CD36_RAT
ID CD36_RAT Reviewed; 472 AA.
AC Q07969; Q925W0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 3.
DT 25-MAY-2022, entry version 150.
DE RecName: Full=Platelet glycoprotein 4;
DE AltName: Full=Adipocyte membrane protein;
DE AltName: Full=Fatty acid translocase;
DE AltName: Full=Fatty acid transport protein;
DE AltName: Full=Glycoprotein IIIb;
DE Short=GPIIIB;
DE AltName: Full=PAS IV;
DE AltName: Full=PAS-4;
DE AltName: Full=Platelet glycoprotein IV;
DE Short=GPIV;
DE AltName: CD_antigen=CD36;
GN Name=Cd36; Synonyms=Fat;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Adipocyte;
RX PubMed=7688729; DOI=10.1016/s0021-9258(17)46753-6;
RA Abumrad N.A., El-Maghrabi M.R., Amri E.-Z., Lopez E., Grimaldi P.A.;
RT "Cloning of a rat adipocyte membrane protein implicated in binding or
RT transport of long-chain fatty acids that is induced during preadipocyte
RT differentiation. Homology with human CD36.";
RL J. Biol. Chem. 268:17665-17668(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar;
RX PubMed=10409247; DOI=10.1152/ajplung.1999.277.1.l191;
RA Guthmann F., Haupt R., Looman A.C., Spener F., Ruestow B.;
RT "Fatty acid translocase/CD36 mediates the uptake of palmitate by type II
RT pneumocytes.";
RL Am. J. Physiol. 277:L191-L196(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Dark agouti;
RA Zhang X., Mayrhofer G., Ey P.L.;
RT "Potential allele of rat CD36 antigen.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 2-31, AND PALMITOYLATION AT CYS-3 AND CYS-7.
RC TISSUE=Adipocyte;
RX PubMed=7504047;
RA Jochen A., Hays J.;
RT "Purification of the major substrate for palmitoylation in rat adipocytes:
RT N-terminal homology with CD36 and evidence for cell surface acylation.";
RL J. Lipid Res. 34:1783-1792(1993).
RN [5]
RP PROTEIN SEQUENCE OF 2-16, AND FUNCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Adipocyte;
RX PubMed=8320718; DOI=10.1007/bf00231876;
RA Harmon C.M., Abumrad N.A.;
RT "Binding of sulfosuccinimidyl fatty acids to adipocyte membrane proteins:
RT isolation and amino-terminal sequence of an 88-kD protein implicated in
RT transport of long-chain fatty acids.";
RL J. Membr. Biol. 133:43-49(1993).
RN [6]
RP FUNCTION.
RX PubMed=16276419; DOI=10.1172/jci25299;
RA Laugerette F., Passilly-Degrace P., Patris B., Niot I., Febbraio M.,
RA Montmayeur J.P., Besnard P.;
RT "CD36 involvement in orosensory detection of dietary lipids, spontaneous
RT fat preference, and digestive secretions.";
RL J. Clin. Invest. 115:3177-3184(2005).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX PubMed=21610069; DOI=10.1074/jbc.m111.233551;
RA Tran T.T., Poirier H., Clement L., Nassir F., Pelsers M.M., Petit V.,
RA Degrace P., Monnot M.C., Glatz J.F., Abumrad N.A., Besnard P., Niot I.;
RT "Luminal lipid regulates CD36 levels and downstream signaling to stimulate
RT chylomicron synthesis.";
RL J. Biol. Chem. 286:25201-25210(2011).
RN [8]
RP FUNCTION.
RX PubMed=23557700; DOI=10.2337/db12-1689;
RA Le Foll C., Dunn-Meynell A., Musatov S., Magnan C., Levin B.E.;
RT "FAT/CD36: a major regulator of neuronal fatty acid sensing and energy
RT homeostasis in rats and mice.";
RL Diabetes 62:2709-2716(2013).
