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Platelet glycoprotein 4 (Glycoprotein IIIb) (GPIIIB) (PAS IV) (PAS-4) (Platelet glycoprotein IV) (GPIV) (CD antigen CD36)

 CD36_MOUSE              Reviewed;         472 AA.
Q08857;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
22-NOV-2017, entry version 149.
RecName: Full=Platelet glycoprotein 4;
AltName: Full=Glycoprotein IIIb;
Short=GPIIIB;
AltName: Full=PAS IV;
AltName: Full=PAS-4;
AltName: Full=Platelet glycoprotein IV;
Short=GPIV;
AltName: CD_antigen=CD36;
Name=Cd36;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Peritoneal macrophage;
PubMed=7685021;
Endemann G., Stanton L.W., Madden K.S., Bryant C.M., White R.T.,
Protter A.A.;
"CD36 is a receptor for oxidized low density lipoprotein.";
J. Biol. Chem. 268:11811-11816(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DISRUPTION
PHENOTYPE.
PubMed=16276419; DOI=10.1172/JCI25299;
Laugerette F., Passilly-Degrace P., Patris B., Niot I., Febbraio M.,
Montmayeur J.P., Besnard P.;
"CD36 involvement in orosensory detection of dietary lipids,
spontaneous fat preference, and digestive secretions.";
J. Clin. Invest. 115:3177-3184(2005).
[4]
INTERACTION WITH THBS2, AND FUNCTION.
PubMed=15748999; DOI=10.1016/j.matbio.2004.11.005;
Simantov R., Febbraio M., Silverstein R.L.;
"The antiangiogenic effect of thrombospondin-2 is mediated by CD36 and
modulated by histidine-rich glycoprotein.";
Matrix Biol. 24:27-34(2005).
[5]
FUNCTION.
PubMed=15690042; DOI=10.1038/nature03253;
Hoebe K., Georgel P., Rutschmann S., Du X., Mudd S., Crozat K.,
Sovath S., Shamel L., Hartung T., Zaehringer U., Beutler B.;
"CD36 is a sensor of diacylglycerides.";
Nature 433:523-527(2005).
[6]
FUNCTION (MICROBIAL INFECTION).
PubMed=16020694; DOI=10.1126/science.1116006;
Philips J.A., Rubin E.J., Perrimon N.;
"Drosophila RNAi screen reveals CD36 family member required for
mycobacterial infection.";
Science 309:1251-1253(2005).
[7]
FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=17507371; DOI=10.1074/jbc.M703330200;
Nassir F., Wilson B., Han X., Gross R.W., Abumrad N.A.;
"CD36 is important for fatty acid and cholesterol uptake by the
proximal but not distal intestine.";
J. Biol. Chem. 282:19493-19501(2007).
[8]
FUNCTION.
PubMed=18162488; DOI=10.1096/fj.07-8415com;
Gaillard D., Laugerette F., Darcel N., El-Yassimi A.,
Passilly-Degrace P., Hichami A., Khan N.A., Montmayeur J.P.,
Besnard P.;
"The gustatory pathway is involved in CD36-mediated orosensory
perception of long-chain fatty acids in the mouse.";
FASEB J. 22:1458-1468(2008).
[9]
UBIQUITINATION.
PubMed=18353783; DOI=10.1074/jbc.M800008200;
Smith J., Su X., El-Maghrabi R., Stahl P.D., Abumrad N.A.;
"Opposite regulation of CD36 ubiquitination by fatty acids and
insulin: effects on fatty acid uptake.";
J. Biol. Chem. 283:13578-13585(2008).
[10]
FUNCTION (MICROBIAL INFECTION), AND TISSUE SPECIFICITY.
TISSUE=Macrophage;
PubMed=19362712; DOI=10.1016/j.cellimm.2009.03.008;
Drage M.G., Pecora N.D., Hise A.G., Febbraio M., Silverstein R.L.,
Golenbock D.T., Boom W.H., Harding C.V.;
"TLR2 and its co-receptors determine responses of macrophages and
dendritic cells to lipoproteins of Mycobacterium tuberculosis.";
Cell. Immunol. 258:29-37(2009).
[11]
FUNCTION (MICROBIAL INFECTION).
