wanglab/gogpt-training-data huggingface dataset:
Protein: Peroxisomal targeting signal 2 receptor (PTS2 receptor) (Peroxin-7) (O59894)
Organism: Komagataella pastoris (Yeast) (Pichia pastoris)
Function: Receptor required for the peroxisomal import of proteins containing a C-terminal PTS2-type peroxisomal targeting signal, such as 3-oxoacyl-CoA thiolase (By similarity). Specifically binds to cargo proteins containing a PTS2 peroxisomal targeting signal in the cytosol (By similarity). Cargo protein-binding triggers interaction with PEX20 and formation of a ternary complex composed of PEX20 and PEX7 along with PTS2-containing cargo proteins, which is tranlocated into peroxisomes by passing through the PEX13-PEX14 docking complex (By similarity). PEX7 receptor is then retrotranslocated into the cytosol, where it is ubiquitinated and degraded.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:25009284, ECO:0000269|PubMed:9472033}. Peroxisome matrix {ECO:0000269|PubMed:25009284, ECO:0000269|PubMed:9472033}.
Interaction partners:
Sequence:
MFKFQTNGFSGYAVRYSPFYDNKIAVATSANYGLVGNGRLYVLSIMDDGNIITDISYDTQDGLFGVAWSETNENHVLTSSGDGCVSLFDTTLKDYPVMKFTEHQREVFSVDWSNIDKNLFCSASWDGSVKVWSPGSNRNTSLLTLRSLASREEKTGRIEKPIPVVQPSQVPMSKTRPNIRNDNNDCVYDAKFSFHDPNIIMSCNSDSHLQLWDTRLPNPLFMDFVAHNGLEALSCDFNRYRPFVVASAGVDKLAKVWDTRMIQPNVHSRPPRALNKFMGHEFAIRKLAWSPHGPTQLLTCSYDMTVRVWNDSPSPTSRVGLLDGASQPHAPPCSKIFSAHTEFVMGCDWSLWGEPGWVVTTGWDEMVYVWNTQRLQ
Protein: Mediator of RNA polymerase II transcription subunit 10 (Mediator complex subunit 10) (D4A7K6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU364146}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 21
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 19
- Mediator complex subunit 12
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 11
Sequence:
MAEKFDHLEEHLEKFVENIRQLGIIVSDFQPSSQAGLSQKLNFIVTGLQDIDKCRQQLHDITVPLEVFEYIDQGRNPQLYTKECLERALAKNEQVKGKIDTMKKFKSLLIQELSKVFPEDMAKYRSIRGEDHPPS
Protein: Retinoblastoma-like protein 2 (130 kDa retinoblastoma-associated protein) (p130) (PPAR-alpha-interacting complex protein 128) (PRIC128) (Retinoblastoma-related protein 2) (RBR-2) (pRb2) (O55081)
Organism: Rattus norvegicus (Rat)
Function: Key regulator of entry into cell division. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases KMT5B and KMT5C, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Probably acts as a transcription repressor by recruiting chromatin-modifying enzymes to promoters. Potent inhibitor of E2F-mediated trans-activation, associates preferentially with E2F5. Binds to cyclins A and E. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein. May act as a tumor suppressor (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- E2F transcription factor 4