CC -!- FUNCTION: Multifunctional glycoprotein that acts as receptor for a
CC broad range of ligands. Ligands can be of proteinaceous nature like
CC thrombospondin, fibronectin, collagen or amyloid-beta as well as of
CC lipidic nature such as oxidized low-density lipoprotein (oxLDL),
CC anionic phospholipids, long-chain fatty acids and bacterial diacylated
CC lipopeptides. They are generally multivalent and can therefore engage
CC multiple receptors simultaneously, the resulting formation of CD36
CC clusters initiates signal transduction and internalization of receptor-
CC ligand complexes. The dependency on coreceptor signaling is strongly
CC ligand specific. Cellular responses to these ligands are involved in
CC angiogenesis, inflammatory response, fatty acid metabolism, taste and
CC dietary fat processing in the intestine (By similarity)
CC (PubMed:8320718). Binds long-chain fatty acids and facilitates their
CC transport into cells, thus participating in muscle lipid utilization,
CC adipose energy storage, and gut fat absorption (By similarity)
CC (PubMed:8320718). Mechanistically, binding of fatty acids activates
CC downstream kinase LYN, which phosphorylates the palmitoyltransferase
CC ZDHHC5 and inactivates it resulting in the subsequent depalmitoylation
CC of CD36 and caveolar endocytosis (By similarity). In the small
CC intestine, plays a role in proximal absorption of dietary fatty acid
CC and cholesterol for optimal chylomicron formation, possibly through the
CC activation of MAPK1/3 (ERK1/2) signaling pathway (By similarity)
CC (PubMed:16276419, PubMed:21610069). Involved in oral fat perception and
CC preferences (By similarity) (PubMed:16276419). Detection into the
CC tongue of long-chain fatty acids leads to a rapid and sustained rise in
CC flux and protein content of pancreatobiliary secretions (By similarity)
CC (PubMed:16276419). In taste receptor cells, mediates the induction of
CC an increase in intracellular calcium levels by long-chain fatty acids,
CC leading to the activation of the gustatory neurons in the nucleus of
CC the solitary tract (By similarity). Important factor in both
CC ventromedial hypothalamus neuronal sensing of long-chain fatty acid and
CC the regulation of energy and glucose homeostasis (By similarity)
CC (PubMed:23557700). Receptor for thrombospondins, THBS1 and THBS2,
CC mediating their antiangiogenic effects (By similarity). As a coreceptor
CC for TLR4:TLR6 heterodimer, promotes inflammation in
CC monocytes/macrophages. Upon ligand binding, such as oxLDL or amyloid-
CC beta 42, interacts with the heterodimer TLR4:TLR6, the complex is
CC internalized and triggers inflammatory response, leading to NF-kappa-B-
CC dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88
CC signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway, as
CC well as IL1B secretion, through the priming and activation of the NLRP3
CC inflammasome. Selective and nonredundant sensor of microbial diacylated
CC lipopeptide that signal via TLR2:TLR6 heterodimer, this cluster
CC triggers signaling from the cell surface, leading to the NF-kappa-B-
CC dependent production of TNF, via MYD88 signaling pathway and
CC subsequently is targeted to the Golgi in a lipid-raft dependent pathway
CC (By similarity). {ECO:0000250|UniProtKB:P16671,
CC ECO:0000250|UniProtKB:Q08857, ECO:0000269|PubMed:16276419,
CC ECO:0000269|PubMed:21610069, ECO:0000269|PubMed:23557700,
CC ECO:0000269|PubMed:8320718}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoate(out) = butanoate(in); Xref=Rhea:RHEA:45248,
CC ChEBI:CHEBI:17968; Evidence={ECO:0000250|UniProtKB:P16671};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45249;
CC Evidence={ECO:0000250|UniProtKB:P16671};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate(out) = (9Z)-octadecenoate(in);
CC Xref=Rhea:RHEA:33655, ChEBI:CHEBI:30823;
CC Evidence={ECO:0000250|UniProtKB:P16671};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33656;
CC Evidence={ECO:0000250|UniProtKB:P16671};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate(out) = (9Z,12Z)-
CC octadecadienoate(in); Xref=Rhea:RHEA:45264, ChEBI:CHEBI:30245;
CC Evidence={ECO:0000250|UniProtKB:P16671};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45265;
CC Evidence={ECO:0000250|UniProtKB:P16671};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=tetradecanoate(out) = tetradecanoate(in);
CC Xref=Rhea:RHEA:45252, ChEBI:CHEBI:30807;
CC Evidence={ECO:0000250|UniProtKB:P16671};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45253;
CC Evidence={ECO:0000250|UniProtKB:P16671};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoate(out) = hexadecanoate(in); Xref=Rhea:RHEA:45256,
CC ChEBI:CHEBI:7896; Evidence={ECO:0000250|UniProtKB:P16671};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45257;
CC Evidence={ECO:0000250|UniProtKB:P16671};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=tetracosanoate(out) = tetracosanoate(in);
CC Xref=Rhea:RHEA:45260, ChEBI:CHEBI:31014;
CC Evidence={ECO:0000250|UniProtKB:P16671};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45261;
CC Evidence={ECO:0000250|UniProtKB:P16671};
CC -!- SUBUNIT: Interacts with THBS1 and THBS2; the interactions mediate the
CC THBS antiangiogenic activity. Upon interaction with a ligand, such as
CC oxidized low-density lipoprotein (oxLDL) or amyloid-beta 42, rapidly
CC forms a complex with TLR4 and TLR6; the complex is internalized and
CC triggers an inflammatory signal. Through its C-terminus, interacts with
CC PTK2, PXN and LYN, but not with SRC. LYN kinase activity is required
CC for facilitating TLR4:TLR6 heterodimerization and signal initiation.
