CD36_MOUSE
ID CD36_MOUSE Reviewed; 472 AA.
AC Q08857;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Platelet glycoprotein 4;
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Peritoneal macrophage;
RX PubMed=7685021; DOI=10.1016/s0021-9258(19)50272-1;
RA Endemann G., Stanton L.W., Madden K.S., Bryant C.M., White R.T.,
RA Protter A.A.;
RT "CD36 is a receptor for oxidized low density lipoprotein.";
RL J. Biol. Chem. 268:11811-11816(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
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 [4]
RP INTERACTION WITH THBS2, AND FUNCTION.
RX PubMed=15748999; DOI=10.1016/j.matbio.2004.11.005;
RA Simantov R., Febbraio M., Silverstein R.L.;
RT "The antiangiogenic effect of thrombospondin-2 is mediated by CD36 and
RT modulated by histidine-rich glycoprotein.";
RL Matrix Biol. 24:27-34(2005).
RN [5]
RP FUNCTION.
RX PubMed=15690042; DOI=10.1038/nature03253;
RA Hoebe K., Georgel P., Rutschmann S., Du X., Mudd S., Crozat K., Sovath S.,
RA Shamel L., Hartung T., Zaehringer U., Beutler B.;
RT "CD36 is a sensor of diacylglycerides.";
RL Nature 433:523-527(2005).
RN [6]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=16020694; DOI=10.1126/science.1116006;
RA Philips J.A., Rubin E.J., Perrimon N.;
RT "Drosophila RNAi screen reveals CD36 family member required for
RT mycobacterial infection.";
RL Science 309:1251-1253(2005).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=17507371; DOI=10.1074/jbc.m703330200;
RA Nassir F., Wilson B., Han X., Gross R.W., Abumrad N.A.;
RT "CD36 is important for fatty acid and cholesterol uptake by the proximal
RT but not distal intestine.";
RL J. Biol. Chem. 282:19493-19501(2007).
RN [8]
RP FUNCTION.
RX PubMed=18162488; DOI=10.1096/fj.07-8415com;
RA Gaillard D., Laugerette F., Darcel N., El-Yassimi A., Passilly-Degrace P.,
RA Hichami A., Khan N.A., Montmayeur J.P., Besnard P.;
RT "The gustatory pathway is involved in CD36-mediated orosensory perception
RT of long-chain fatty acids in the mouse.";
RL FASEB J. 22:1458-1468(2008).
RN [9]
RP UBIQUITINATION.
RX PubMed=18353783; DOI=10.1074/jbc.m800008200;
RA Smith J., Su X., El-Maghrabi R., Stahl P.D., Abumrad N.A.;
RT "Opposite regulation of CD36 ubiquitination by fatty acids and insulin:
RT effects on fatty acid uptake.";
RL J. Biol. Chem. 283:13578-13585(2008).
RN [10]
RP FUNCTION (MICROBIAL INFECTION), AND TISSUE SPECIFICITY.
RC TISSUE=Macrophage;
RX PubMed=19362712; DOI=10.1016/j.cellimm.2009.03.008;
RA Drage M.G., Pecora N.D., Hise A.G., Febbraio M., Silverstein R.L.,
RA Golenbock D.T., Boom W.H., Harding C.V.;
RT "TLR2 and its co-receptors determine responses of macrophages and dendritic
RT cells to lipoproteins of Mycobacterium tuberculosis.";
RL Cell. Immunol. 258:29-37(2009).
RN [11]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=19864601; DOI=10.4049/jimmunol.0901374;
RA Erdman L.K., Cosio G., Helmers A.J., Gowda D.C., Grinstein S., Kain K.C.;
RT "CD36 and TLR interactions in inflammation and phagocytosis: implications
RT for malaria.";
RL J. Immunol. 183:6452-6459(2009).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18753675; DOI=10.1194/jlr.p700032-jlr200;
RA Masuda D., Hirano K., Oku H., Sandoval J.C., Kawase R., Yuasa-Kawase M.,
RA Yamashita Y., Takada M., Tsubakio-Yamamoto K., Tochino Y., Koseki M.,
RA Matsuura F., Nishida M., Kawamoto T., Ishigami M., Hori M., Shimomura I.,
RA Yamashita S.;
RT "Chylomicron remnants are increased in the postprandial state in CD36
RT deficiency.";
RL J. Lipid Res. 50:999-1011(2009).
RN [13]
RP FUNCTION.