PubMed=19864601; DOI=10.4049/jimmunol.0901374;
Erdman L.K., Cosio G., Helmers A.J., Gowda D.C., Grinstein S.,
Kain K.C.;
"CD36 and TLR interactions in inflammation and phagocytosis:
implications for malaria.";
J. Immunol. 183:6452-6459(2009).
[12]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18753675; DOI=10.1194/jlr.P700032-JLR200;
Masuda D., Hirano K., Oku H., Sandoval J.C., Kawase R.,
Yuasa-Kawase M., Yamashita Y., Takada M., Tsubakio-Yamamoto K.,
Tochino Y., Koseki M., Matsuura F., Nishida M., Kawamoto T.,
Ishigami M., Hori M., Shimomura I., Yamashita S.;
"Chylomicron remnants are increased in the postprandial state in CD36
deficiency.";
J. Lipid Res. 50:999-1011(2009).
[13]
FUNCTION.
PubMed=19847289; DOI=10.1371/journal.pone.0007411;
Jimenez-Dalmaroni M.J., Xiao N., Corper A.L., Verdino P., Ainge G.D.,
Larsen D.S., Painter G.F., Rudd P.M., Dwek R.A., Hoebe K., Beutler B.,
Wilson I.A.;
"Soluble CD36 ectodomain binds negatively charged diacylglycerol
ligands and acts as a co-receptor for TLR2.";
PLoS ONE 4:E7411-E7411(2009).
[14]
REVIEW OF FUNCTION.
PubMed=19471024; DOI=10.1126/scisignal.272re3;
Silverstein R.L., Febbraio M.;
"CD36, a scavenger receptor involved in immunity, metabolism,
angiogenesis, and behavior.";
Sci. Signal. 2:RE3-RE3(2009).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[16]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=20037584; DOI=10.1038/ni.1836;
Stewart C.R., Stuart L.M., Wilkinson K., van Gils J.M., Deng J.,
Halle A., Rayner K.J., Boyer L., Zhong R., Frazier W.A.,
Lacy-Hulbert A., El Khoury J., Golenbock D.T., Moore K.J.;
"CD36 ligands promote sterile inflammation through assembly of a Toll-
like receptor 4 and 6 heterodimer.";
Nat. Immunol. 11:155-161(2010).
[17]
FUNCTION, SUBCELLULAR LOCATION, AND UBIQUITINATION.
PubMed=21610069; DOI=10.1074/jbc.M111.233551;
Tran T.T., Poirier H., Clement L., Nassir F., Pelsers M.M., Petit V.,
Degrace P., Monnot M.C., Glatz J.F., Abumrad N.A., Besnard P.,
Niot I.;
"Luminal lipid regulates CD36 levels and downstream signaling to
stimulate chylomicron synthesis.";
J. Biol. Chem. 286:25201-25210(2011).
[18]
TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
PubMed=21901153; DOI=10.1371/journal.pone.0024014;
Martin C., Passilly-Degrace P., Gaillard D., Merlin J.F., Chevrot M.,
Besnard P.;
"The lipid-sensor candidates CD36 and GPR120 are differentially
regulated by dietary lipids in mouse taste buds: impact on spontaneous
fat preference.";
PLoS ONE 6:E24014-E24014(2011).
[19]
FUNCTION, FUNCTION (MICROBIAL INFECTION), INTERACTION WITH FCER1G;
ITGB1; ITGB2; CD9 AND CD81, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=23395392; DOI=10.1016/j.devcel.2013.01.007;
Heit B., Kim H., Cosio G., Castano D., Collins R., Lowell C.A.,
Kain K.C., Trimble W.S., Grinstein S.;
"Multimolecular signaling complexes enable Syk-mediated signaling of
CD36 internalization.";
Dev. Cell 24:372-383(2013).
[20]
FUNCTION.
PubMed=23557700; DOI=10.2337/db12-1689;
Le Foll C., Dunn-Meynell A., Musatov S., Magnan C., Levin B.E.;
"FAT/CD36: a major regulator of neuronal fatty acid sensing and energy
homeostasis in rats and mice.";
Diabetes 62:2709-2716(2013).