- Transcription factor E2F5
- Cyclin-dependent kinase 2
- E2F transcription factor 3
- Transcription factor E2F1
- Transcription factor
- cyclin-dependent kinase
- Transcription factor
- Cyclin-dependent kinase 4
- G1/S-specific cyclin-D2
Sequence:
MASGGNQSSPPPPAAAASSEEEEEDGDTADRAQPAGSPSHQIQQRFEELCSRLNMDEAARAEAWSSYRSMSESYTLEGNDLHWLACALYVACRKSVPTVSKGTAEGNYVSLTRILRCSEQSLIEFFNKMKKWEDMANLPPHFRERTERLERNFTVSAVIFKKYEPIFQDIFKYPQEEQPRQQRGRKQRRQPCTTSEIFHFCWVLFIYAKGNFPMISDDLVNSYHLLLCALDLVYGNALQCSNRKELVNPNFKGVSEDGHPRDSHPSSDPPCVIEKLCSLHDGLVLEAKGIKQHFWKPYIRKLFEKKLLRGKEENLTGFLEPGNFAESFKAVNKAYEEYVLATGSLDERIFLGEDAEEEVGTFSRCVSAASGTESAERTQMRDILQQHLDKSKTLRVCNPLTGVRYVQENSPCVTPVSTATHSLNRLHTMLAGLRNAPSEKLEQILRSCSRDPTRAIADRLREMYEIYSQHFQPDENVSNCAKEMANKHFRFAEMLYYKVLESVIEQEQKRLGDMDLSGVLEQDAFHKSLLACCLEVVAFSYKPPGNFPFIAEIFDVPHYHFYKVIEVFIRAEDGLCREVVKHLNQIEEQILDHLAWKTKSPLWDRIRDNENRVPTCEEVTPPHNLERTDEIYIAGSPLTPRRVGEVRTDAGGLGRSVTSPTTLYDRYSSPTVSTTRRRLFESDSPSEGSTAGRIPPQPLVNAVPVQNVSGETVSVTPVPGQTLVTMATATVTANNGQTVTIPVQGIANENGGITFFPVQVNVGGQAQAVTGSIQPLSAQALAGSLSSQQVTGTTLQVPGPVAIQQISPGGQQQNQGQPLTSSSIRPRKTSSLSLFFRKVYYLAGVRLRDLCTKLDISDELRKKIWTCFEFSIVQCPELMMDRHLDQLLMCAIYVMAKVTKEDKSFQNIMRCYRTQPQARSQVYRSVLIKGKRRNSGSCENRSHQNSPTELNTDRASRDSSPVMRSNSTLPVPQPSSAPPTPTRLTGANSDIEEEERGDLIQFYNNIYRKQIQTFAMKYSQANSQMDTPPLSPYPFVRTGSPRRVQLSQSHPIYISPHKNEAMLSPREKIFYYFSNSPSKRLREINSMIRTGETPTKKRGILLDDGSESPAKRICPENHSALLRRLQDVANDRGSH
Protein: Uncharacterized protein (Q38DJ7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MAMHRLCVRARRPTHGMVRLIGGIFSSHRLVSNISTPYRPLSDLEKQVEPLVPFTFTALTQIAHSVDEDLMERVAELGGLRSFLVSCPQTFRVAKVGDVYVARRLRKSVAFHSTVSKDVKPRPQNKEGHHSRALSCDPIRAVPDEVFKLIPSFFVPLDALLDRIRKAGSIQDGSSNSLLNAGDTGDFEDLVARFVEQCSNYIDLVLLKDTNDGGGTVQQRYVRLRPSVSRQCDDLQVFPKDEKCVAHNMESYEVAEYEQHRAARLIPIVEKFVSITRDMRDSAALLLPAGRSLIHVFVSAPHLFDVRDKPELSVRFILDPRFRPNLTLTREEIEKKLEEVNDSRGSSAMRLPINRKKRRALQRQLQFMINPLPFFDENVIAQALFDLLPIDGPISTSNLFSLLSREAHHCLPALPHRIFTKYNHMFRTVEGETELLVQRADLPLPEERNLSEISSEEIVMQLYNNFPRRRHPICGTCVERCSVGFPQSVRLRLRQLDVLNDVLRQQPDKVEVMDGLDEELLKNGVQFAQPGRLQLFRFVGIYQEELIKRYETLCLKLGRDPNKTMKLC
Protein: G-protein coupled receptor 35 (Kynurenic acid receptor) (KYNA receptor) (Q9ES90)
Organism: Mus musculus (Mouse)
Function: Acts as a receptor for kynurenic acid, an intermediate in the tryptophan metabolic pathway. The activity of this receptor is mediated by G-proteins that elicit calcium mobilization and inositol phosphate production through G(qi/o) proteins.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- C-X-C motif chemokine 17
- Indoleamine 2,3-dioxygenase 2
Sequence:
MNSTTCNSTLTWPASVNNFFIIYSALLLVLGLLLNSVALWVFCYRMHQWTETRIYMTNLAVADLCLLCSLPFVLYSLKYSSSDTPVCQLSQGIYLANRYMSISLVTAIAVDRYVAVRHPLRARELRSPRQAAAVCVALWVIVVTSLVVRWRLGMQEGGFCFSSQTRRNFSTTAFSLLGFYLPLAIVVFCSLQVVTVLSRRPAADVGQAEATQKATHMVWANLAVFVICFLPLHVVLTVQVSLNLNTCAARDTFSRALSITGKLSDTNCCLDAICYYYMAREFQEASKPATSSNTPHKSQDSQILSLT