RX PubMed=19847289; DOI=10.1371/journal.pone.0007411;
RA Jimenez-Dalmaroni M.J., Xiao N., Corper A.L., Verdino P., Ainge G.D.,
RA Larsen D.S., Painter G.F., Rudd P.M., Dwek R.A., Hoebe K., Beutler B.,
RA Wilson I.A.;
RT "Soluble CD36 ectodomain binds negatively charged diacylglycerol ligands
RT and acts as a co-receptor for TLR2.";
RL PLoS ONE 4:E7411-E7411(2009).
RN [14]
RP REVIEW OF FUNCTION.
RX PubMed=19471024; DOI=10.1126/scisignal.272re3;
RA Silverstein R.L., Febbraio M.;
RT "CD36, a scavenger receptor involved in immunity, metabolism, angiogenesis,
RT and behavior.";
RL Sci. Signal. 2:RE3-RE3(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20037584; DOI=10.1038/ni.1836;
RA Stewart C.R., Stuart L.M., Wilkinson K., van Gils J.M., Deng J., Halle A.,
RA Rayner K.J., Boyer L., Zhong R., Frazier W.A., Lacy-Hulbert A.,
RA El Khoury J., Golenbock D.T., Moore K.J.;
RT "CD36 ligands promote sterile inflammation through assembly of a Toll-like
RT receptor 4 and 6 heterodimer.";
RL Nat. Immunol. 11:155-161(2010).
RN [17]
RP FUNCTION, 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 [18]
RP TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21901153; DOI=10.1371/journal.pone.0024014;
RA Martin C., Passilly-Degrace P., Gaillard D., Merlin J.F., Chevrot M.,
RA Besnard P.;
RT "The lipid-sensor candidates CD36 and GPR120 are differentially regulated
RT by dietary lipids in mouse taste buds: impact on spontaneous fat
RT preference.";
RL PLoS ONE 6:E24014-E24014(2011).
RN [19]
RP FUNCTION, FUNCTION (MICROBIAL INFECTION), INTERACTION WITH FCER1G; ITGB1;
RP ITGB2; CD9 AND CD81, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23395392; DOI=10.1016/j.devcel.2013.01.007;
RA Heit B., Kim H., Cosio G., Castano D., Collins R., Lowell C.A., Kain K.C.,
RA Trimble W.S., Grinstein S.;
RT "Multimolecular signaling complexes enable Syk-mediated signaling of CD36
RT internalization.";
RL Dev. Cell 24:372-383(2013).
RN [20]
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).
RN [21]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23812099; DOI=10.1038/ni.2639;
RA Sheedy F.J., Grebe A., Rayner K.J., Kalantari P., Ramkhelawon B.,
RA Carpenter S.B., Becker C.E., Ediriweera H.N., Mullick A.E., Golenbock D.T.,
RA Stuart L.M., Latz E., Fitzgerald K.A., Moore K.J.;
RT "CD36 coordinates NLRP3 inflammasome activation by facilitating
RT intracellular nucleation of soluble ligands into particulate ligands in
RT sterile inflammation.";
RL Nat. Immunol. 14:812-820(2013).
RN [22]
RP FUNCTION, PALMITOYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=30605677; DOI=10.1016/j.celrep.2018.12.022;
RA Wang J., Hao J.W., Wang X., Guo H., Sun H.H., Lai X.Y., Liu L.Y., Zhu M.,
RA Wang H.Y., Li Y.F., Yu L.Y., Xie C., Wang H.R., Mo W., Zhou H.M., Chen S.,
RA Liang G., Zhao T.J.;
RT "DHHC4 and DHHC5 Facilitate Fatty Acid Uptake by Palmitoylating and
RT Targeting CD36 to the Plasma Membrane.";
RL Cell Rep. 26:209-221(2019).
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 (PubMed:7685021). They are generally multivalent and can
CC therefore engage multiple receptors simultaneously, the resulting
CC formation of CD36 clusters initiates signal transduction and
CC internalization of receptor-ligand complexes. The dependency on
CC coreceptor signaling is strongly ligand specific. Cellular responses to
CC these ligands are involved in angiogenesis, inflammatory response,
CC fatty acid metabolism, taste and dietary fat processing in the
CC intestine (Probable) (PubMed:19847289, PubMed:20037584,
CC PubMed:23395392). 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 (PubMed:30605677).