[21]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=23812099; DOI=10.1038/ni.2639;
Sheedy F.J., Grebe A., Rayner K.J., Kalantari P., Ramkhelawon B.,
Carpenter S.B., Becker C.E., Ediriweera H.N., Mullick A.E.,
Golenbock D.T., Stuart L.M., Latz E., Fitzgerald K.A., Moore K.J.;
"CD36 coordinates NLRP3 inflammasome activation by facilitating
intracellular nucleation of soluble ligands into particulate ligands
in sterile inflammation.";
Nat. Immunol. 14:812-820(2013).
-!- FUNCTION: Multifunctional glycoprotein that acts as receptor for a
broad range of ligands. Ligands can be of proteinaceous nature
like thrombospondin, fibronectin, collagen or amyloid-beta as well
as of lipidic nature such as oxidized low-density lipoprotein
(oxLDL), anionic phospholipids, long-chain fatty acids and
bacterial diacylated lipopeptides (PubMed:7685021). They are
generally multivalent and can therefore engage multiple receptors
simultaneously, the resulting formation of CD36 clusters initiates
signal transduction and internalization of receptor-ligand
complexes. The dependency on coreceptor signaling is strongly
ligand specific. Cellular responses to these ligands are involved
in angiogenesis, inflammatory response, fatty acid metabolism,
taste and dietary fat processing in the intestine (Probable)
(PubMed:19847289, PubMed:20037584, PubMed:23395392). Binds long-
chain fatty acids and facilitates their transport into cells, thus
participating in muscle lipid utilization, adipose energy storage,
and gut fat absorption (By similarity). In the small intestine,
plays a role in proximal absorption of dietary fatty acid and
cholesterol for optimal chylomicron formation, possibly through
the activation of MAPK1/3 (ERK1/2) signaling pathway (By
similarity) (PubMed:17507371, PubMed:18753675, PubMed:21610069).
Involved in oral fat perception and preferences (PubMed:16276419).
Detection into the tongue of long-chain fatty acids leads to a
rapid and sustained rise in flux and protein content of
pancreatobiliary secretions (By similarity) (PubMed:16276419). In
taste receptor cells, mediates the induction of an increase in
intracellular calcium levels by long-chain fatty acids, leading to
the activation of the gustatory neurons in the nucleus of the
solitary tract (PubMed:18162488). Important factor in both
ventromedial hypothalamus neuronal sensing of long-chain fatty
acid and the regulation of energy and glucose homeostasis (By
similarity) (PubMed:23557700). Receptor for thombospondins, THBS1
and THBS2, mediating their antiangiogenic effects
(PubMed:15748999). As a coreceptor for TLR4:TLR6 heterodimer,
promotes inflammation in monocytes/macrophages. Upon ligand
binding, such as oxLDL or amyloid-beta 42, interacts with the
heterodimer TLR4:TLR6, the complex is internalized and triggers
inflammatory response, leading to NF-kappa-B-dependent production
of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway,
and CCL5 cytokine, via TICAM1 signaling pathway, as well as IL1B
secretion, through the priming and activation of the NLRP3
inflammasome (PubMed:20037584, PubMed:23812099). Selective and
nonredundant sensor of microbial diacylated lipopeptide that
signal via TLR2:TLR6 heterodimer, this cluster triggers signaling
from the cell surface, leading to the NF-kappa-B-dependent
production of TNF, via MYD88 signaling pathway and subsequently is
targeted to the Golgi in a lipid-raft dependent pathway (By
similarity) (PubMed:15690042, PubMed:19847289).
{ECO:0000250|UniProtKB:P16671, ECO:0000250|UniProtKB:Q07969,
ECO:0000269|PubMed:15690042, ECO:0000269|PubMed:15748999,
ECO:0000269|PubMed:16276419, ECO:0000269|PubMed:17507371,
ECO:0000269|PubMed:18162488, ECO:0000269|PubMed:18753675,
ECO:0000269|PubMed:19847289, ECO:0000269|PubMed:20037584,
ECO:0000269|PubMed:21610069, ECO:0000269|PubMed:23395392,
ECO:0000269|PubMed:23557700, ECO:0000269|PubMed:23812099,
ECO:0000269|PubMed:7685021, ECO:0000305|PubMed:19471024}.