Protein: Complex I intermediate-associated protein 30, mitochondrial (NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 1) (H0YNN4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MALVHKLLRGTYFLRKFSKPTSALYPFLGIRFAEYSSSLQKPVASPGKASSQRKTEGDLQGDHQKEVALDITSSEEKPDVSFDKAIRDEAIYHFRLLKDEIVDHWRGPEGHPLHEVLLEQAKVVWQFRGKEDLDKWTVTSDKTIGGRSEVFLKMGKNNQSALLYGTLSSEAPQDGESTRSGYCAMISRIPRGAFERKMSYDWSQFNTLYLRVRGDGRPWMVNIKEDTDFFQRTNQMYSYFMFTRGGPYWQEVKIPFSKFFFSNRGRIRDVQHELPLDKAGVQWHDLGSLQPLPPGFKHFSCLSLLSSWNYRCLPPHLANLCILSRDEVLPYWAGWFLTGPCDLPTLASQCW
Protein: Homeobox protein SIX1 (Sine oculis homeobox homolog 1) (Q15475)
Organism: Homo sapiens (Human)
Function: Transcription factor that is involved in the regulation of cell proliferation, apoptosis and embryonic development (By similarity). Plays an important role in the development of several organs, including kidney, muscle and inner ear (By similarity). Depending on context, functions as transcriptional repressor or activator (By similarity). Lacks an activation domain, and requires interaction with EYA family members for transcription activation. Mediates nuclear translocation of EYA1 and EYA2. Binds the 5'-TCA[AG][AG]TTNC-3' motif present in the MEF3 element in the MYOG promoter and CIDEA enhancer. Regulates the expression of numerous genes, including MYC, CCND1 and EZR (By similarity). Acts as activator of the IGFBP5 promoter, probably coactivated by EYA2 (By similarity). Repression of precursor cell proliferation in myoblasts is switched to activation through recruitment of EYA3 to the SIX1-DACH1 complex (By similarity). During myogenesis, seems to act together with EYA2 and DACH2 (By similarity). Regulates the expression of CCNA1. Promotes brown adipocyte differentiation (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:10801845, ECO:0000269|PubMed:17130831, ECO:0000269|PubMed:19497856}. Cytoplasm.
Interaction partners:
- Protein phosphatase EYA1
- Protein phosphatase EYA2
- Dachshund homolog 1
- Paired box protein Pax-3
- Protein phosphatase EYA3
- Protein phosphatase EYA4
- Myogenin
- Myoblast determination protein 1
- Paired box protein Pax-2
- Sal-like protein 1
Sequence:
MSMLPSFGFTQEQVACVCEVLQQGGNLERLGRFLWSLPACDHLHKNESVLKAKAVVAFHRGNFRELYKILESHQFSPHNHPKLQQLWLKAHYVEAEKLRGRPLGAVGKYRVRRKFPLPRTIWDGEETSYCFKEKSRGVLREWYAHNPYPSPREKRELAEATGLTTTQVSNWFKNRRQRDRAAEAKERENTENNNSSSNKQNQLSPLEGGKPLMSSSEEEFSPPQSPDQNSVLLLQGNMGHARSSNYSLPGLTASQPSHGLQTHQHQLQDSLLGPLTSSLVDLGS
Protein: Sucrase-isomaltase (EC 3.2.1.10) (B5THE3)
Organism: Mus musculus (Mouse)
Subcellular location: Apical cell membrane {ECO:0000256|ARBA:ARBA00004655}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004655}.