CC Mechanistically, binding of fatty acids activates downstream kinase
CC LYN, which phosphorylates the palmitoyltransferase ZDHHC5 and
CC inactivates it resulting in the subsequent depalmitoylation of CD36 and
CC caveolar endocytosis (By similarity). In the small intestine, plays a
CC role in proximal absorption of dietary fatty acid and cholesterol for
CC optimal chylomicron formation, possibly through the activation of
CC MAPK1/3 (ERK1/2) signaling pathway (By similarity) (PubMed:17507371,
CC PubMed:18753675, PubMed:21610069). Involved in oral fat perception and
CC preferences (PubMed:16276419). Detection into the tongue of long-chain
CC fatty acids leads to a rapid and sustained rise in flux and protein
CC 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 (PubMed:18162488). 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 (PubMed:15748999). As a
CC coreceptor 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 (PubMed:20037584, PubMed:23812099). Selective and
CC nonredundant sensor of microbial diacylated lipopeptide that signal via
CC TLR2:TLR6 heterodimer, this cluster triggers signaling from the cell
CC surface, leading to the NF-kappa-B-dependent production of TNF, via
CC MYD88 signaling pathway and subsequently is targeted to the Golgi in a
CC lipid-raft dependent pathway (By similarity) (PubMed:15690042,
CC PubMed:19847289). {ECO:0000250|UniProtKB:P16671,
CC ECO:0000250|UniProtKB:Q07969, ECO:0000269|PubMed:15690042,
CC ECO:0000269|PubMed:15748999, ECO:0000269|PubMed:16276419,
CC ECO:0000269|PubMed:17507371, ECO:0000269|PubMed:18162488,
CC ECO:0000269|PubMed:18753675, ECO:0000269|PubMed:19847289,
CC ECO:0000269|PubMed:20037584, ECO:0000269|PubMed:21610069,
CC ECO:0000269|PubMed:23395392, ECO:0000269|PubMed:23557700,
CC ECO:0000269|PubMed:23812099, ECO:0000269|PubMed:30605677,
CC ECO:0000269|PubMed:7685021, ECO:0000305|PubMed:19471024}.
CC -!- FUNCTION: (Microbial infection) Acts as an accessory receptor for
CC M.tuberculosis lipoprotein LprA, in conjunction with coreceptors TLR2
CC and TLR1; the lipoprotein acts as an agonist to modulate antigen
CC presenting cell functions in response to the pathogen
CC (PubMed:19362712). Directly mediates cytoadherence of Plasmodium
CC falciparum parasitized erythrocytes and the internalization of
CC particles independently of TLR signaling (PubMed:19864601,
CC PubMed:23395392). Mediates uptake of E.coli and S.aureus but has no
CC effect on uptake of M.fortuitum (PubMed:16020694).
CC {ECO:0000269|PubMed:16020694, ECO:0000269|PubMed:19362712,
CC ECO:0000269|PubMed:19864601, ECO:0000269|PubMed:23395392}.
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 (By similarity) (PubMed:15748999). Upon
CC interaction with a ligand, such as oxidized low-density lipoprotein
CC (oxLDL) or amyloid-beta 42, rapidly forms a complex with TLR4 and TLR6;
CC the complex is internalized and triggers an inflammatory signal.
CC Through its C-terminus, interacts with PTK2, PXN and LYN, but not with
CC SRC. LYN kinase activity is required for facilitating TLR4-TLR6
CC heterodimerization and signal initiation (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 (PubMed:23395392). {ECO:0000250|UniProtKB:P16671,
CC ECO:0000269|PubMed:15748999, ECO:0000269|PubMed:23395392}.
CC -!- INTERACTION:
CC Q08857; P07948: LYN; Xeno; NbExp=2; IntAct=EBI-8346984, EBI-79452;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23395392,
CC ECO:0000269|PubMed:30605677}; Multi-pass membrane protein
CC {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:16276419,
CC ECO:0000269|PubMed:21610069}. Membrane raft
CC {ECO:0000250|UniProtKB:P16671}. Golgi apparatus
CC {ECO:0000250|UniProtKB:P16671}. Note=Upon ligand-binding, internalized
CC through dynamin-dependent endocytosis. {ECO:0000250|UniProtKB:P16671}.
CC -!- TISSUE SPECIFICITY: Expressed in the apical side of lingual taste bud
CC cells of the circumvallate papillae (PubMed:16276419, PubMed:21901153).
CC Highly expressed in the intestine on the luminal surface of
CC enterocytes. In small intestines expression levels follow a steep
CC decreasing gradient from proximal to distal segments (PubMed:17507371).