-!- FUNCTION: (Microbial infection) Acts as an accessory receptor for
M.tuberculosis lipoprotein LprA, in conjunction with coreceptors
TLR2 and TLR1; the lipoprotein acts as an agonist to modulate
antigen presenting cell functions in response to the pathogen
(PubMed:19362712). Directly mediates cytoadherence of Plasmodium
falciparum parasitized erythrocytes and the internalization of
particles independently of TLR signaling (PubMed:19864601,
PubMed:23395392). Mediates uptake of E.coli and S.aureus but has
no effect on uptake of M.fortuitum (PubMed:16020694).
{ECO:0000269|PubMed:16020694, ECO:0000269|PubMed:19362712,
ECO:0000269|PubMed:19864601, ECO:0000269|PubMed:23395392}.
-!- SUBUNIT: Interacts with THBS1 and THBS2; the interactions mediate
the THBS antiangiogenic activity (By similarity)
(PubMed:15748999). Upon interaction with a ligand, such as
oxidized low-density lipoprotein (oxLDL) or amyloid-beta 42,
rapidly forms a complex with TLR4 and TLR6; the complex is
internalized and triggers an inflammatory signal. Through its C-
terminus, interacts with PTK2, PXN and LYN, but not with SRC. LYN
kinase activity is required for facilitating TLR4-TLR6
heterodimerization and signal initiation (By similarity).
Interacts with CD9, CD81, FCER1G, ITGB2 and/or ITGB2; forming a
membrane heteromeric complex required for the internalization of
CD36 and its ligands (PubMed:23395392).
{ECO:0000250|UniProtKB:P16671, ECO:0000269|PubMed:15748999,
ECO:0000269|PubMed:23395392}.
-!- INTERACTION:
P07948:LYN (xeno); NbExp=2; IntAct=EBI-8346984, EBI-79452;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23395392};
Multi-pass membrane protein {ECO:0000255}. Apical cell membrane
{ECO:0000269|PubMed:16276419, ECO:0000269|PubMed:21610069}.
Membrane raft {ECO:0000250|UniProtKB:P16671}. Golgi apparatus
{ECO:0000250|UniProtKB:P16671}. Note=Upon ligand-binding,
internalized through dynamin-dependent endocytosis.
{ECO:0000250|UniProtKB:P16671}.
-!- TISSUE SPECIFICITY: Expressed in the apical side of lingual taste
bud cells of the circumvallate papillae (PubMed:16276419,
PubMed:21901153). Highly expressed in the intestine on the luminal
surface of enterocytes. In small intestines expression levels
follow a steep decreasing gradient from proximal to distal
segments (PubMed:17507371). Expressed in macrophages
(PubMed:23395392, PubMed:23812099). Cell surface expression
detected in lung alveolar macrophages, dendritic macrophages and
lung macrophages (at protein level) (PubMed:19362712).
{ECO:0000269|PubMed:16276419, ECO:0000269|PubMed:17507371,
ECO:0000269|PubMed:19362712, ECO:0000269|PubMed:21901153,
ECO:0000269|PubMed:23395392, ECO:0000269|PubMed:23812099}.
-!- INDUCTION: Expressed in a circadian manner in the circumvallate
papillae, levels being lower during the dark period. Protein
levels decrease in presence of lipids.
{ECO:0000269|PubMed:21901153}.
-!- PTM: Ubiquitinated at Lys-469 and Lys-472. Ubiquitination is
induced by fatty acids such as oleic acid and leads to degradation
by the proteasome (PubMed:21610069, PubMed:18353783).
Ubiquitination and degradation are inhibited by insulin which
blocks the effect of fatty acids (PubMed:18353783).
{ECO:0000269|PubMed:18353783, ECO:0000269|PubMed:21610069}.
