMMNQTHVKAINHLQEVVRVSEAQTLAGEWTGYAKREPEFIHGSVPPRSVDAIKYPGKNDQPTVPIMAGYLIRKTSFLKKKQRGFYAFTHSGYLYEFKSSDSLQDPEPEFALYIPDCLIGRPSEKKPKFKITGKDATKKIFGARNDYAFRASNNTELMRWWEALNTHIANVNYIQPLSNANGPSAVSDSDDDDDDPNDFRPAVERQSSTMNTRMSQPSSAVNTNRSYGSEQIPSYADSQGNSGANNNFIYNASATGHNAWNV
Protein: ATP-dependent Clp protease proteolytic subunit (Q8IL98)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- ATP-dependent protease subunit ClpQ
- ATP-dependent protease ATPase subunit ClpY
- Heat shock protein 101
- Chaperone protein ClpB1
- Clp
- ATP-dependent Clp protease regulatory subunit ClpC
Sequence:
MQGLLLFMLICINFCKCTKIITRYNFITNKINIKRYKKKNNNKSPLYYSYNEHHKYNINIPSLLLSKRIIFLSSPIYPHISEQIISQLLYLEYESKRKPIHLYINSTGDIDNNKIINLNGITDVISIVDVINYISSDVYTYCLGKAYGIACILASSGKKGYRFSLKNSSFCLNQSYSIIPFNQATNIEIQNKEIMNTKKKVIEIISKNTEKDTNVISNVLERDKYFNADEAVDFKLIDHILEKE
Protein: UDP-glucuronosyltransferase (Q13460)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MARTGWTSPIPLCVSLLLTCGFAEAGKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMPEVSWQLGKSLNCTVKTYSTSYTLEDLDREFMDFADAQWKAQVRSLFSLFLSSSNGFFNLFFSHCRSLFNDRKLVEYLKESSFDAVFLDPFDACALIVAKYFSLPSVVFARGIGCHYLEEGAQCPAPLSYVPRILLGFSDAMTFKERVRNHIMHLEEHLFCQYFSKNALEIASEILQTPVTAYDLYSHTSIWLLRTDFVLDYPKPVMPNMIFIGGINCHQGKPLPMVSHLSFSTLGIILALEIKKRFLTEL
Protein: Ifr2p (A0A1D8PSE7)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MKAAVVPESVTETKLAEVKEIPKPTIGDDQILIKAEAAAVNPTDWKHIVFQMSKPGDVIGSDVSGTVEEVGSKVTNFKKGDTVSSFIIGNISPDSGAFGEYVIAYPQATIKYDHSLSHSSATNSSTIKSYEGAASVTLGLSTIGISFSHYLNIGKHKKEGDSILIWGGATATGILAIQVAKLVYNLNVITTASPKNHAFLKELGADHTLDYNDPNVIENLKALGPIKFGLDTIANTTTFQGLYDATAGTPEVYLDSLLGLDGKSIKTDPSRENSVHWGYTLAYLCVIKEKSFGPTKFVQTPELVDDYLKWWNEVLPTFIGKIKHANLKILGDGLASANEALQLSRDSKVSAQKIVFTV
Protein: WAT1-related protein At4g19185 (Q8W4R9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MTAPMILTGSGSAAERDARMAHTAMAFVQLFNGGYHVITKVALNVGVNQLVFCVCRDLLALSILAPLAYFRERKIRTPMNKSLLLSFFFLGLAGVFGNQLLFLIGLTYTNPTYAAAIQPSIPVFTFLLAVMMGTERVNLLRIEGQTKVGGTLVCVMGAVFMVVFRGPALLGDKDADFAMNNEISAKGQPEPTGWLVSGFLDLGFEQWHIGVLCLIGNCMCMATFLAIQAPLLKKYPANLSVAALSYFFGTVLMCTTAFFMVKEPLDWKLTQSEVLAVIYAGVIASALNYGLLTWSNKIIGPALVALYNPLQPAASAFLSRIFLGSPIYLGSVVGGFFIILGLYMVTWASFRERKTAVSGIGIAPHGLKTSEPLIFNGTVNRLGQLFSGLPSSSVKSAD
Protein: C2H2-type domain-containing protein (Q0PCD8)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MSYHYQMNNNNTDFFDSANYIPQMQMHHGYQDFYASDSTSSMPSSGTTQQALQQTENGIIQGQNGSDHGAYGGWRQHDWNSTSSWSIGNQLEMENGTLTMSHGATNDGNIRNNQQMMTSNHITTDSFRQIPPSGLCYMDPTPSLRLPKKEPLPVQRPMARSTPKPFRCQTCGKAFSQAANLTAHKRIHTGEKPFMCPVCNRPFSQSSSLVTHRRTHTGERPYPCAQCEKAFTDSSTLTKHLRTHTGHKPYVCSICMMKFTQSGNLHRHMKTHK