Interaction partners:
Sequence:
MAKKKFSGLEISLIVLFIIVTIIAIALVVVLATKVPAVEEVKSPTSTPSPGRCPPEQGEPLNERINCIPEQHPTKAKCEERGCCWRPWNNTIIPWCFFADNHGYTAASVTNDNSGLKATLSRIPSPTLFGEDIKSVLLTTQSQTRNRFRFKLTDPNNKRYEVPHQFVKDGNGIPAADTLYDVKVSENPFSIKVIRKSNNKVLFDTSIGPLVYSNQYLQISTRLPSEYIYGFGEHIHKRFRHDLYWKTWPIFTRDEIPGDNNHNLYGHQTFFMGIEDNSGKSYGVFLMNSNAMEVFIQPTPIITYRVTGGVLDFYIFLGDTPEQVVQQYQELIGRPAMPAYWNLGFQLSRWNYVSLDKVKEVVRRNREAGIPYDAQVTDIDYMEDKKDFTYDEVAFKGLPEFAQDLHNHGQKYIIILDPAISINKRANGAEYQTYVRGNEQNVWVKESDGTTSLIGEVWPGLTVYPDFTNPRTWEWWANECNLFHQQVEYDGLWIDMNEVSSFIHGSQKGCAPNLLNYPPFTPGILDKIMYSKTLCMDAVQHWGNQYDVHSLYGYSMAIATEKAVEKVFPNKRSFILTRSTFAGSGHHAAHWLGDNTASWEQMEWSITGMLEFGMFGMPLVGADICGFLANTTEELCRRWMQLGAFYPFSRNHNAEGYAEQDPAFWGADSLLVNTSRHYLTIRYTLLPFLYTLFYRAHAFGETVARPFLHEFYEDPNSWIEDTQFLWGPALLITPVLRPETKYVSAYIPDATWYDYETGEKRPWRKQRVDMYLPEDKIGLHLRGGYIIPTQQPDVTTTASRKNPLGLIVALDENQAAKGELFWDDGESKDTIEKKIYILYEFSVSNNNLIVNCTHSSYPEGNTLVFKTIKVLGLSATVTAVTVGENDQQMNPHLAFTFDAFNKILSITDLTFNLGKTFIVRWTTQSFSDNEKFTCYPDVGTATEKTCVERGCIWEPVSGLANVPPCYFPSNHNPYLLTSTQKLATGITAELQLNPASARIKLPSNPISTLRVEVKYHKNDMLQFKIYDAHHKRYEVPVPLNIPDTPTSSEENRLYDVEIKENPFGIQVRRRSTGKLIWDSCLPGFAFNDQFIQISTRLPSQYLYGFGEAEHTAFKRNLNWHTWGMFTRDQPPGYKLNSYGFHPYYMALEDEGNAHGVLLQNSNGMDVTFQPTPALTYRTIGGILDFYMFLGPTPEGATKQYHEVIGFPVMPPYWALGFQLCRYGYRNTSEIEQLYNDMKAAQIPYDVQYTDINYMERQLDFTIGERFKTLPQFVEKIRKEGMKYIVILDPAISGNETQPYPAFERGIQKDVFVKWPNTNDICWAKVWPDLPNITIDETITEDEAVNASRAHVAFPDFFRNSTSEWWTREIYDFYNEKMKFDGLWIDMNEPSSFVNGTVTNKCRNDTLNYPPYFPELTKRNEGLHFRTMCMETEHILSDGSSVLHYDVHNLYGWSQVKPTLDALRNTTGLRGIVISRSTYPTAGRWGGHWLGDNYANWENLEKSLIGMLEFNLFGIPYVGADICGFFNDSEYHLCARWMQVGAFYPYSRNHNIQFTRRQDPVSWNETFAQMSKKVLEIRYTLLPYFYTQMHEAHIHGGTVIRPLMHEFFDDKETWEIYKQFLWGPAFMVTPVIGPFQTAVNGYVPKARWFDYHTGEDIKVRGKLQTFSAPFDTINLHVRGGYILPCQEPAQNTYYSRQNYMKLIVAADDNQTAKGSLFWDDGESIDTYEKNQYTLIEFNLNQKTLTSTVLKNGYRNKSEMKLGNIYVWGKGTTHINQVNLTYGGNEQQLLFTQDEAKEILTIELKNVNVTLDEPIQISWS
Protein: Small ribosomal subunit protein eS24 (40S ribosomal protein S24) (P62849)
Organism: Mus musculus (Mouse)
Function: Required for processing of pre-rRNA and maturation of 40S ribosomal subunits.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:36517592}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P62847}.