-!- DISRUPTION PHENOTYPE: The preference to lipids such linoleic acid
is fully abolished in mutant mice as well as the induction of both
flux and protein content of pancreatobiliary secretions
(PubMed:21901153, PubMed:16276419). Animals with a double knockout
of APOE and CD36, fed a Western diet for 12 weeks, exhibit much
lower levels of CXCL1, CXCL2 and CCL5 cytokine mRNA expression in
the descending aorta and a corresponding decrease in
atherosclerotic lesion formation, compared to APOE single knockout
mice. Enterocytes from proximal small intestine exhibit reduced
uptake of fatty acid and cholesterol. They also show reduced fatty
acid incorporation into triglycerides and triglyceride secretion
(PubMed:17507371). After oral fat loading, animals have
lipoproteins smaller than chylomicron in size in plasma and
intestinal lymph (PubMed:18753675). {ECO:0000269|PubMed:16276419,
ECO:0000269|PubMed:17507371, ECO:0000269|PubMed:18753675,
ECO:0000269|PubMed:20037584, ECO:0000269|PubMed:21901153}.
-!- SIMILARITY: Belongs to the CD36 family. {ECO:0000305}.
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EMBL; L23108; AAA53028.1; -; mRNA.
EMBL; BC010262; AAH10262.1; -; mRNA.
CCDS; CCDS19100.1; -.
PIR; I49590; I49590.
RefSeq; NP_001153027.1; NM_001159555.1.
RefSeq; NP_001153028.1; NM_001159556.1.
RefSeq; NP_001153029.1; NM_001159557.1.
RefSeq; NP_001153030.1; NM_001159558.1.
RefSeq; NP_031669.3; NM_007643.4.
RefSeq; XP_006535683.1; XM_006535620.3.
RefSeq; XP_006535684.1; XM_006535621.3.
RefSeq; XP_006535685.1; XM_006535622.3.
RefSeq; XP_006535686.1; XM_006535623.3.
RefSeq; XP_006535687.1; XM_006535624.3.
RefSeq; XP_006535688.1; XM_006535625.1.
UniGene; Mm.18628; -.
UniGene; Mm.406799; -.
ProteinModelPortal; Q08857; -.
SMR; Q08857; -.
BioGrid; 198587; 2.
CORUM; Q08857; -.
IntAct; Q08857; 9.
MINT; MINT-4090233; -.
STRING; 10090.ENSMUSP00000080974; -.
ChEMBL; CHEMBL2176845; -.
TCDB; 9.B.39.1.1; the long chain fatty acid translocase (lcfat) family.
iPTMnet; Q08857; -.
PhosphoSitePlus; Q08857; -.
SwissPalm; Q08857; -.
PaxDb; Q08857; -.
PeptideAtlas; Q08857; -.
PRIDE; Q08857; -.
Ensembl; ENSMUST00000082367; ENSMUSP00000080974; ENSMUSG00000002944.
Ensembl; ENSMUST00000165232; ENSMUSP00000126300; ENSMUSG00000002944.
Ensembl; ENSMUST00000169095; ENSMUSP00000131832; ENSMUSG00000002944.
Ensembl; ENSMUST00000170051; ENSMUSP00000133008; ENSMUSG00000002944.
Ensembl; ENSMUST00000197890; ENSMUSP00000143061; ENSMUSG00000002944.
GeneID; 12491; -.
KEGG; mmu:12491; -.
UCSC; uc008wnn.2; mouse.
CTD; 948; -.
MGI; MGI:107899; Cd36.
eggNOG; KOG3776; Eukaryota.
eggNOG; ENOG410XS17; LUCA.
GeneTree; ENSGT00530000062927; -.
HOGENOM; HOG000252951; -.
HOVERGEN; HBG002754; -.
InParanoid; Q08857; -.
KO; K06259; -.
OMA; VEQSVII; -.
OrthoDB; EOG091G0CH9; -.
PhylomeDB; Q08857; -.
TreeFam; TF317925; -.
Reactome; R-MMU-114608; Platelet degranulation.
Reactome; R-MMU-1236973; Cross-presentation of particulate exogenous antigens (phagosomes).
Reactome; R-MMU-3000471; Scavenging by Class B Receptors.
Reactome; R-MMU-5686938; Regulation of TLR by endogenous ligand.
Reactome; R-MMU-6798695; Neutrophil degranulation.
PRO; PR:Q08857; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000002944; -.
CleanEx; MM_CD36; -.
ExpressionAtlas; Q08857; baseline and differential.
Genevisible; Q08857; MM.
