wanglab/gogpt-training-data huggingface dataset:
Protein: Acidic mammalian chitinase (AMCase) (EC 3.2.1.14) (Lung-specific protein TSA1902) (Q9BZP6)
Organism: Homo sapiens (Human)
Function: Degrades chitin and chitotriose. May participate in the defense against nematodes, fungi and other pathogens. Plays a role in T-helper cell type 2 (Th2) immune response. Contributes to the response to IL-13 and inflammation in response to IL-13. Stimulates chemokine production by pulmonary epithelial cells. Protects lung epithelial cells against apoptosis and promotes phosphorylation of AKT1. Its function in the inflammatory response and in protecting cells against apoptosis is inhibited by allosamidin, suggesting that the function of this protein depends on carbohydrate binding.
Subcellular location: [Isoform 1]: Secreted. Note=Secretion depends on EGFR activity.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm.
Interaction partners:
- Beta-hexosaminidase subunit beta
- Beta-hexosaminidase subunit alpha
- Chitotriosidase-1
- N-acetyl-D-glucosamine kinase
- N-acylglucosamine 2-epimerase
- Transcriptional repressor CTCF
- Interleukin-13
- Arginase-1
- MyoD family inhibitor domain-containing protein
- Interleukin-4
Sequence:
MTKLILLTGLVLILNLQLGSAYQLTCYFTNWAQYRPGLGRFMPDNIDPCLCTHLIYAFAGRQNNEITTIEWNDVTLYQAFNGLKNKNSQLKTLLAIGGWNFGTAPFTAMVSTPENRQTFITSVIKFLRQYEFDGLDFDWEYPGSRGSPPQDKHLFTVLVQEMREAFEQEAKQINKPRLMVTAAVAAGISNIQSGYEIPQLSQYLDYIHVMTYDLHGSWEGYTGENSPLYKYPTDTGSNAYLNVDYVMNYWKDNGAPAEKLIVGFPTYGHNFILSNPSNTGIGAPTSGAGPAGPYAKESGIWAYYEICTFLKNGATQGWDAPQEVPYAYQGNVWVGYDNIKSFDIKAQWLKHNKFGGAMVWAIDLDDFTGTFCNQGKFPLISTLKKALGLQSASCTAPAQPIEPITAAPSGSGNGSGSSSSGGSSGGSGFCAVRANGLYPVANNRNAFWHCVNGVTYQQNCQAGLVFDTSCDCCNWA
Protein: Copine-5 (Copine V) (Q8JZW4)
Organism: Mus musculus (Mouse)
Function: Probable calcium-dependent phospholipid-binding protein that may play a role in calcium-mediated intracellular processes. Plays a role in dendrite formation by melanocytes.
Subcellular location: Perikaryon {ECO:0000269|PubMed:18614158}. Cell projection {ECO:0000269|PubMed:18614158}.
Interaction partners:
Sequence:
MEQPEDMASLSEFDSLAGSIPATKVEITVSCRNLLDKDMFSKSDPLCVMYTQGMENKQWREFGRTEVIDNTLNPDFVRKFIVDYFFEEKQNLRFDLYDVDSKSPDLSKHDFLGQAFCTLGEIVGSSGSRLEKPLTIGTFSLNSRTGKPMPAVSNGGVPGKKCGTIILSAEELSNCRDVATMQFCANKLDKKDFFGKSDPFLVFYRSNEDGTFTICHKTEVMKNTLNPVWQTFSIPVRALCNGDYDRTIKVEVYDWDRDGSHDFIGEFTTSYRELARGQSQFNIYEVINPKKKMKKKKYVNSGTVTLLSFAVESESTFLDYIKGGTQINFTVAIDFTASNGNPSQSTSLHYMSPYQLNAYALALTAVGEIIQHYDSDKMFPALGFGAKLPPDGRVSHEFPLNGNQENPSCCGIDGILEAYHSSLRTVQLYGPTNFAPVVTHVARNAAAVQDGSQYSVLLIITDGVISDMAQTKEAIVNAAKLPMSIIIVGVGQAEFDAMVELDGDDVRISSRGKLAERDIVQFVPFRDYVDRTGNHVLSMARLARDVLAEIPDQLVSYMKAQGIRPRPPPAAPAQSPPQSPAHSPPGSPVHTHI
Protein: Medium-chain acyl-CoA ligase ACSF2, mitochondrial (EC 6.2.1.2) (Q8VCW8)
Organism: Mus musculus (Mouse)
Function: Acyl-CoA synthases catalyze the initial reaction in fatty acid metabolism, by forming a thioester with CoA. Has some preference toward medium-chain substrates. Plays a role in adipocyte differentiation.
