ID A0A8D1FB21_PIG Unreviewed; 393 AA. AC A0A8D1FB21; DT 19-JAN-2022, integrated into UniProtKB/TrEMBL. DT 19-JAN-2022, sequence version 1. DT 29-MAY-2024, entry version 10. DE RecName: Full=Platelet glycoprotein 4 {ECO:0000256|ARBA:ARBA00020772}; DE AltName: Full=Glycoprotein IIIb {ECO:0000256|ARBA:ARBA00032780}; DE AltName: Full=PAS IV {ECO:0000256|ARBA:ARBA00031821}; DE AltName: Full=PAS-4 {ECO:0000256|ARBA:ARBA00032188}; DE AltName: Full=Platelet glycoprotein IV {ECO:0000256|ARBA:ARBA00029966}; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00040032753.1, ECO:0000313|Proteomes:UP000694722}; RN [1] {ECO:0000313|Ensembl:ENSSSCP00040032753.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2023) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=(9Z)-octadecenoate(out) = (9Z)-octadecenoate(in); CC Xref=Rhea:RHEA:33655, ChEBI:CHEBI:30823; CC Evidence={ECO:0000256|ARBA:ARBA00000626}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33656; CC Evidence={ECO:0000256|ARBA:ARBA00000626}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(9Z,12Z)-octadecadienoate(out) = (9Z,12Z)- CC octadecadienoate(in); Xref=Rhea:RHEA:45264, ChEBI:CHEBI:30245; CC Evidence={ECO:0000256|ARBA:ARBA00000542}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45265; CC Evidence={ECO:0000256|ARBA:ARBA00000542}; CC -!- CATALYTIC ACTIVITY: CC Reaction=butanoate(out) = butanoate(in); Xref=Rhea:RHEA:45248, CC ChEBI:CHEBI:17968; Evidence={ECO:0000256|ARBA:ARBA00001892}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45249; CC Evidence={ECO:0000256|ARBA:ARBA00001892}; CC -!- CATALYTIC ACTIVITY: CC Reaction=hexadecanoate(out) = hexadecanoate(in); Xref=Rhea:RHEA:45256, CC ChEBI:CHEBI:7896; Evidence={ECO:0000256|ARBA:ARBA00000934}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45257; CC Evidence={ECO:0000256|ARBA:ARBA00000934}; CC -!- CATALYTIC ACTIVITY: CC Reaction=tetracosanoate(out) = tetracosanoate(in); CC Xref=Rhea:RHEA:45260, ChEBI:CHEBI:31014; CC Evidence={ECO:0000256|ARBA:ARBA00023949}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45261; CC Evidence={ECO:0000256|ARBA:ARBA00023949}; CC -!- CATALYTIC ACTIVITY: CC Reaction=tetradecanoate(out) = tetradecanoate(in); CC Xref=Rhea:RHEA:45252, ChEBI:CHEBI:30807; CC Evidence={ECO:0000256|ARBA:ARBA00000996}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45253; CC Evidence={ECO:0000256|ARBA:ARBA00000996}; CC -!- SUBCELLULAR LOCATION: Apical cell membrane CC {ECO:0000256|ARBA:ARBA00004221}. Cell membrane CC {ECO:0000256|ARBA:ARBA00004236}. Golgi apparatus CC {ECO:0000256|ARBA:ARBA00004555}. Membrane raft CC {ECO:0000256|ARBA:ARBA00004285}. CC -!- SIMILARITY: Belongs to the CD36 family. CC {ECO:0000256|ARBA:ARBA00010532}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR Ensembl; ENSSSCT00035076818.1; ENSSSCP00035031394.1; ENSSSCG00035057183.1. DR Ensembl; ENSSSCT00040076228.1; ENSSSCP00040032753.1; ENSSSCG00040045688.1. DR Ensembl; ENSSSCT00045065334.1; ENSSSCP00045046230.1; ENSSSCG00045037617.1. DR Ensembl; ENSSSCT00060043742.1; ENSSSCP00060018662.1; ENSSSCG00060031988.1. DR Ensembl; ENSSSCT00065078150.1; ENSSSCP00065033989.1; ENSSSCG00065056849.1. DR