CC Upon interaction with ligands such as diacylated lipopeptides,
CC interacts with the TLR2:TLR6 heterodimer (By similarity). Interacts
CC with CD9, CD81, FCER1G, ITGB2 and/or ITGB2; forming a membrane
CC heteromeric complex required for the internalization of CD36 and its
CC ligands (By similarity). {ECO:0000250|UniProtKB:P16671,
CC ECO:0000250|UniProtKB:Q08857}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21610069};
CC Multi-pass membrane protein {ECO:0000255}. Membrane raft
CC {ECO:0000250|UniProtKB:P16671}. Golgi apparatus
CC {ECO:0000250|UniProtKB:P16671}. Apical cell membrane
CC {ECO:0000269|PubMed:21610069}. Note=Upon ligand-binding, internalized
CC through dynamin-dependent endocytosis. {ECO:0000250|UniProtKB:P16671}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in heart, intestine,
CC spleen, adipose tissue, skeletal muscle and, at lower levels, in
CC testes. {ECO:0000269|PubMed:7688729}.
CC -!- DEVELOPMENTAL STAGE: Induced during preadipocyte differentiation.
CC {ECO:0000269|PubMed:7688729}.
CC -!- PTM: Palmitoylated by ZDHHC5. Palmitoylation is required for proper
CC localization at the plasma membrane. {ECO:0000250|UniProtKB:P16671}.
CC -!- PTM: Ubiquitinated at Lys-469 and Lys-472. Ubiquitination is induced by
CC fatty acids such as oleic acid and leads to degradation by the
CC proteasome (PubMed:21610069). Ubiquitination and degradation are
CC inhibited by insulin which blocks the effect of fatty acids (By
CC similarity). {ECO:0000250|UniProtKB:P16671,
CC ECO:0000250|UniProtKB:Q08857, ECO:0000269|PubMed:21610069}.
CC -!- SIMILARITY: Belongs to the CD36 family. {ECO:0000305}.
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 EMBL; L19658; AAA02878.1; -; mRNA.
DR EMBL; AF072411; AAC24876.1; -; mRNA.
DR EMBL; AF113914; AAF25552.1; -; mRNA.
DR PIR; A47402; A47402.
DR AlphaFoldDB; Q07969; -.
DR SMR; Q07969; -.
DR STRING; 10116.ENSRNOP00000058398; -.
DR BindingDB; Q07969; -.
DR ChEMBL; CHEMBL2163174; -.
DR GlyGen; Q07969; 9 sites.
DR iPTMnet; Q07969; -.
DR PhosphoSitePlus; Q07969; -.
DR PaxDb; Q07969; -.
DR PRIDE; Q07969; -.
DR RGD; 2301; Cd36.
DR eggNOG; KOG3776; Eukaryota.
DR InParanoid; Q07969; -.
DR PhylomeDB; Q07969; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-3000471; Scavenging by Class B Receptors.
DR Reactome; R-RNO-434313; Intracellular metabolism of fatty acids regulates insulin secretion.
DR Reactome; R-RNO-5686938; Regulation of TLR by endogenous ligand.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q07969; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0045177; C:apical part of cell; IDA:RGD.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031526; C:brush border membrane; IDA:UniProtKB.
DR GO; GO:0005901; C:caveola; IDA:RGD.
DR GO; GO:0071944; C:cell periphery; ISO:RGD.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0042383; C:sarcolemma; IDA:RGD.
DR GO; GO:0001540; F:amyloid-beta binding; ISO:RGD.
DR GO; GO:0008035; F:high-density lipoprotein particle binding; ISO:RGD.
DR GO; GO:0008289; F:lipid binding; ISO:RGD.
DR GO; GO:0071813; F:lipoprotein particle binding; ISO:RGD.
DR GO; GO:0070892; F:lipoteichoic acid immune receptor activity; ISO:RGD.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; ISO:RGD.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; ISO:RGD.
DR GO; GO:0005041; F:low-density lipoprotein particle receptor activity; ISO:RGD.
DR GO; GO:1901480; F:oleate transmembrane transporter activity; ISO:RGD.
DR GO; GO:0070538; F:oleic acid binding; IDA:RGD.