Interaction partners:
- Large ribosomal subunit protein eL37
- Large ribosomal subunit protein eL28
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein eS7
- Large ribosomal subunit protein eL13
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein eL38
- Large ribosomal subunit protein uL30
- Small ribosomal subunit protein uS9
- Large ribosomal subunit protein eL31
Sequence:
MNDTVTIRTRKFMTNRLLQRKQMVIDVLHPGKATVPKTEIREKLAKMYKTTPDVIFVFGFRTHFGGGKTTGFGMIYDSLDYAKKNEPKHRLARHGLYEKKKTSRKQRKERKNRMKKVRGTAKANVGAGKKPKE
Protein: Menaquinone reductase, iron-sulfur cluster-binding subunit (EC 1.97.-.-) (Quinone reductase complex subunit C) (Type I cytochrome c3:menaquinone oxidoreductase subunit C) (Q72E85)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Function: Component of the respiratory Qrc complex, that catalyzes the reduction of the menaquinone pool using electrons transferred from the reduced periplasmic cytochrome c3, and which is probably involved in sulfate respiration. Is likely essential for growth on H(2) or formate since the periplasmic hydrogenases and/or formate dehydrogenases act as primary electron donors for the Qrc complex. QrcC is an electron-transferring subunit; its cubane iron sulfur clusters form a pathway for electron transfer between the hemes of QrcA and the membrane quinone pool.
Subcellular location: Periplasm {ECO:0000305|PubMed:20498375}.
Interaction partners:
- Menaquinone reductase, molybdopterin-binding-like subunit
- Menaquinone reductase, integral membrane subunit
- Reductase, transmembrane subunit, putative
- Thiosulfate reductase, putative
- Molybdopterin oxidoreductase domain protein
- Iron-sulfur cluster-binding protein
- Formate dehydrogenase, alpha subunit, selenocysteine-containing
- Formate dehydrogenase, alpha subunit, selenocysteine-containing
- Formate dehydrogenase 2 subunit alpha
- Protein DVU_0534
Sequence:
MSSFKEFKIKWGMVIDLDKCTGCGACMVACQAENNIAPQPDASNKLKSLNWLVVYELNNGKPFPEHDVAYLPRPCMQCGKPSCVSVCPVVATDKNEEGGIVSQVYPRCIGCRYCMASCPYHARYFNWFDPTWPEGMDKTLTPDVSVRPRGVVEKCTFCHHRFMQAKDKARVEGRDPSALRDGDYVTSCTEACPNGAIIFGDFNNPEHRVHELHKSKYAFRLLERLGTDPQVYYLSRREWVRRLGDNYLEHEKVKG
Protein: Bifunctional inhibitor/plant lipid transfer protein/seed storage helical domain-containing protein (M4D425)
Organism: Brassica campestris (Field mustard)
Interaction partners:
Sequence:
MATGSRVLIGLAMILIISGELLVPGQGTCQGDIEGLMRECAVYVQRPGPKVNPSAACCKVVKRSDIPCACGRITPSVQKMIDMNKVVLVTSFCGRPLAHGTKCGSKSVIN
Protein: Cytochrome c oxidase subunit 8A, mitochondrial (Cytochrome c oxidase polypeptide VIII-liver) (Cytochrome c oxidase subunit 8-2) (P80433)
Organism: Rattus norvegicus (Rat)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P10176}; Single-pass membrane protein {ECO:0000250|UniProtKB:P10176}.