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- Superoxide dismutase, mitochondrial
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein uL11m
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein mL43
- Large ribosomal subunit protein uL24m
- Large ribosomal subunit protein bL21m
Sequence:
MAVYHGMLRFGRLCIASLGARGPRTLLSRPRPNSKLQSVRALSSGMVNCTNPLPIGGLSYIQGHTDSHLVNTTVGECLDATAQRFPDREALVILHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGCKGIVFPKQFKTQQYYDILKQVCPELEKAQPGALKSERLPDLTTVISVDAPLPGTLLLDDIVAAGGKEQNLAQLRYNQRFLSCYDPINIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPTKTAEELRLVLPSPLYHCLGSVGGTMVSMMHGATLLLSSPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPPELIRAIINKMNMKELVVVYGTTENSPVTFMNFPEDTLEQKAGSVGRIMPHTEAQIVNVETGELTNLNVPGELYIRGYCVMQGYWGEPQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQMEQHLKL
Protein: Origin recognition complex subunit 6 (Q9WUJ8)
Organism: Mus musculus (Mouse)
Function: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Origin recognition complex subunit 2
- Origin recognition complex subunit 5
- Origin recognition complex subunit 4
- Origin recognition complex subunit 3
- Origin recognition complex subunit 1
- Cell division control protein 6 homolog
- DNA replication licensing factor MCM7
- DNA replication factor Cdt1
- Protein DBF4 homolog A
- DNA replication licensing factor MCM4
Sequence:
MESELVRRLAPRLGLAEPSVLRKAEEFLRLSKVKCVSLSARSSETSNAVICLDLAASCRKCPLDRAYLIRLSGLNKMMYQSCLKSFECLLGLNSNVGIRDLAVQFSCTEAVNLAAEILQSYKSGLPETQRADLDLSRPLFTTAALLSACKILKIKVDKTKMITTSGVKKAILDRLCKQLEKIGQQINRDSADLARPALKRKKPEFSPTLKKKEPGLEPPAKEIEVIETLHKLPKDEDLTQDYEEWKRKILENAAKAQTATAE
Protein: Eukaryotic translation initiation factor 4 gamma 1 (eIF-4-gamma 1) (eIF-4G 1) (eIF-4G1) (p220) (Q04637)
Organism: Homo sapiens (Human)
Function: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome. As a member of the eIF4F complex, required for endoplasmic reticulum stress-induced ATF4 mRNA translation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17984221}. Nucleus {ECO:0000269|PubMed:17984221}. Cytoplasm, Stress granule {ECO:0000269|PubMed:22872150}.
Interaction partners:
- Eukaryotic translation initiation factor 4B
- Eukaryotic translation initiation factor 4E
- Eukaryotic initiation factor 4A-II
- Polyadenylate-binding protein 1
- Eukaryotic initiation factor 4A-I
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 1