CC Expressed in macrophages (PubMed:23395392, PubMed:23812099). Cell
CC surface expression detected in lung alveolar macrophages, dendritic
CC macrophages and lung macrophages (at protein level) (PubMed:19362712).
CC {ECO:0000269|PubMed:16276419, ECO:0000269|PubMed:17507371,
CC ECO:0000269|PubMed:19362712, ECO:0000269|PubMed:21901153,
CC ECO:0000269|PubMed:23395392, ECO:0000269|PubMed:23812099}.
CC -!- INDUCTION: Expressed in a circadian manner in the circumvallate
CC papillae, levels being lower during the dark period. Protein levels
CC decrease in presence of lipids. {ECO:0000269|PubMed:21901153}.
CC -!- PTM: Palmitoylated by ZDHHC5. Palmitoylation is required for proper
CC localization at the plasma membrane. {ECO:0000269|PubMed:30605677}.
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, PubMed:18353783). Ubiquitination and
CC degradation are inhibited by insulin which blocks the effect of fatty
CC acids (PubMed:18353783). {ECO:0000269|PubMed:18353783,
CC ECO:0000269|PubMed:21610069}.
CC -!- DISRUPTION PHENOTYPE: The preference to lipids such linoleic acid is
CC fully abolished in mutant mice as well as the induction of both flux
CC and protein content of pancreatobiliary secretions (PubMed:21901153,
CC PubMed:16276419). Animals with a double knockout of APOE and CD36, fed
CC a Western diet for 12 weeks, exhibit much lower levels of CXCL1, CXCL2
CC and CCL5 cytokine mRNA expression in the descending aorta and a
CC corresponding decrease in atherosclerotic lesion formation, compared to
CC APOE single knockout mice. Enterocytes from proximal small intestine
CC exhibit reduced uptake of fatty acid and cholesterol. They also show
CC reduced fatty acid incorporation into triglycerides and triglyceride
CC secretion (PubMed:17507371). After oral fat loading, animals have
CC lipoproteins smaller than chylomicron in size in plasma and intestinal
CC lymph (PubMed:18753675). {ECO:0000269|PubMed:16276419,
CC ECO:0000269|PubMed:17507371, ECO:0000269|PubMed:18753675,
CC ECO:0000269|PubMed:20037584, ECO:0000269|PubMed:21901153}.
CC -!- SIMILARITY: Belongs to the CD36 family. {ECO:0000305}.
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DR EMBL; L23108; AAA53028.1; -; mRNA.
DR EMBL; BC010262; AAH10262.1; -; mRNA.
DR CCDS; CCDS19100.1; -.
DR PIR; I49590; I49590.
DR RefSeq; NP_001153027.1; NM_001159555.1.
DR RefSeq; NP_001153028.1; NM_001159556.1.
DR RefSeq; NP_001153029.1; NM_001159557.1.
DR RefSeq; NP_001153030.1; NM_001159558.1.
DR RefSeq; NP_031669.3; NM_007643.4.
DR RefSeq; XP_006535683.1; XM_006535620.3.
DR RefSeq; XP_006535684.1; XM_006535621.3.
DR RefSeq; XP_006535685.1; XM_006535622.3.
DR RefSeq; XP_006535686.1; XM_006535623.3.
DR RefSeq; XP_006535687.1; XM_006535624.3.
DR RefSeq; XP_006535688.1; XM_006535625.1.
DR AlphaFoldDB; Q08857; -.
DR SMR; Q08857; -.
DR BioGRID; 198587; 6.
DR CORUM; Q08857; -.
DR IntAct; Q08857; 7.
DR STRING; 10090.ENSMUSP00000131832; -.
DR ChEMBL; CHEMBL2176845; -.
DR TCDB; 9.B.39.1.1; the long chain fatty acid translocase (lcfat) family.
DR GlyConnect; 2588; 3 N-Linked glycans (1 site).
DR GlyGen; Q08857; 8 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q08857; -.
DR PhosphoSitePlus; Q08857; -.
DR SwissPalm; Q08857; -.
DR jPOST; Q08857; -.
DR PaxDb; Q08857; -.
DR PeptideAtlas; Q08857; -.
DR PRIDE; Q08857; -.
DR ProteomicsDB; 281267; -.
DR Antibodypedia; 659; 1753 antibodies from 49 providers.
DR DNASU; 12491; -.
DR Ensembl; ENSMUST00000082367; ENSMUSP00000080974; ENSMUSG00000002944.
