CD36_HUMAN
ID CD36_HUMAN Reviewed; 472 AA.
AC P16671; D9IX66; D9IX67; D9IX68; D9IX69; Q13966; Q16093; Q8TCV7; Q9BPZ8;
AC Q9BQC2; Q9BZM8; Q9BZN3; Q9BZN4; Q9BZN5;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 225.
DE RecName: Full=Platelet glycoprotein 4;
DE AltName: Full=Fatty acid translocase;
DE Short=FAT;
DE AltName: Full=Glycoprotein IIIb;
DE Short=GPIIIB;
DE AltName: Full=Leukocyte differentiation antigen CD36;
DE AltName: Full=PAS IV;
DE AltName: Full=PAS-4;
DE AltName: Full=Platelet collagen receptor;
DE AltName: Full=Platelet glycoprotein IV;
DE Short=GPIV;
DE AltName: Full=Thrombospondin receptor;
DE AltName: CD_antigen=CD36;
GN Name=CD36; Synonyms=GP3B, GP4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=2473841; DOI=10.1016/0092-8674(89)90406-6;
RA Oquendo P., Hundt E., Lawler J., Seed B.;
RT "CD36 directly mediates cytoadherence of Plasmodium falciparum parasitized
RT erythrocytes.";
RL Cell 58:95-101(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Sugimoto Y., Tsuruo T.;
RL Submitted (AUG-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7693552; DOI=10.1016/0378-1119(93)90639-k;
RA Taylor K.T., Tang Y., Sobieski D.A., Lipsky R.H.;
RT "Characterization of two alternatively spliced 5'-untranslated exons of the
RT human CD36 gene in different cell types.";
RL Gene 133:205-212(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Platelet;
RX PubMed=7505064;
RA Wyler B., Daviet L., Bortkiewicz H., Bordet J.C., McGregor J.L.;
RT "Cloning of the cDNA encoding human platelet CD36: comparison to PCR
RT amplified fragments of monocyte, endothelial and HEL cells.";
RL Thromb. Haemost. 70:500-505(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7518447; DOI=10.1016/s0021-9258(17)32263-9;
RA Armesilla A.L., Vega M.A.;
RT "Structural organization of the gene for human CD36 glycoprotein.";
RL J. Biol. Chem. 269:18985-18991(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG SeattleSNPs variation discovery resource;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), AND VARIANTS TRP-386
RP AND ILE-470.
RA Wu G.-G., Curtis B.R., He B.-R., Zhou Z.-L., Zhou Y., Yang Y.-L., Li H.-Y.,
RA Shen W.-D., Liu J.-L., Zhao T.-M.;
RT "Frequency of CD36 deficiency and identification of novel CD36 gene
RT mutations in the Chinese population.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
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 [10]
RP PROTEIN SEQUENCE OF 2-37, AND GLYCOSYLATION.
RC TISSUE=Platelet;
RX PubMed=2468669; DOI=10.1016/s0021-9258(18)83272-0;
RA Tandon N.N., Lipsky R.H., Burgess W.H., Jamieson G.A.;
RT "Isolation and characterization of platelet glycoprotein IV (CD36).";
RL J. Biol. Chem. 264:7570-7575(1989).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-203; 274-375 AND 419-472, AND
RP VARIANTS LYS-123; ALA-174; ASN-232 INS AND THR-271.
RX PubMed=11668637; DOI=10.1002/humu.1215;
RA Gelhaus A., Scheding A., Browne E., Burchard G.D., Horstmann R.D.;
RT "Variability of the CD36 gene in West Africa.";
RL Hum. Mutat. 18:444-450(2001).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 144-203 (ISOFORM 1/2).
RX PubMed=7503937; DOI=10.1006/geno.1993.1401;
RA Fernandez-Ruiz E., Armesilla A.L., Sanchez-Madrid F., Vega M.A.;
RT "Gene encoding the collagen type I and thrombospondin receptor CD36 is
RT located on chromosome 7q11.2.";
RL Genomics 17:759-761(1993).
RN [13]
RP PROTEIN SEQUENCE OF 261-273 AND 369-385.
RC TISSUE=Adipocyte;
RX PubMed=15242332; DOI=10.1042/bj20040647;
RA Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.;
RT "Vectorial proteomics reveal targeting, phosphorylation and specific
RT fragmentation of polymerase I and transcript release factor (PTRF) at the
RT surface of caveolae in human adipocytes.";
RL Biochem. J. 383:237-248(2004).
RN [14]
RP INTERACTION WITH THBS1 AND THBS2.
RX PubMed=1371676; DOI=10.1016/0006-291x(92)91860-s;
RA Asch A.S., Silbiger S., Heimer E., Nachman R.L.;
RT "Thrombospondin sequence motif (CSVTCG) is responsible for CD36 binding.";
RL Biochem. Biophys. Res. Commun. 182:1208-1217(1992).