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 4H
- Eukaryotic initiation factor 4A-III
Sequence:
MNKAPQSTGPPPAPSPGLPQPAFPPGQTAPVVFSTPQATQMNTPSQPRQHFYPSRAQPPSSAASRVQSAAPARPGPAAHVYPAGSQVMMIPSQISYPASQGAYYIPGQGRSTYVVPTQQYPVQPGAPGFYPGASPTEFGTYAGAYYPAQGVQQFPTGVAPTPVLMNQPPQIAPKRERKTIRIRDPNQGGKDITEEIMSGARTASTPTPPQTGGGLEPQANGETPQVAVIVRPDDRSQGAIIADRPGLPGPEHSPSESQPSSPSPTPSPSPVLEPGSEPNLAVLSIPGDTMTTIQMSVEESTPISRETGEPYRLSPEPTPLAEPILEVEVTLSKPVPESEFSSSPLQAPTPLASHTVEIHEPNGMVPSEDLEPEVESSPELAPPPACPSESPVPIAPTAQPEELLNGAPSPPAVDLSPVSEPEEQAKEVTASMAPPTIPSATPATAPSATSPAQEEEMEEEEEEEEGEAGEAGEAESEKGGEELLPPESTPIPANLSQNLEAAAATQVAVSVPKRRRKIKELNKKEAVGDLLDAFKEANPAVPEVENQPPAGSNPGPESEGSGVPPRPEEADETWDSKEDKIHNAENIQPGEQKYEYKSDQWKPLNLEEKKRYDREFLLGFQFIFASMQKPEGLPHISDVVLDKANKTPLRPLDPTRLQGINCGPDFTPSFANLGRTTLSTRGPPRGGPGGELPRGPAGLGPRRSQQGPRKEPRKIIATVLMTEDIKLNKAEKAWKPSSKRTAADKDRGEEDADGSKTQDLFRRVRSILNKLTPQMFQQLMKQVTQLAIDTEERLKGVIDLIFEKAISEPNFSVAYANMCRCLMALKVPTTEKPTVTVNFRKLLLNRCQKEFEKDKDDDEVFEKKQKEMDEAATAEERGRLKEELEEARDIARRRSLGNIKFIGELFKLKMLTEAIMHDCVVKLLKNHDEESLECLCRLLTTIGKDLDFEKAKPRMDQYFNQMEKIIKEKKTSSRIRFMLQDVLDLRGSNWVPRRGDQGPKTIDQIHKEAEMEEHREHIKVQQLMAKGSDKRRGGPPGPPISRGLPLVDDGGWNTVPISKGSRPIDTSRLTKITKPGSIDSNNQLFAPGGRLSWGKGSSGGSGAKPSDAASEAARPATSTLNRFSALQQAVPTESTDNRRVVQRSSLSRERGEKAGDRGDRLERSERGGDRGDRLDRARTPATKRSFSKEVEERSRERPSQPEGLRKAASLTEDRDRGRDAVKREAALPPVSPLKAALSEEELEKKSKAIIEEYLHLNDMKEAVQCVQELASPSLLFIFVRHGVESTLERSAIAREHMGQLLHQLLCAGHLSTAQYYQGLYEILELAEDMEIDIPHVWLYLAELVTPILQEGGVPMGELFREITKPLRPLGKAASLLLEILGLLCKSMGPKKVGTLWREAGLSWKEFLPEGQDIGAFVAEQKVEYTLGEESEAPGQRALPSEELNRQLEKLLKEGSSNQRVFDWIEANLSEQQIVSNTLVRALMTAVCYSAIIFETPLRVDVAVLKARAKLLQKYLCDEQKELQALYALQALVVTLEQPPNLLRMFFDALYDEDVVKEDAFYSWESSKDPAEQQGKGVALKSVTAFFKWLREAEEESDHN
Protein: Filensin (Beaded filament structural protein 1) (Lens fiber cell beaded-filament structural protein CP 95) (CP95) [Cleaved into: Filensin C-terminal fragment; Filensin N-terminal fragment] (A2AMT1)
Organism: Mus musculus (Mouse)
Function: Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA. Involved in altering the calcium regulation of MIP water permeability (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:19029034}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q06002}; Cytoplasmic side {ECO:0000250|UniProtKB:Q06002}. Cytoplasm {ECO:0000269|PubMed:19029034, ECO:0000269|PubMed:27559293}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q06002}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q06002}.