DR Ensembl; ENSMUST00000165232; ENSMUSP00000126300; ENSMUSG00000002944.
DR Ensembl; ENSMUST00000169095; ENSMUSP00000131832; ENSMUSG00000002944.
DR Ensembl; ENSMUST00000170051; ENSMUSP00000133008; ENSMUSG00000002944.
DR Ensembl; ENSMUST00000197890; ENSMUSP00000143061; ENSMUSG00000002944.
DR GeneID; 12491; -.
DR KEGG; mmu:12491; -.
DR UCSC; uc008wnn.2; mouse.
DR CTD; 948; -.
DR MGI; MGI:107899; Cd36.
DR VEuPathDB; HostDB:ENSMUSG00000002944; -.
DR eggNOG; KOG3776; Eukaryota.
DR GeneTree; ENSGT00940000153372; -.
DR HOGENOM; CLU_019853_0_0_1; -.
DR InParanoid; Q08857; -.
DR OMA; IVKSNGC; -.
DR OrthoDB; 1106566at2759; -.
DR PhylomeDB; Q08857; -.
DR TreeFam; TF317925; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-1236973; Cross-presentation of particulate exogenous antigens (phagosomes).
DR Reactome; R-MMU-3000471; Scavenging by Class B Receptors.
DR Reactome; R-MMU-434313; Intracellular metabolism of fatty acids regulates insulin secretion.
DR Reactome; R-MMU-5686938; Regulation of TLR by endogenous ligand.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 12491; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Cd36; mouse.
DR PRO; PR:Q08857; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q08857; protein.
DR Bgee; ENSMUSG00000002944; Expressed in right lung and 212 other tissues.
DR ExpressionAtlas; Q08857; baseline and differential.
DR Genevisible; Q08857; MM.
DR GO; GO:0045177; C:apical part of cell; IDA:UniProtKB.
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; ISO:MGI.
DR GO; GO:0071944; C:cell periphery; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; ISO:MGI.
DR GO; GO:0001540; F:amyloid-beta binding; ISO:MGI.
DR GO; GO:0008035; F:high-density lipoprotein particle binding; IDA:MGI.
DR GO; GO:0008289; F:lipid binding; ISS:BHF-UCL.
DR GO; GO:0071813; F:lipoprotein particle binding; ISO:MGI.
DR GO; GO:0070892; F:lipoteichoic acid immune receptor activity; IMP:MGI.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; ISO:MGI.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; IMP:BHF-UCL.
DR GO; GO:0005041; F:low-density lipoprotein particle receptor activity; IMP:BHF-UCL.
DR GO; GO:1901480; F:oleate transmembrane transporter activity; ISO:MGI.
DR GO; GO:0070538; F:oleic acid binding; ISO:MGI.
DR GO; GO:0150025; F:oxidised low-density lipoprotein particle receptor activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0005044; F:scavenger receptor activity; ISO:MGI.
DR GO; GO:0015636; F:short-chain fatty acid transmembrane transporter activity; ISO:MGI.
DR GO; GO:0070053; F:thrombospondin receptor activity; ISO:MGI.
DR GO; GO:0035325; F:Toll-like receptor binding; ISO:MGI.
DR GO; GO:0050431; F:transforming growth factor beta binding; ISO:MGI.
DR GO; GO:1990000; P:amyloid fibril formation; IDA:UniProtKB.
DR GO; GO:0150094; P:amyloid-beta clearance by cellular catabolic process; ISO:MGI.
DR GO; GO:0043277; P:apoptotic cell clearance; IMP:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:1904646; P:cellular response to amyloid-beta; ISO:MGI.
DR GO; GO:0071221; P:cellular response to bacterial lipopeptide; IMP:MGI.
DR GO; GO:0071726; P:cellular response to diacyl bacterial lipopeptide; ISS:UniProtKB.
DR GO; GO:0071447; P:cellular response to hydroperoxide; IMP:BHF-UCL.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:MGI.
DR GO; GO:0071223; P:cellular response to lipoteichoic acid; IDA:MGI.
DR GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; IDA:UniProtKB.
DR GO; GO:0140052; P:cellular response to oxidised low-density lipoprotein particle stimulus; ISO:MGI.
DR GO; GO:0019934; P:cGMP-mediated signaling; ISO:MGI.
DR GO; GO:0070508; P:cholesterol import; IMP:UniProtKB.
DR GO; GO:0030301; P:cholesterol transport; IMP:BHF-UCL.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:MGI.