DR GO; GO:0150025; F:oxidised low-density lipoprotein particle receptor activity; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0005044; F:scavenger receptor activity; IMP:ARUK-UCL.
DR GO; GO:0015636; F:short-chain fatty acid transmembrane transporter activity; ISO:RGD.
DR GO; GO:0070053; F:thrombospondin receptor activity; IDA:BHF-UCL.
DR GO; GO:0035325; F:Toll-like receptor binding; ISO:RGD.
DR GO; GO:0050431; F:transforming growth factor beta binding; IDA:BHF-UCL.
DR GO; GO:1990000; P:amyloid fibril formation; ISS:UniProtKB.
DR GO; GO:0150094; P:amyloid-beta clearance by cellular catabolic process; IMP:ARUK-UCL.
DR GO; GO:0043277; P:apoptotic cell clearance; ISO:RGD.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:RGD.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IEP:RGD.
DR GO; GO:1904646; P:cellular response to amyloid-beta; ISO:RGD.
DR GO; GO:0071221; P:cellular response to bacterial lipopeptide; ISO:RGD.
DR GO; GO:0071726; P:cellular response to diacyl bacterial lipopeptide; ISS:UniProtKB.
DR GO; GO:0071447; P:cellular response to hydroperoxide; ISO:RGD.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:RGD.
DR GO; GO:0071223; P:cellular response to lipoteichoic acid; ISO:RGD.
DR GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISS:UniProtKB.
DR GO; GO:0140052; P:cellular response to oxidised low-density lipoprotein particle stimulus; ISO:RGD.
DR GO; GO:0019934; P:cGMP-mediated signaling; ISO:RGD.
DR GO; GO:0070508; P:cholesterol import; ISS:UniProtKB.
DR GO; GO:0030301; P:cholesterol transport; ISO:RGD.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:RGD.
DR GO; GO:0048565; P:digestive tract development; IEP:RGD.
DR GO; GO:0042755; P:eating behavior; IMP:RGD.
DR GO; GO:0097009; P:energy homeostasis; IMP:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IDA:RGD.
DR GO; GO:0019395; P:fatty acid oxidation; IMP:RGD.
DR GO; GO:0015908; P:fatty acid transport; IDA:RGD.
DR GO; GO:0042593; P:glucose homeostasis; IMP:RGD.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0050892; P:intestinal absorption; ISS:UniProtKB.
DR GO; GO:0030299; P:intestinal cholesterol absorption; ISS:UniProtKB.
DR GO; GO:0019915; P:lipid storage; ISO:RGD.
DR GO; GO:1990379; P:lipid transport across blood-brain barrier; ISO:RGD.
DR GO; GO:0042953; P:lipoprotein transport; ISO:RGD.
DR GO; GO:0015911; P:long-chain fatty acid import across plasma membrane; ISO:RGD.
DR GO; GO:0044539; P:long-chain fatty acid import into cell; ISS:UniProtKB.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; IMP:RGD.
DR GO; GO:0015909; P:long-chain fatty acid transport; IMP:RGD.
DR GO; GO:0034383; P:low-density lipoprotein particle clearance; ISO:RGD.
DR GO; GO:0055096; P:low-density lipoprotein particle mediated signaling; ISO:RGD.
DR GO; GO:0001893; P:maternal placenta development; IEP:RGD.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IMP:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; ISO:RGD.
DR GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; IMP:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0007263; P:nitric oxide mediated signal transduction; ISO:RGD.
DR GO; GO:0150024; P:oxidised low-density lipoprotein particle clearance; ISO:RGD.
DR GO; GO:0006910; P:phagocytosis, recognition; ISO:RGD.
DR GO; GO:0034381; P:plasma lipoprotein particle clearance; ISO:RGD.
DR GO; GO:0030194; P:positive regulation of blood coagulation; ISO:RGD.
DR GO; GO:2000334; P:positive regulation of blood microparticle formation; ISO:RGD.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:RGD.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISO:RGD.
DR GO; GO:0010886; P:positive regulation of cholesterol storage; ISO:RGD.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0001819; P:positive regulation of cytokine production; IMP:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; IDA:RGD.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISS:UniProtKB.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; ISO:RGD.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:RGD.
DR GO; GO:0060907; P:positive regulation of macrophage cytokine production; ISO:RGD.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; ISO:RGD.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:RGD.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:RGD.
DR GO; GO:1900227; P:positive regulation of NLRP3 inflammasome complex assembly; ISS:UniProtKB.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IMP:RGD.
DR GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; ISO:RGD.
DR GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; ISO:RGD.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISO:RGD.
DR GO; GO:0090208; P:positive regulation of triglyceride metabolic process; IDA:RGD.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:RGD.