Interaction partners:
- Lens fiber major intrinsic protein
- Phakinin
- Alpha-crystallin A chain
- Beta-crystallin A1
- Beta-crystallin A2
- Gap junction alpha-8 protein
- Gamma-crystallin S
- Beta-crystallin B1
- Beta-crystallin B3
- Gap junction alpha-3 protein
Sequence:
MYRRSYVFQARQERYERAQPAGPAAQPGGTAPGLAALQALGERVAVQVQRARALQQRHAGLRRQLDAFQRLGEQPGPEDALARHVEANLQRARDLTAEHARLERQEAEAQRALDEFRSKYENECECQLVLKEMLERLNKEADEALLRNLHLQLEAQFLQADISVAKDRYKKNLLEIQTYITVLQQIVQTAPQVSLVTGMRESGLLMQEKLFTEREVAALQNQLEEGREAVTHLQAQKAELQAQTTALEQAIKHAHECYDEELQLYNEQIENLRKEIEEAERSLERSSYDCRQLAVAQQTLRNELDRYHRIIEIEGSRLSSVFIETPISLITPSHGAPLSLGSSVKDLARAVQDITAAKPRQKALPKSLPKRKEIIAQDKVEETLEDAPLKPPQEPKALQVERKAEGGSQPGAGGGHGVSPTQEGGPEDVPDGGQISKAFGKLCKVVKERVSGHKEPEPEPPTDLFTKGRHVLVTGESSFVDPEFYSSSIPARGGVVISIEEDSMHHDGHVEPSPGQPMPPVENGQGVPQGREGDHSNHQQGTDKNGLRAKEPKDLEEKDDDGKKEAEGSRRPCPVIIPGPDEPSTSHSQTSGSNQGGPVGPASKSSSLLAKGPSKALSIKKVEVVESIEKISTESIQTYEETSVIVETLIGKSKGNKKLGEKSLPDTRA
Protein: Peptidyl-prolyl cis-trans isomerase FKBP8 (PPIase FKBP8) (EC 5.2.1.8) (38 kDa FK506-binding protein) (38 kDa FKBP) (FKBP-38) (mFKBP38) (FK506-binding protein 8) (FKBP-8) (FKBPR38) (Rotamase) (O35465)
Organism: Mus musculus (Mouse)
Function: Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis (By similarity). Required for normal embryonic development.
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:15105374}; Single-pass membrane protein {ECO:0000269|PubMed:15105374}; Cytoplasmic side {ECO:0000269|PubMed:15105374}.
Interaction partners:
- Regulatory-associated protein of mTOR
- Target of rapamycin complex subunit LST8
- Proline-rich AKT1 substrate 1
- Microtubule-associated protein 1 light chain 3 alpha
- Apoptosis regulator Bcl-2
- DEP domain-containing mTOR-interacting protein
- Heat shock protein HSP 90-beta
- Heat shock protein HSP 90-alpha
- GTP-binding protein Rheb
- Egl nine homolog 1
Sequence:
MASWAEPSEPAALRLPGAPLLEGFEVLDGVDDAEEEDDLSGLPPLEDMGQPTVEEAEQPGALAREFLAATEPEPAPAPAPEEWLDILGNGLLRMKTLVPGPKGSSRPLKGQVVTVHLQMSLENGTRVQEEPELAFTLGDCDVIQALDLSVPLMDVGETAMVTADSKYCYGPQGRSPYIPPHAALCLEVTLKTAEDGPDLEMLSGQERVALANRKRECGNAHYQRADFVLAANSYDLAIKAITSNTKVDMTCEEEEELLQLKVKCLNNLAASQLKLDHYRAALRSCSQVLEHQPDNIKALFRKGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAELSKLVKKRAAQRSTETALYRKMLGNPSRLPAKCPGKGAWSIPWKWLFGATAVALGGVALSVVIAARN
Protein: Carnitine O-acetyltransferase (Q5AMQ5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Carnitine O-acetyltransferase
- Peroxisomal hydratase-dehydrogenase-epimerase
- Carnitine O-acetyltransferase
- Mitochondrial thiamine pyrophosphate carrier 1
- acetyl-CoA C-acyltransferase
- Acyl-coenzyme A oxidase
- 2,4-dienoyl-CoA reductase [
- acetyl-CoA C-acyltransferase
- Oleate-induced peroxisomal protein POX18
- Mitochondrial thiamine pyrophosphate carrier 1
Sequence:
MFKFRIPQQILKQNSTSSKSIIMPVLKKPFSTSNPKGDLFKYQSQLPKLPVPSLEETATKYLKTVEPFLNKEQLAATKQKVENFIQPGGAGEALQARLNDFASDKDNWLAEFWDDYAYMSYRDPVVPYVSYFFSHKDVNNVIGNDQLLKASLIAYYTIEFQEKVLDESLDPEVIKGNPYCMNAFKYMFNNSRVPAEGSDITQHYDGEANRFFIVIYKNNFYKVPTHNESGQRLSKGELYSYLQQVKNDATPKGLGLGALTSLNRDEWLGAYNNLLKSPINQASLESIFASAFVICLDSHNPVTIEEKSKNCWHGDGQNRFFDKPLEFFVSANGNSGFLGEHSRMDATPTVQLNNTVYKKITEESPEDLIVEIGGSAPKIGPAEILPFDINPTTRANIADAIAKFDATIAAHDEEIFQHYGYGKGLIKKFKVSPDAYVQMLMQLAYFKYTGKIRPTYESAATRKFLKGRTETGRTVSNESKKFVETWTNPKATNEEKVSTFQAAAKQHVAYLSAAADGKGVDRHLFGLKQMLQPNEPVPEIFTDPIFSYSQTWYISSSQVPSEYFQSWGWSQVIDDGFGLAYLINNDWIHVHISCKRGNGLKSDHLKWYLVESANEMKDILTKGLLSEPKAKL
Protein: Probable shikimate 5-dehydrogenase AroE (5-dehydroshikimate reductase) (I6Y120)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- 3-phosphoshikimate 1-carboxyvinyltransferase