Protein: Nuclear pore membrane glycoprotein 210-like (Nucleoporin 210 kDa-like) (Nucleoporin Nup210-like) (Q9D2F7)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Nuclear pore membrane glycoprotein 210
- Nuclear pore complex protein Nup107
- Nuclear pore complex protein Nup160
- Nucleoporin NUP35
- Nuclear pore complex protein Nup133
- Nuclear pore complex protein Nup155
Sequence:
MIAFGAPRRRSFGLLFSLAPHLFFLFLIGTLANKLNVPQVLLPFSREPGRVPFLLEAQRGCYIWHSTHHDAVTIQPLYENGTSCSQRAVLVAESTQPIRLSSIILAREVVTDHELRCDVKVDVIDNIEIVSRTRELYVDDAPLELMVRALDSKGNTFSTLAGMVFEWSIAQDNESSREELSSKIRILKYSEAEYSPPDYIIEMEKQERQGDVILVSGMRTGAAVVKVRIYEPFYKKVAAALIRLLVLENIFLIPSHDTYLLVGAYIKYRVAKMVQGRMTEVNFPLEHYTLELQDHRLTNGGLPSKSVALLDEKTAMVTAVQLGQTNLVFVHKNVHMRSVSGLPNSTIYVVEPGFLGFSIHPGGRWSLEVGQVYVITVEVFDKSSTRVYISDNLKITFQFSKEYFEEQLSTSNGSYHVVKALKDGVVVINATLTSSLQERNSSQPKTYQISHQQEVKIYFPIQLKPSFLAFPHHPLGISNRFTVQVEGGSGNFTWSSSNETVAMVTTKGVVTAGQVRGNSTILARDVQNPSRSGDIKVYVMKLNKMELLPFQADVEIGQIIEVPIAMYHVNTETKEAIAFTDCSHLPLDLNSDKQGVFTLFKEGIQKPGAMHCSSVHIAATSPGHTLVTVSVTGHEEHAWSSATFAAYEPLKALNPVDVALVTWQSVKEMVFEGGPHPWILEPSRFFLELSMEKAEAIRVAEVRLPAKRKQNQYVYRVLCLELGEQVLTFRIGNHPGVLNPSPSVEKVQVRFICAHPASMLVTPMYKAPSGTQPCPLPQYNKQLIPVSSLRDSVLELAVFDQHGRKFDNFSSLMLEWKSSNETLAHFEDSKSVEMVARDDGSGQTRLHGHQILKVHQMKGTVLIGVNFAGYSGKKSPKGISNSPRSAGVELILVEDVTVQPENATIYNHPDVKEIFNLVEGSGYFLINSSEQDIVTITYREAESSVQLVPAHPGFLTLEVYDLCLAYLGPAVAQIRVSDIQELELDLIDKVEIGKTVLVVVRVLGSSKHPFRNKYFRNMEVRLQLASAIVTLRLMEDQDEYSENYMLRAVTVGQTTLVAIATDRMGKKFTSAPRHIEVFPPFRLIPEKMTLIATNMMQIMSEGGPQPQSIIHFSISNQTVAVVNRRGQVTGKSVGTAVLHGTIQTVNEDTGKVIVFSQDEVQIEVVQLQAVRILAAATRLVTATEMPVYVMGVTSTQTPFSFSNASPLLTFHWSMSKRDVLDLVPRHSEVFLQLPAENNFAMVVHTKAAGRTTIKVTVRSENSSSGQLEGNLLELSDEIQILVFEKLQLFYANCQPEQILMPMNSQLKLHTNREGAAFVSSRVLKCFPNSSVIEEDGGGLLRSGSIAGTAVLEVTSIEPFGVNQTTITGVQVAPVTYLRLSSYPKLYTAQGRTLSAFPLGMSLTFIVEFYNNIGEKFHTHNTRLYMALNRDDLLLIGPGNRNYTYMAQAVNKGVTVVGLWDQRHPGMADYIPVAVEHAIEPDTKLIFVGDVICFSTQLVNQHGEPGVWMISTNNIVQTDTATGVGVARNPGTATIFHNIPGVVKTFREVVVNASSRLTLSYDLKTYLTNTPNATAFKLFISTGRNVNLKGSCTPSQALAIEKVLLPETLMLCHVQFSNTLLDIPASKVFHIHSEFSVEKGVYVCLIKVRQESKELRQVLSVADTSVYGWATLVSERGKNGMQRILIPFIPGFYMNQSEFVLGHKDTGELRILGVERVLESLEVFHSSPFLAVSGYKHSMLTTGLTVYLVRIVNFTAFQQMSSPAFINVSCALTNQQEAVIVRAKDASGADHCEDSGVFKNFVGSYQILLFTLFAVLASTSFIFLAHNAFLNKVQTIPVVYVPTTGTTQPGSYTATCSPPHFLSSRPPLVQSRLQHWLWSIKH