Interaction partners:
- Cytochrome c oxidase subunit 6A1, mitochondrial
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
- Cytochrome c oxidase subunit 5B, mitochondrial
- Cytochrome c oxidase subunit 6B1
- Cytochrome c oxidase subunit 7A2, mitochondrial
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase subunit 6C-2
- NDUFA4, mitochondrial complex-associated.
- Cytochrome c oxidase subunit 7B, mitochondrial
Sequence:
MSSLTPLLLRSLTGPARRLMVPRAQVHSKPPREQLGVLDITIGLTSCFVCCLLPAGWVLSHLESYKKRE
Protein: Serine/threonine-protein phosphatase (EC 3.1.3.16) (A0A1D8PSJ8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Uncharacterized protein
- Serine/threonine-protein phosphatase 4 regulatory subunit 3
- Serine/threonine-protein kinase
- Type 2A phosphatase-associated protein 42
- Protein phosphatase 2A structural subunit
- Rfa2p
- Serine/threonine-protein phosphatase 2A activator 1
- Serine/threonine-protein kinase RAD53
- Tip41p
- Protein phosphatase PP2A regulatory subunit B
Sequence:
MLNLDETIENIKQCKHIPEGDVEELCTKVIELLIEEANIQHIDTPVTICGDIHGQLHDLITLFKTGGELPDTQYLFLGDFVDRGFYSFESFLLLISLKLRYPDRITLIRGNHESRQITTVYGFYDECLRKYGSINVWRYCCEVFDYLSLGAIVGGSQGVFCIHGGLSPEIDTVDQIRVLDRKKEVPHEGGMCDLLWSDPELVNGWSISPRGAGYLFGENEVNKFLHDNNISLIARAHQLVMEGYKEMFNQGLVTVWSAPNYCYRCGNVASVLTIGDDLSREYKVFEASPHDIGSIPSRKPPVEYFI
Protein: L-amino-acid oxidase (LAAO) (LAO) (EC 1.4.3.2) (EC 1.4.3.25) (Interleukin-4-induced protein 1) (IL4-induced protein 1) (mIL4I1) (Protein Fig-1) (mFIG1) (O09046)
Organism: Mus musculus (Mouse)
Function: Secreted L-amino-acid oxidase that acts as a key immunoregulator. Has preference for L-aromatic amino acids: converts phenylalanine (Phe), tyrosine (Tyr) and tryptophan (Trp) to phenylpyruvic acid (PP), hydroxyphenylpyruvic acid (HPP), and indole-3-pyruvic acid (I3P), respectively. Also has weak L-arginine oxidase activity (By similarity). Acts as a negative regulator of anti-tumor immunity by mediating Trp degradation via an indole pyruvate pathway that activates the transcription factor AHR. IL4I1-mediated Trp catabolism generates I3P, giving rise to indole metabolites (indole-3-acetic acid (IAA) and indole-3-aldehyde (I3A)) and kynurenic acid, which act as ligands for AHR, a ligand-activated transcription factor that plays important roles in immunity and cancer (By similarity). AHR activation by indoles following IL4I1-mediated Trp degradation enhances tumor progression by promoting cancer cell motility and suppressing adaptive immunity. Also has an immunoregulatory function in some immune cell, probably by mediating Trp degradation and promoting downstream AHR activation: inhibits T-cell activation and proliferation, promotes the differentiation of naive CD4(+) T-cells into FOXP3(+) regulatory T-cells (Treg) and regulates the development and function of B-cells. Also regulates M2 macrophage polarization by inhibiting T-cell activation. Also has antibacterial properties by inhibiting growth of Gram negative and Gram positive bacteria through the production of NH4(+) and H2O2 (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q96RQ9}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:Q96RQ9}. Note=Secreted at the immunological synapse. {ECO:0000250|UniProtKB:Q96RQ9}.; SUBCELLULAR LOCATION: [Isoform 1]: Lysosome {ECO:0000269|PubMed:15383589}.; SUBCELLULAR LOCATION: [Isoform 2]: Lysosome {ECO:0000269|PubMed:15383589}.