- 3-dehydroquinate synthase
- Shikimate kinase
- 3-dehydroquinate dehydratase
- Chorismate synthase
- Endolytic murein transglycosylase
- Prepilin type IV endopeptidase peptidase domain-containing protein
- Putative pre-16S rRNA nuclease
- Salicylate synthase
- Alanine--tRNA ligase
Sequence:
MSEGPKKAGVLGSPIAHSRSPQLHLAAYRALGLHDWTYERIECGAAELPVVVGGFGPEWVGVSVTMPGKFAALRFADERTARADLVGSANTLVRTPHGWRADNTDIDGVAGALGAAAGHALVLGSGGTAPAAVVGLAELGVTDITVVARNSDKAARLVDLGTRVGVATRFCAFDSGGLADAVAAAEVLVSTIPAEVAAGYAGTLAAIPVLLDAIYDPWPTPLAAAVGSAGGRVISGLQMLLHQAFAQVEQFTGLPAPREAMTCALAALD
Protein: Peroxisomal membrane protein PEX15 (Peroxin-15) (Peroxisome biosynthesis protein PAS21) (Q08215)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Peroxisomal docking factor that anchors PEX1 and PEX6 to peroxisome membranes. PEX26 is therefore required for the formation of the PEX1-PEX6 AAA ATPase complex, a complex that mediates the extraction of the PEX5 receptor from peroxisomal membrane.
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:24821790}; Single-pass membrane protein {ECO:0000269|PubMed:14562095}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095}; Single-pass membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Peroxisomal ATPase PEX6
- Peroxisomal ATPase PEX1
- Peroxisomal targeting signal receptor
- Peroxisome assembly protein 22
- Ubiquitin-conjugating enzyme E2-21 kDa
- Peroxisomal membrane protein PEX13
- Peroxisomal membrane protein PEX14
- Proteasome subunit beta type-6
- Peroxisomal biogenesis factor 3
- Peroxisomal membrane protein PEX17
Sequence:
MAASEIMNNLPMHSLDSSLRDLLNDDLFIESDESTKSVNDQRSEVFQECVNLFIKRDIKDCLEKMSEVGFIDITVFKSNPMILDLFVSACDIMPSFTKLGLTLQSEILNIFTLDTPQCIETRKIILGDLSKLLVINKFFRCCIKVIQFNLTDHTEQEEKTLELESIMSDFIFVYITKMRTTIDVVGLQELIEIFIFQVKVKLHHKKPSPNMYWALCKTLPKLSPTLKGLYLSKDVSIEDAILNSIDNKIQKDKAKSKGKQRGVKQKIHHFHEPMLHNSSEEQVKVEDAFNQRTSTDSRLQSTGTAPRKKNNDITVLAGSFWAVLKHHFTRSVLNKNGLLLTGLLLLLCLKKYKSLMAIFKHVPAAFHTVYPQIVGLLKLLASI
Protein: C-type lectin domain family 4 member D (C-type lectin superfamily member 8) (Dendritic cell-associated C-type lectin 3) (DC-associated C-type lectin 3) (Dectin-3) (Macrophage-restricted C-type lectin) (CD antigen CD368) (Q9Z2H6)
Organism: Mus musculus (Mouse)
Function: Calcium-dependent lectin that acts as a pattern recognition receptor (PRR) of the innate immune system: recognizes damage-associated molecular patterns (DAMPs) of pathogen-associated molecular patterns (PAMPs) of bacteria and fungi. The PAMPs include alpha-mannans on C.albicans hypheas and mycobacterial trehalose 6,6'-dimycolate (TDM). Interacts with signaling adapter Fc receptor gamma chain/FCER1G, likely via CLEC4E, to form a functional complex in myeloid cells (By similarity). Binding of mycobacterial TDM or C.albicans alpha-mannans to this receptor complex leads to phosphorylation of the immunoreceptor tyrosine-based activation motif (ITAM) of FCER1G, triggering activation of SYK, CARD9 and NF-kappa-B, consequently driving maturation of antigen-presenting cells and shaping antigen-specific priming of T-cells toward effector T-helper 1 and T-helper 17 cell subtypes. The heterodimer formed with CLEC6A is active against fungal infection (By similarity). Functions as an endocytic receptor (By similarity). May be involved in antigen uptake at the site of infection, either for clearance of the antigen, or for processing and further presentation to T-cells (By similarity).