RN [15]
RP PALMITOYLATION AT CYS-3; CYS-7; CYS-464 AND CYS-466.
RX PubMed=8798390; DOI=10.1074/jbc.271.37.22315;
RA Tao N., Wagner S.J., Lublin D.M.;
RT "CD36 is palmitoylated on both N- and C-terminal cytoplasmic tails.";
RL J. Biol. Chem. 271:22315-22320(1996).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TLR2 AND TLR6.
RX PubMed=16880211; DOI=10.1074/jbc.m602794200;
RA Triantafilou M., Gamper F.G., Haston R.M., Mouratis M.A., Morath S.,
RA Hartung T., Triantafilou K.;
RT "Membrane sorting of toll-like receptor (TLR)-2/6 and TLR2/1 heterodimers
RT at the cell surface determines heterotypic associations with CD36 and
RT intracellular targeting.";
RL J. Biol. Chem. 281:31002-31011(2006).
RN [17]
RP FUNCTION, UBIQUITINATION AT LYS-469 AND LYS-472, AND MUTAGENESIS OF
RP 469-LYS--LYS-472.
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 [18]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-417.
RC TISSUE=Platelet;
RX PubMed=16263699; DOI=10.1074/mcp.m500324-mcp200;
RA Lewandrowski U., Moebius J., Walter U., Sickmann A.;
RT "Elucidation of N-glycosylation sites on human platelet proteins: a
RT glycoproteomic approach.";
RL Mol. Cell. Proteomics 5:226-233(2006).
RN [19]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-321.
RC TISSUE=Milk;
RX PubMed=18780401; DOI=10.1002/pmic.200701057;
RA Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
RT "Identification of N-linked glycoproteins in human milk by hydrophilic
RT interaction liquid chromatography and mass spectrometry.";
RL Proteomics 8:3833-3847(2008).
RN [20]
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 [21]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-205 AND ASN-417.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [22]
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 [23]
RP FUNCTION, INTERACTION WITH LYN; PTK2; PXN; TLR4 AND TLR6, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF 462-SER--LYS-473; TYR-463 AND CYS-464.
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 [24]
RP FUNCTION, UBIQUITINATION AT LYS-469 AND LYS-472, AND MUTAGENESIS OF
RP 469-LYS--LYS-472.
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 [25]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=21395585; DOI=10.1111/j.1471-4159.2011.07245.x;
RA Mitchell R.W., On N.H., Del Bigio M.R., Miller D.W., Hatch G.M.;
RT "Fatty acid transport protein expression in human brain and potential role
RT in fatty acid transport across human brain microvessel endothelial cells.";
RL J. Neurochem. 117:735-746(2011).
RN [26]
RP FUNCTION.
RX PubMed=22240721; DOI=10.1038/oby.2011.374;
RA Keller K.L., Liang L.C., Sakimura J., May D., van Belle C., Breen C.,
RA Driggin E., Tepper B.J., Lanzano P.C., Deng L., Chung W.K.;
RT "Common variants in the CD36 gene are associated with oral fat perception,
RT fat preferences, and obesity in African Americans.";
RL Obesity 20:1066-1073(2012).
RN [27]
RP FUNCTION.
RX PubMed=25822988; DOI=10.1017/s0007114515000343;
RA Mrizak I., Sery O., Plesnik J., Arfa A., Fekih M., Bouslema A., Zaouali M.,
RA Tabka Z., Khan N.A.;
RT "The A allele of cluster of differentiation 36 (CD36) SNP 1761667
RT associates with decreased lipid taste perception in obese Tunisian women.";
RL Br. J. Nutr. 113:1330-1337(2015).
RN [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [29]
RP FUNCTION, SUBCELLULAR LOCATION, AND PALMITOYLATION.
RX PubMed=32958780; DOI=10.1038/s41467-020-18565-8;
RA Hao J.W., Wang J., Guo H., Zhao Y.Y., Sun H.H., Li Y.F., Lai X.Y., Zhao N.,
RA Wang X., Xie C., Hong L., Huang X., Wang H.R., Li C.B., Liang B., Chen S.,
RA Zhao T.J.;
RT "CD36 facilitates fatty acid uptake by dynamic palmitoylation-regulated
RT endocytosis.";
RL Nat. Commun. 11:4765-4765(2020).
RN [30]
RP VARIANT PG4D SER-90.
RX PubMed=7533783; DOI=10.1172/jci117749;
RA Kashiwagi H., Tomiyama Y., Honda S., Kosugi S., Shiraga M., Nagao N.,
RA Sekiguchi S., Kanayama Y., Kurata Y., Matsuzawa Y.;
RT "Molecular basis of CD36 deficiency. Evidence that a 478C-->T substitution
RT (proline90-->serine) in CD36 cDNA accounts for CD36 deficiency.";
RL J. Clin. Invest. 95:1040-1046(1995).