Interaction partners:
- Amine oxidase [flavin-containing] A
- Amine oxidase [flavin-containing] B
- Indoleamine 2,3-dioxygenase 1
- Tryptophan 2,3-dioxygenase
- Aspartate aminotransferase, mitochondrial
- Indoleamine 2,3-dioxygenase 2
- Branched-chain-amino-acid aminotransferase, cytosolic
- D-aspartate oxidase
- Omega-amidase NIT2
- Branched-chain-amino-acid aminotransferase, mitochondrial
Sequence:
MAGLALRLVLAATLLGLAGSLDWKAASSLNPIEKCMEDHDYEQLLKVVTLGLNRTSKPQKVVVVGAGVAGLVAAKMLSDAGHKVTILEADNRIGGRIFTFRDEKTGWIGELGAMRMPSSHRILHKLCRTLGLNLTQFTQYDENTWTEVHNVKLRNYVVEKMPEKLGYNLNNRERGHSPEDIYQMALNKAFKDLKALGCKKAMNKFNKHTLLEYLLEEGNLSRPAVQLLGDVMSEEGFFYLSFAEALRAHACLSDRLRYSRIVGGWDLLPRALLSSLSGALLLNAPVVSITQGRNDVRVHIATSLHSEKTLTADVVLLTASGPALQRITFSPPLTRKRQEALRALHYVAASKVFLSFRRPFWHEEHIEGGHSNTDRPSRLIFYPARGEGSLLLASYTWSDAAAPFAGLSTDQTLRLVLQDVAALHGPVVFRLWDGRGVVKRWAEDPHSQGGFVVQPPLYGREAEDYDWSAPFGRIYFAGEHTALPHGWVETAVKSGLRAAVRINNNYGYGEVDPQMMEHAYAEANYLDQYPEGERPEEQQAREEVSPDEQEPSHKHLLVETSPEGQQHAFVEAIPELQGHVFVETVPQEKGHAHQNIYPSEHVQVHGEVIPEWHGHGGSGTPQMHRVGDHS
Protein: Uncharacterized protein C18H10.20c (O60150)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- E3 ubiquitin-protein ligase pub1
- Amino acid transporter 1
- Cationic amino acid transporter 1
- Tuberous sclerosis 2 protein homolog
- Meiotically up-regulated gene 170 protein
- Uncharacterized protein C557.05
Sequence:
MPLKLALPRSTTPKDPARCTLDIRMESPPLVFLGSPETSSGALASGILKLTILHQPFIKVHTLKLQLIKRITVLHPAISHCSACAGSKEVLQTWDLAANTTYRPGTQHWPFSWLFPGSLPASVSNRYIKLEYYLEATLCYGTPEGGISPSKPEVLKFPLQLKRAAIPSPDTIHKRIFPPTNLVANITLPSTLHPHGAALMEVTMTGFAQNDGNDWKINRVTWRLEEHMQFSCQPCERHRDLVKPRPIEEKRILSTQDLQSGWKFIDNQMFLSTQINTSSLREPSCDVEIPAPFSLKVSHHLIFETIVNRKKNVAGNNMGNARILRVSVVQPLTTPAGLGISWDEECPPVFESVGPAPPAYT
Protein: Laminin subunit alpha-4 (Laminin-14 subunit alpha) (Laminin-8 subunit alpha) (Laminin-9 subunit alpha) (Q16363)
Organism: Homo sapiens (Human)
Function: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane. Secreted {ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717}. Note=Major basement membrane component.