Subcellular location: Cell membrane {ECO:0000305|PubMed:23602766}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- C-type lectin domain family 4 member E
- High affinity immunoglobulin epsilon receptor subunit gamma
- C-type lectin domain family 6 member A
- C-type lectin domain family 9 member A
- C-type lectin domain family 1 member A
Sequence:
MWLEESQMKSKGTRHPQLIPCVFAVVSISFLSACFISTCLVTHHYFLRWTRGSVVKLSDYHTRVTCIREEPQPGATGGTWTCCPVSWRAFQSNCYFPLNDNQTWHESERNCSGMSSHLVTINTEAEQNFVTQLLDKRFSYFLGLADENVEGQWQWVDKTPFNPHTVFWEKGESNDFMEEDCVVLVHVHEKWVWNDFPCHFEVRRICKLPGITFNWKPSK
Protein: Serine palmitoyltransferase 1 (EC 2.3.1.50) (Long chain base biosynthesis protein 1) (LCB 1) (Serine-palmitoyl-CoA transferase 1) (SPT 1) (SPT1) (O54695)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Function: Serine palmitoyltransferase (SPT). The heterodimer formed with SPTLC2 or SPTLC3 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates, with a slight preference for C14-CoA. The SPTLC1-SPTLC2-SPTSSB complex shows a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme displays an ability to use a broader range of acyl-CoAs, without apparent preference (By similarity). Required for adipocyte cell viability and metabolic homeostasis (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12464627}; Single-pass membrane protein {ECO:0000269|PubMed:12464627}.
Interaction partners:
Sequence:
MAMAAEQWVLVEMVQALYEAPAYHLILEGILILWIIRLVFSKTYKLQERSDLTAKEKEELIEEWQPEPLVPPVSKNHPALNYNIVSGPPTHNIVVNGKECVNFASFNFLGLLANPRVKAAALASLKKYGVGTCGPRGFYGTFDVHLDLEERLAKFMRTEEAIIYSYGFSTIASAIPAYSKRGDIVFVDSAACFAIQKGLQASRSDIKLFKHNDVADLERLLKEQEIEDQKNPRKARVTRRFIVVEGLYMNTGTVCPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGISIDDIDLISANMENALASVGGFCCGRSFVVDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENPGIFAVLKKKCQHIHKSLQGISGLKVVGESLSPALHLQLEESTGSREKDVQLLQEMVIHCMNEGIALTQARYLDKEEKCLPPPSIRVVVTVEQTEEELERAASTIREAAQAVLL