GO; GO:0045177; C:apical part of cell; IDA:UniProtKB.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0031526; C:brush border membrane; IDA:UniProtKB.
GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005622; C:intracellular; ISO:MGI.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0043235; C:receptor complex; ISO:MGI.
GO; GO:0008035; F:high-density lipoprotein particle binding; IDA:MGI.
GO; GO:0008289; F:lipid binding; ISS:BHF-UCL.
GO; GO:0071813; F:lipoprotein particle binding; ISO:MGI.
GO; GO:0070892; F:lipoteichoic acid receptor activity; IMP:MGI.
GO; GO:0030169; F:low-density lipoprotein particle binding; IMP:BHF-UCL.
GO; GO:0005041; F:low-density lipoprotein receptor activity; IMP:BHF-UCL.
GO; GO:0035325; F:Toll-like receptor binding; ISO:MGI.
GO; GO:1990000; P:amyloid fibril formation; IDA:UniProtKB.
GO; GO:0043277; P:apoptotic cell clearance; IMP:MGI.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:BHF-UCL.
GO; GO:1904646; P:cellular response to amyloid-beta; ISO:MGI.
GO; GO:0071221; P:cellular response to bacterial lipopeptide; IMP:MGI.
GO; GO:0071726; P:cellular response to diacyl bacterial lipopeptide; ISS:UniProtKB.
GO; GO:0071447; P:cellular response to hydroperoxide; IMP:BHF-UCL.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:MGI.
GO; GO:0071223; P:cellular response to lipoteichoic acid; IDA:MGI.
GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; IDA:UniProtKB.
GO; GO:0140052; P:cellular response to oxidised low-density lipoprotein particle stimulus; ISO:MGI.
GO; GO:0019934; P:cGMP-mediated signaling; ISO:MGI.
GO; GO:0070508; P:cholesterol import; IMP:UniProtKB.
GO; GO:0030301; P:cholesterol transport; IMP:BHF-UCL.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:MGI.
GO; GO:0006955; P:immune response; IEA:InterPro.
GO; GO:0050702; P:interleukin-1 beta secretion; IDA:UniProtKB.
GO; GO:0050892; P:intestinal absorption; IMP:UniProtKB.
GO; GO:0030299; P:intestinal cholesterol absorption; IMP:UniProtKB.
GO; GO:0019915; P:lipid storage; IMP:BHF-UCL.
GO; GO:0042953; P:lipoprotein transport; IMP:BHF-UCL.
GO; GO:0044539; P:long-chain fatty acid import; IMP:UniProtKB.
GO; GO:0034383; P:low-density lipoprotein particle clearance; IMP:BHF-UCL.
GO; GO:0055096; P:low-density lipoprotein particle mediated signaling; IDA:BHF-UCL.
GO; GO:0010629; P:negative regulation of gene expression; IMP:BHF-UCL.
GO; GO:0044130; P:negative regulation of growth of symbiont in host; IMP:MGI.
GO; GO:0042992; P:negative regulation of transcription factor import into nucleus; IMP:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0007263; P:nitric oxide mediated signal transduction; ISO:MGI.
GO; GO:0006910; P:phagocytosis, recognition; IDA:MGI.
GO; GO:0034381; P:plasma lipoprotein particle clearance; IMP:BHF-UCL.
GO; GO:0030194; P:positive regulation of blood coagulation; IMP:BHF-UCL.
GO; GO:2000334; P:positive regulation of blood microparticle formation; IMP:BHF-UCL.
GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISO:MGI.
GO; GO:0010886; P:positive regulation of cholesterol storage; IMP:BHF-UCL.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:MGI.
GO; GO:0032735; P:positive regulation of interleukin-12 production; IMP:MGI.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:MGI.
GO; GO:0060907; P:positive regulation of macrophage cytokine production; IMP:MGI.
GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IMP:BHF-UCL.
GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:MGI.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IGI:ARUK-UCL.
GO; GO:1900227; P:positive regulation of NLRP3 inflammasome complex assembly; IDA:UniProtKB.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL.
GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; IDA:MGI.
GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; IMP:ARUK-UCL.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IMP:BHF-UCL.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:MGI.
GO; GO:0031623; P:receptor internalization; IDA:UniProtKB.
GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
GO; GO:2000505; P:regulation of energy homeostasis; IMP:UniProtKB.
GO; GO:0043497; P:regulation of protein heterodimerization activity; ISO:MGI.
GO; GO:2000121; P:regulation of removal of superoxide radicals; IMP:BHF-UCL.
GO; GO:0034121; P:regulation of toll-like receptor signaling pathway; ISO:MGI.
GO; GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IC:BHF-UCL.
GO; GO:0070542; P:response to fatty acid; IDA:UniProtKB.
GO; GO:0070543; P:response to linoleic acid; IDA:UniProtKB.
GO; GO:0033993; P:response to lipid; IDA:UniProtKB.
GO; GO:0035634; P:response to stilbenoid; IEP:UniProtKB.
GO; GO:0050909; P:sensory perception of taste; IDA:UniProtKB.
GO; GO:0034197; P:triglyceride transport; IMP:UniProtKB.
InterPro; IPR005428; CD36/SCARB1/SNMP1.
InterPro; IPR033076; CD36_chordates.
InterPro; IPR002159; CD36_fam.
PANTHER; PTHR11923; PTHR11923; 1.
PANTHER; PTHR11923:SF12; PTHR11923:SF12; 1.
Pfam; PF01130; CD36; 1.
PRINTS; PR01610; CD36ANTIGEN.
PRINTS; PR01609; CD36FAMILY.
1: Evidence at protein level;
Cell adhesion; Cell membrane; Complete proteome; Disulfide bond;
Glycoprotein; Golgi apparatus; Lipoprotein; Membrane; Palmitate;
Receptor; Reference proteome; Transmembrane; Transmembrane helix;
Transport; Ubl conjugation.
CHAIN 1 472 Platelet glycoprotein 4.
/FTId=PRO_0000144153.
TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.
TRANSMEM 8 29 Helical. {ECO:0000255}.
TOPO_DOM 30 439 Extracellular. {ECO:0000255}.
TRANSMEM 440 461 Helical. {ECO:0000255}.
TOPO_DOM 462 472 Cytoplasmic. {ECO:0000255}.
REGION 93 120 Required for interaction with
thrombospondins, THBS1 and THBS2.
{ECO:0000269|PubMed:15748999}.
REGION 460 472 Interaction with PTK2, PXN and LYN.
{ECO:0000250|UniProtKB:P16671}.
SITE 463 463 Critical for TLR4-TLR6 dimerization and
signaling.
{ECO:0000250|UniProtKB:P16671}.
LIPID 3 3 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 7 7 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 464 464 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 466 466 S-palmitoyl cysteine. {ECO:0000250}.
CARBOHYD 79 79 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 134 134 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 205 205 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 220 220 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 235 235 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 247 247 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 321 321 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 417 417 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 243 311 {ECO:0000250}.
DISULFID 272 333 {ECO:0000250}.
DISULFID 313 322 {ECO:0000250}.
SEQUENCE 472 AA; 52698 MW; 80AEABB18206534F CRC64;
MGCDRNCGLI AGAVIGAVLA VFGGILMPVG DMLIEKTIKR EVVLEEGTTA FKNWVKTGTT
VYRQFWIFDV QNPDDVAKNS SKIKVKQRGP YTYRVRYLAK ENITQDPEDH TVSFVQPNGA
IFEPSLSVGT EDDNFTVLNL AVAAAPHIYQ NSFVQVVLNS LIKKSKSSMF QTRSLKELLW
GYKDPFLSLV PYPISTTVGV FYPYNDTVDG VYKVFNGKDN ISKVAIIESY KGKRNLSYWP
SYCDMINGTD AASFPPFVEK SRTLRFFSSD ICRSIYAVFG SEIDLKGIPV YRFVLPANAF
ASPLQNPDNH CFCTEKVISN NCTSYGVLDI GKCKEGKPVY ISLPHFLHAS PDVSEPIEGL
HPNEDEHRTY LDVEPITGFT LQFAKRLQVN ILVKPARKIE ALKNLKRPYI VPILWLNETG
TIGDEKAEMF KTQVTGKIKL LGMVEMALLG IGVVMFVAFM ISYCACKSKN GK


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