DR GO; GO:0042755; P:eating behavior; ISO:MGI.
DR GO; GO:0097009; P:energy homeostasis; IMP:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; ISO:MGI.
DR GO; GO:0019395; P:fatty acid oxidation; ISO:MGI.
DR GO; GO:0015908; P:fatty acid transport; ISO:MGI.
DR GO; GO:0042593; P:glucose homeostasis; ISO:MGI.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0050892; P:intestinal absorption; IMP:UniProtKB.
DR GO; GO:0030299; P:intestinal cholesterol absorption; IMP:UniProtKB.
DR GO; GO:0019915; P:lipid storage; IMP:BHF-UCL.
DR GO; GO:1990379; P:lipid transport across blood-brain barrier; ISO:MGI.
DR GO; GO:0042953; P:lipoprotein transport; IMP:BHF-UCL.
DR GO; GO:0015911; P:long-chain fatty acid import across plasma membrane; ISO:MGI.
DR GO; GO:0044539; P:long-chain fatty acid import into cell; IMP:UniProtKB.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; ISO:MGI.
DR GO; GO:0015909; P:long-chain fatty acid transport; ISO:MGI.
DR GO; GO:0034383; P:low-density lipoprotein particle clearance; IMP:BHF-UCL.
DR GO; GO:0055096; P:low-density lipoprotein particle mediated signaling; IDA:BHF-UCL.
DR GO; GO:0000165; P:MAPK cascade; IMP:MGI.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; IMP:BHF-UCL.
DR GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0007263; P:nitric oxide mediated signal transduction; ISO:MGI.
DR GO; GO:0150024; P:oxidised low-density lipoprotein particle clearance; ISO:MGI.
DR GO; GO:0006910; P:phagocytosis, recognition; IDA:MGI.
DR GO; GO:0034381; P:plasma lipoprotein particle clearance; IMP:BHF-UCL.
DR GO; GO:0030194; P:positive regulation of blood coagulation; IMP:BHF-UCL.
DR GO; GO:2000334; P:positive regulation of blood microparticle formation; IMP:BHF-UCL.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISO:MGI.
DR GO; GO:0010886; P:positive regulation of cholesterol storage; IMP:BHF-UCL.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISO:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; ISO:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:MGI.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IDA:UniProtKB.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; IMP:MGI.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:MGI.
DR GO; GO:0060907; P:positive regulation of macrophage cytokine production; IMP:MGI.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IMP:BHF-UCL.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IGI:ARUK-UCL.
DR GO; GO:1900227; P:positive regulation of NLRP3 inflammasome complex assembly; IDA:UniProtKB.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISO:MGI.
DR GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; IDA:MGI.
DR GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; IMP:ARUK-UCL.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IMP:BHF-UCL.
DR GO; GO:0090208; P:positive regulation of triglyceride metabolic process; ISO:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:MGI.
DR GO; GO:0031623; P:receptor internalization; IDA:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISO:MGI.
DR GO; GO:0098900; P:regulation of action potential; IMP:ARUK-UCL.
DR GO; GO:0043254; P:regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:2000121; P:regulation of removal of superoxide radicals; IMP:BHF-UCL.
DR GO; GO:0034121; P:regulation of toll-like receptor signaling pathway; ISO:MGI.
DR GO; GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IC:BHF-UCL.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0070542; P:response to fatty acid; IDA:UniProtKB.
DR GO; GO:0070543; P:response to linoleic acid; IDA:UniProtKB.
DR GO; GO:0033993; P:response to lipid; IDA:UniProtKB.
DR GO; GO:0009612; P:response to mechanical stimulus; ISO:MGI.
DR GO; GO:0035634; P:response to stilbenoid; IEP:UniProtKB.
DR GO; GO:0050909; P:sensory perception of taste; IDA:UniProtKB.
DR GO; GO:0015912; P:short-chain fatty acid transport; ISO:MGI.
DR GO; GO:0006641; P:triglyceride metabolic process; ISO:MGI.
DR GO; GO:0034197; P:triglyceride transport; IMP: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; Disulfide bond; Glycoprotein;
KW Golgi apparatus; Isopeptide bond; Lipid transport; Lipoprotein; Membrane;
KW Palmitate; Receptor; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation.
FT CHAIN 1..472
FT /note="Platelet glycoprotein 4"
FT /id="PRO_0000144153"
FT TOPO_DOM 1..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:0000269|PubMed:15748999"
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:0000250"
FT LIPID 7
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
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 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"
SQ 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