Protein: Quattro (Q6DN89)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MNPSSLDWSIQSALSSLFPPFEATAPTVLSQLFRTIEERYHGDALQCLLNFLIPAKHILESVQQAACAAYSDVLFQCEGWPLCLSDRVVIQLAAINPLLLRPGDFYLQVEPFGEQSGRIVLKSLLVQEDLLGQENLILQAGSRVLECPTIEETPILETSYPCIFTESWLREINEGRQGNRLSRCVLSSDKGVVKVPWTEVANPEFLDRPKSNVWPDSKPCSTATIRVRDLNTEISDIESKVVVDFLPLEMETRIVPAIDGLALSVQLVESGSRLVKVNQAHTISSFAGKPVGWVSPNTWDSRQTQELEGEYVDLLEFNKEKETLVPNKIAMPMKPLGFKLVRTAQPSSKSNVSICGVDCNPNKQPSEIMQHDPDSKCRYRQSYMAALRNPVNFERASMLPCLDETRTDAGKAEPSCEGYGVGLRLQPSSCMFGQTPNQADRNPMQSFENSAQQKQSPKNSTQPSQNVTHDRKSRENAESPDQHMTQLITSMVQARQPHKSFLTGQPDLPQTVLGTKALPDKRHPCLNNAIRQDSFHMRISGQKHAKTQHLPKMGLRALPDHGGHRHDAKLCLQGFSPIQHSQNQPTQITEQTPQPQISQNPFRNENRLLDCNVFCEDRHCGRGPGSPVQVIKGKSRSKSRSSSSVSETARQCLQSNKPTNRSHSDVYPEIIPMLPAIHGIKHTADLVSPKLNRPQEARKVSLSGKAGAPVVNGVELQKLQHSDQPTTGQSVTEIQGIYISQDPTIKSLLQLGIICLPGGRDRAGRAVVEVYGGRNGWISPQVSPLELCRLLLYLHSIPRSEVRELGLTVVIDSRKCPLTSVFYKSLLMVQEQALHAVHTILMLVDKDANPRPEKHPGLQIDVVTSLKALHKTVDGHQLTSDLSGSFPYSHEDWLQFHQKLSLFQIELEAASSLLQTAIRRLDVKRTDTAKDVQSCIQEQRSSMKMVLEDTRLVALQREGGAILARMRREESRFAHSEDFRDSLESVTCLYNQVEESVHTLVMKSNQSLQHLEHVLLLRETQDSLHTIQKWCDAEERLWQKDKDDAEKTLQKIQQRLQDTQTLLRQAKENKERGMLLIKDVERKSKGTHYPETDAFRCYTTGFKTRMTGFLLKAEERKSDLQTSVDLYRFCEEASSLVKECMEYLDHMKSSNSPMSVCWSSLHAFEQRFQHFSPQHFQDRSAALLERLPDGIWMWNAVQTQCRDIRQRLSEILQAAHTHKDSQDEAQLNPVSGQTQNRAAEQGDNETLTYLQSAEGSKFEQVMTSSVHEESASRIQQSVECTEQETRHLHETKDKLHNASSMHNASASHAQQSVQCTVQKASMLQETNDTSHNPSMHKDSASHIQESVQCTDQNTSHLHEPQAISHHPSDRKLKEHHHKHSHSDDDLRKSGRIHKFGQTAHYKVFIRSQSAESCLRGYRYNIPLCKTDAAASCVGATLEGLSSELNQHDSFCSSASGFSQKCSSDCGSEDHGSVSGVTCSDNVFTKQEKSVCKPECTLENSSTALKLQRIMQELLQTEQEYVRALAYVVENYMPELERPDVPQDLRGQRGLIFGNLEKLRDFHQHHFIQELELCLEKPFSVGRCFLKHKESFGLYALYSKNKPRSENLLIQHGKDFFKQKQQQLKDALDLSSYLLKPVQRISKYSLLLQDLLRECECVTNAELQRTEIHTALNIIQFQLRHGNNLLAMDDIYGCDVNLKEQGQLIRQDEFLLTFRKKKCYRHIFLFQDLILFSKTRKTDIGNDTYIYKQSFKTSDIGMTHNSGDSGLCFEIWFRRRKTQDTYVLQAASREVKESWTRDLERILWEQAIHNREIRMQERVFMGIGHKPFMDIKPSEMAISDRAINCVLTGRGGVSVLRLNSIGSASGTSSSGSQSSCSSGWGSPSPSAVCPVGGDDVRYVQETSGILEEDDLDQESGNHSTLVASSESSGESVSCFSTSAHSCSSVIGGDCEHTPSELGKQHKQDHLKTTNQTRNQSGSKVQSSIGKSTEV
Protein: Nidogen 2 (A0A4X1WD80)
Organism: Sus scrofa (Pig)
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
Interaction partners:
Sequence:
MRGYRGARRPALRAPPLLLLLLLSRAVALQPDELFPYGQSLGDQLLQEGDDESSAAVKLALPLRFYDAQFSDLYVGTNGIISTQDFPRETQYVDDDFPTDFPAIAPFLADIDTSHGRGRVLYREDTSPDVLSLAARYVRTGFPRSAAHFVPTHAFLATWERVGAYEEPKRGAPPSGELNTFQAVLASDESDTYALFLYPANGLQFFGTRPKESYNVQLELPARVGFSRGEVDDLKREGQYFSLTSTEQSVKNLYQHSNLGIPGVWAFHIGSASPLDNVKPAIAGGDLSKAHPSVPLRHSSSHAVAPEGEDTEDNLDYYDENEEEVEYPPGETEEESNGHSPDDVSFHSRADLKPSGGGISLPGSDLPSPLPRPTSRDGLETESATLDPQTKEGRPQEEIDAPDLKGRGETSEQPGAQVPAPPKTERDSPDPSWAALPPHPDEGALPAERDVPPVPSGGEVVLPNYPRRPDHAPPLGRGRQVVGVEDDIGSNTKVFTYNAANRETCEHNHERCSRHAFCTDYATGFCCHCQSRFYGNGKHCLPEGAPHRVNGKVSGHLLVGHTPVHFTDVDLHAYVVGNDGRAYTAISHIPQPAAQALLPLMPIGGLFGWLFALEKPGWENGFSLTGATFIHDMEVTFHPGGERVRITQTAEGLDPENYLSIKTNIQGQVPYIPANFTVHITPYKELYHYSGSAVTSTSSRAYSLTYGAINQTRSYSIHQNITYQTCRHAPRHWAIPTTQQLNVDRVFALYTDEEKVLRFAVTNQIGPVEGDSEPAPVNPCYDGSHTCATTAQCHPATGVDYTCECASGYQGDGRRCVVIAPPPNPCEDGSHNCAPTSQARCIHHGGRSFSCACLPGYAGDGHQCADVDECSENRCHPSATCSNTPGSFSCHCQPGYHGDGFQCTPDPALGLKPCEHQQREAQAQRTHPGARLHIPQCDEQGHFLPLQCHGSTGFCWCVDPNGQEVPGTRTPPGSLPPHCGPPEPTQRPRTVCERWRESLLEHYGGTPRDDQYVPQCDDLGHFTPLQCHGKSDFCWCVDQDGREVQGTRSQPGTTPACIPTVAPPTMRPTPRPDVTPPPVGTFLLYAQGQQIGHLPLNGTRLQKDMAKTLLSLHGSIVVGIDYDCRERMVYWTDVAGRTISRASLEPGAEPETIVNSGLISPEGLAIDHFRGTMYWTDSGLDKIERARLDGSERRALFHTDLVNPRAIAVDPIRGNLYWTDWNREAPKIEMSSLDGENRRILVNKDIGLPNGLTFDPFSKLLCWADAGTKKLECTLPDGTGRRVIQNNLNYPFSIVSYADHFYHTDWRRDGVISVNRDSGQFTDEYLPEQRSHLYGITAVYPYCPTGRK
Protein: Thiol:disulfide interchange protein, putative (O53924)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MTHSRLIGALTVVAIIVTACGSQPKSQPAVAPTGDAAAATQVPAGQTVPAQLQFSAKTLDGHDFHGESLLGKPAVLWFWAPWCPTCQGEAPVVGQVAASHPEVTFVGVAGLDQVPAMQEFVNKYPVKTFTQLADTDGSVWANFGVTQQPAYAFVDPHGNVDVVRGRMSQDELTRRVTALTSR
Protein: Pickpocket 29, isoform H (A0A0B4LGF3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MWRKSVMNFRGFIRSFVENKGLLWIFVIGISGWSTVSILVLLKTRYETDSTTIGVSTAYSRWINTFPSIGICLTKSRAFNEFKAMMREYFQEDFAFSFTRMIYEYAFLNPNNIFTKEPTKNTSYPYNFNILDIRRKMFPTNCTECFKEIYFRGELVTDCEEIFKFHVTEMGYCFLANNLLDYDSIEEMPLRYSSLDNNRSLRLYMRSSVMYKYEMYVNSPEDLPFFNSLTYTISTDPTTYAFNVEEIHNHEGVIDEPISQRKCKFPSESSIEGFPYSFSACMSIIRSEFEMKTCDCSLFNPKDRNESLYCGLQHADCLIKEGFATRVKEYVGSSTVCLPSCVEQQISLGHN