DR GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IMP:ARUK-UCL.
DR GO; GO:0098900; P:regulation of action potential; ISO:RGD.
DR GO; GO:0043254; P:regulation of protein-containing complex assembly; ISO:RGD.
DR GO; GO:2000121; P:regulation of removal of superoxide radicals; ISO:RGD.
DR GO; GO:0034121; P:regulation of toll-like receptor signaling pathway; ISO:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0070542; P:response to fatty acid; IDA:UniProtKB.
DR GO; GO:0060416; P:response to growth hormone; IEP:RGD.
DR GO; GO:0070543; P:response to linoleic acid; ISS:UniProtKB.
DR GO; GO:0033993; P:response to lipid; IMP:UniProtKB.
DR GO; GO:0009612; P:response to mechanical stimulus; IMP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0035634; P:response to stilbenoid; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0050909; P:sensory perception of taste; ISS:UniProtKB.
DR GO; GO:0015912; P:short-chain fatty acid transport; ISO:RGD.
DR GO; GO:0006641; P:triglyceride metabolic process; IMP:RGD.
DR GO; GO:0034197; P:triglyceride transport; ISS:UniProtKB.
DR InterPro; IPR005428; CD36/SCARB1/SNMP1.
DR InterPro; IPR033076; CD36_chordates.
DR InterPro; IPR002159; CD36_fam.
DR PANTHER; PTHR11923; PTHR11923; 1.
DR PANTHER; PTHR11923:SF12; PTHR11923:SF12; 1.
DR Pfam; PF01130; CD36; 1.
DR PRINTS; PR01610; CD36ANTIGEN.
DR PRINTS; PR01609; CD36FAMILY.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Golgi apparatus; Isopeptide bond; Lipid transport;
KW Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7504047,
FT ECO:0000269|PubMed:8320718"
FT CHAIN 2..472
FT /note="Platelet glycoprotein 4"
FT /id="PRO_0000144154"
FT TOPO_DOM 2..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..439
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 440..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 462..472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 93..120
FT /note="Required for interaction with thrombospondins, THBS1
FT and THBS2"
FT /evidence="ECO:0000250"
FT REGION 460..472
FT /note="Interaction with PTK2, PXN and LYN"
FT /evidence="ECO:0000250|UniProtKB:P16671"
FT SITE 463
FT /note="Critical for TLR4-TLR6 dimerization and signaling"
FT /evidence="ECO:0000250|UniProtKB:P16671"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:7504047"
FT LIPID 7
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:7504047"
FT LIPID 464
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 466
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 243..311
FT /evidence="ECO:0000250"
FT DISULFID 272..333
FT /evidence="ECO:0000250"
FT DISULFID 313..322
FT /evidence="ECO:0000250"
FT CROSSLNK 469
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P16671"
FT CROSSLNK 472
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P16671"
FT CONFLICT 67
FT /note="I -> V (in Ref. 1; AAA02878)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="K -> I (in Ref. 1; AAA02878)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="F -> S (in Ref. 1; AAA02878)"
FT /evidence="ECO:0000305"
FT CONFLICT 257..258
FT /note="FV -> LG (in Ref. 1; AAA02878)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="Q -> R (in Ref. 1; AAA02878)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="I -> N (in Ref. 1; AAA02878)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="N -> T (in Ref. 1; AAA02878)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="A -> S (in Ref. 1; AAA02878)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 472 AA; 52731 MW; 69F9513B1B85CBF0 CRC64;
MGCDRNCGLI TGAVIGAVLA VFGGILMPVG DLLIEKTIKR EVVLEEGTIA FKNWVKTGTT
VYRQFWIFDV QNPEEVAKNS SKIKVKQRGP YTYRVRYLAK ENITQDPKDS TVSFVQPNGA
IFEPSLSVGT ENDNFTVLNL AVAAAPHIYT NSFVQGVLNS LIKKSKSSMF QTRSLKELLW
GYKDPFLSLV PYPISTTVGV FYPYNNTVDG VYKVFNGKDN ISKVAIIDTY KGKRNLSYWE
SYCDMINGTD AASFPPFVEK SQTLRFFSSD ICRSIYAVFE SEVNLKGIPV YRFVLPANAF
ASPLQNPDNH CFCTEKVISN NCTSYGVLDI GKCKEGKPVY ISLPHFLHAS PDVSEPIEGL
NPNEDEHRTY LDVEPITGFT LQFAKRLQVN ILVKPARKIE ALKNLKRPYI VPILWLNETG
TIGDEKAEMF RNQVTGKIKL LGLVEMVLLG VGVVMFVAFM ISYCACRSKN GK