Interaction partners:
- Laminin subunit beta-3
- Laminin subunit gamma-2
- Laminin subunit beta-1
- Laminin subunit gamma-1
- Cell surface glycoprotein MUC18
- Laminin subunit gamma-3
- Integrin beta-1
- Laminin subunit beta-2
- Integrin alpha-6
- CD44 antigen
Sequence:
MALSSAWRSVLPLWLLWSAACSRAASGDDNAFPFDIEGSSAVGRQDPPETSEPRVALGRLPPAAEKCNAGFFHTLSGECVPCDCNGNSNECLDGSGYCVHCQRNTTGEHCEKCLDGYIGDSIRGAPQFCQPCPCPLPHLANFAESCYRKNGAVRCICNENYAGPNCERCAPGYYGNPLLIGSTCKKCDCSGNSDPNLIFEDCDEVTGQCRNCLRNTTGFKCERCAPGYYGDARIAKNCAVCNCGGGPCDSVTGECLEEGFEPPTGMDCPTISCDKCVWDLTDDLRLAALSIEEGKSGVLSVSSGAAAHRHVNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDTINHASQLVEQAHDMRDKIQEINNKMLYYGEEHELSPKEISEKLVLAQKMLEEIRSRQPFFTQRELVDEEADEAYELLSQAESWQRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQDLQQEANELSRKLHSSDMNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQAKAESSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERGDAQQRLGQSRLITEEANRTTMEVQQATAPMANNLTNWSQNLQHFDSSAYNTAVNSARDAVRNLTEVVPQLLDQLRTVEQKRPASNVSASIQRIRELIAQTRSVASKIQVSMMFDGQSAVEVHSRTSMDDLKAFTSLSLYMKPPVKRPELTETADQFILYLGSKNAKKEYMGLAIKNDNLVYVYNLGTKDVEIPLDSKPVSSWPAYFSIVKIERVGKHGKVFLTVPSLSSTAEEKFIKKGEFSGDDSLLDLDPEDTVFYVGGVPSNFKLPTSLNLPGFVGCLELATLNNDVISLYNFKHIYNMDPSTSVPCARDKLAFTQSRAASYFFDGSGYAVVRDITRRGKFGQVTRFDIEVRTPADNGLILLMVNGSMFFRLEMRNGYLHVFYDFGFSGGPVHLEDTLKKAQINDAKYHEISIIYHNDKKMILVVDRRHVKSMDNEKMKIPFTDIYIGGAPPEILQSRALRAHLPLDINFRGCMKGFQFQKKDFNLLEQTETLGVGYGCPEDSLISRRAYFNGQSFIASIQKISFFDGFEGGFNFRTLQPNGLLFYYASGSDVFSISLDNGTVIMDVKGIKVQSVDKQYNDGLSHFVISSVSPTRYELIVDKSRVGSKNPTKGKIEQTQASEKKFYFGGSPISAQYANFTGCISNAYFTRVDRDVEVEDFQRYTEKVHTSLYECPIESSPLFLLHKKGKNLSKPKASQNKKGGKSKDAPSWDPVALKLPERNTPRNSHCHLSNSPRAIEHAYQYGGTANSRQEFEHLKGDFGAKSQFSIRLRTRSSHGMIFYVSDQEENDFMTLFLAHGRLVYMFNVGHKKLKIRSQEKYNDGLWHDVIFIRERSSGRLVIDGLRVLEESLPPTEATWKIKGPIYLGGVAPGKAVKNVQINSIYSFSGCLSNLQLNGASITSASQTFSVTPCFEGPMETGTYFSTEGGYVVLDESFNIGLKFEIAFEVRPRSSSGTLVHGHSVNGEYLNVHMKNGQVIVKVNNGIRDFSTSVTPKQSLCDGRWHRITVIRDSNVVQLDVDSEVNHVVGPLNPKPIDHREPVFVGGVPESLLTPRLAPSKPFTGCIRHFVIDGHPVSFSKAALVSGAVSINSCPAA