Proteomes; UP000694720; Unplaced. DR Proteomes; UP000694722; Unplaced. DR Proteomes; UP000694723; Unplaced. DR Proteomes; UP000694725; Unplaced. DR Proteomes; UP000694728; Unplaced. DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005901; C:caveola; IEA:TreeGrafter. DR GO; GO:0009986; C:cell surface; IEA:TreeGrafter. DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell. DR GO; GO:0030169; F:low-density lipoprotein particle binding; IEA:TreeGrafter. DR GO; GO:0005041; F:low-density lipoprotein particle receptor activity; IEA:TreeGrafter. DR GO; GO:0005044; F:scavenger receptor activity; IEA:TreeGrafter. DR GO; GO:0150094; P:amyloid-beta clearance by cellular catabolic process; IEA:TreeGrafter. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0019915; P:lipid storage; IEA:TreeGrafter. DR GO; GO:0042953; P:lipoprotein transport; IEA:TreeGrafter. DR GO; GO:0044539; P:long-chain fatty acid import into cell; IEA:TreeGrafter. DR GO; GO:0034383; P:low-density lipoprotein particle clearance; IEA:TreeGrafter. DR GO; GO:0006898; P:receptor-mediated endocytosis; IEA:TreeGrafter. DR InterPro; IPR005428; CD36/SCARB1/SNMP1. DR InterPro; IPR002159; CD36_fam. DR PANTHER; PTHR11923:SF12; PLATELET GLYCOPROTEIN 4; 1. DR PANTHER; PTHR11923; SCAVENGER RECEPTOR CLASS B TYPE-1 SR-B1; 1. DR Pfam; PF01130; CD36; 1. DR PRINTS; PR01610; CD36ANTIGEN. DR PRINTS; PR01609; CD36FAMILY. PE 3: Inferred from homology; KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889}; KW Disulfide bond {ECO:0000256|PIRSR:PIRSR605428-52}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034}; KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499, KW ECO:0000256|PIRSR:PIRSR605428-51}; KW Lipid transport {ECO:0000256|ARBA:ARBA00023055}; KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Palmitate {ECO:0000256|ARBA:ARBA00023139}; KW Receptor {ECO:0000256|ARBA:ARBA00023170}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}; KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843, KW ECO:0000256|PIRSR:PIRSR605428-51}. FT TRANSMEM 61..83 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 359..384 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT SITE 384 FT /note="Critical for TLR4-TLR6 dimerization and signaling" FT /evidence="ECO:0000256|PIRSR:PIRSR605428-50" FT DISULFID 164..232 FT /evidence="ECO:0000256|PIRSR:PIRSR605428-52" FT DISULFID 193..254 FT /evidence="ECO:0000256|PIRSR:PIRSR605428-52" FT DISULFID 234..243 FT /evidence="ECO:0000256|PIRSR:PIRSR605428-52" FT CROSSLNK 390 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000256|PIRSR:PIRSR605428-51" SQ SEQUENCE 393 AA; 44308 MW; 1D24F188CB38403F CRC64; SGMEGNLSVK QKLYSIRYLA KKNIVQDPKT HTVSFLQPKG AIFEPSLSVG TENDTFTVLN LAVAAAPHLY PSAFIQLILN VFIKRSKSSM FQKRTLKELL WGYTDPFLNL IPYSTPTTVG MFYPHHNTSD GVYKVFSGKN DASKVAIIDS YKGKKNLPYW PSYCGMINGT DGASFPPFIE KTRVLRFFAS EICRSFYAVF GAEVNLKGIP VYRFILPSMT FASPLQNPEN RCFCTEKIIS KNCTLYGVLD ISKCKEGKPV YISLPHFLHA SPEIAKTIEG LNPNQEEHST YLDVEPITGF TLRFAQRLQI NLLVKPARII EALKNLKQNY IVPVLWLNET GTISDEKAEM FRKQVTEKIN LLGLVEMILL SVGVVMFIAF MISYCTCRSK KVN //