RN [31]
RP VARIANT PHE-154.
RX PubMed=10391209; DOI=10.1038/10290;
RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA Lander E.S.;
RT "Characterization of single-nucleotide polymorphisms in coding regions of
RT human genes.";
RL Nat. Genet. 22:231-238(1999).
RN [32]
RP ERRATUM OF PUBMED:10391209.
RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA Lander E.S.;
RL Nat. Genet. 23:373-373(1999).
RN [33]
RP ROLE IN MALARIA INFECTION.
RX PubMed=10890433; DOI=10.1038/35016636;
RA Aitman T.J., Cooper L.D., Norsworthy P.J., Wahid F.N., Gray J.K.,
RA Curtis B.R., McKeigue P.M., Kwiatkowski D., Greenwood B.M., Snow R.W.,
RA Hill A.V., Scott J.;
RT "Malaria susceptibility and CD36 mutation.";
RL Nature 405:1015-1016(2000).
RN [34]
RP VARIANTS PG4D SER-90; LEU-254 AND LEU-413.
RX PubMed=11950861; DOI=10.1136/jmg.39.4.286;
RA Hanawa H., Watanabe K., Nakamura T., Ogawa Y., Toba K., Fuse I., Kodama M.,
RA Kato K., Fuse K., Aizawa Y.;
RT "Identification of cryptic splice site, exon skipping, and novel point
RT mutations in type I CD36 deficiency.";
RL J. Med. Genet. 39:286-291(2002).
RN [35]
RP VARIANT LEU-127, AND ROLE IN MALARIA INFECTION.
RX PubMed=12506336; DOI=10.1086/346091;
RA Omi K., Ohashi J., Patarapotikul J., Hananantachai H., Naka I.,
RA Looareesuwan S., Tokunaga K.;
RT "CD36 polymorphism is associated with protection from cerebral malaria.";
RL Am. J. Hum. Genet. 72:364-374(2003).
RN [36]
RP INVOLVEMENT IN CHDS7.
RX PubMed=15282206; DOI=10.1093/hmg/ddh233;
RA Ma X., Bacci S., Mlynarski W., Gottardo L., Soccio T., Menzaghi C.,
RA Iori E., Lager R.A., Shroff A.R., Gervino E.V., Nesto R.W., Johnstone M.T.,
RA Abumrad N.A., Avogaro A., Trischitta V., Doria A.;
RT "A common haplotype at the CD36 locus is associated with high free fatty
RT acid levels and increased cardiovascular risk in Caucasians.";
RL Hum. Mol. Genet. 13:2197-2205(2004).
RN [37]
RP ERRATUM OF PUBMED:15282206.
RA Ma X., Bacci S., Mlynarski W., Gottardo L., Soccio T., Menzaghi C.,
RA Iori E., Lager R.A., Shroff A.R., Gervino E.V., Nesto R.W., Johnstone M.T.,
RA Abumrad N.A., Avogaro A., Trischitta V., Doria A.;
RL Hum. Mol. Genet. 14:3973-3973(2005).
RN [38]
RP INVOLVEMENT IN PG4D, AND FUNCTION.
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 [39] {ECO:0007744|PDB:5LGD}
RP X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS), AND INTERACTION WITH PLASMODIUM
RP FALCIPARUM EMP1.
RX PubMed=27667267; DOI=10.1038/ncomms12837;
RA Hsieh F.L., Turner L., Bolla J.R., Robinson C.V., Lavstsen T.,
RA Higgins M.K.;
RT "The structural basis for CD36 binding by the malaria parasite.";
RL Nat. Commun. 7:12837-12837(2016).
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 (Probable). Binds long-chain
CC fatty acids and facilitates their transport into cells, thus
CC participating in muscle lipid utilization, adipose energy storage, and
CC gut fat absorption (By similarity) (PubMed:18353783, PubMed:21610069).
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 (PubMed:32958780). 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:18753675).
CC Involved in oral fat perception and preferences (PubMed:22240721,
CC PubMed:25822988). Detection into the tongue of long-chain fatty acids
CC leads to a rapid and sustained rise in flux and protein content of
CC pancreatobiliary secretions (By similarity). In taste receptor cells,
CC mediates the induction of an increase in intracellular calcium levels
CC by long-chain fatty acids, leading to the activation of the gustatory
CC neurons in the nucleus of the solitary tract (By similarity). Important
CC factor in both ventromedial hypothalamus neuronal sensing of long-chain
CC fatty acid and the regulation of energy and glucose homeostasis (By
CC similarity). Receptor for thrombospondins, THBS1 and THBS2, mediating
CC their antiangiogenic effects (By similarity). As a coreceptor for
CC TLR4:TLR6 heterodimer, promotes inflammation in monocytes/macrophages.
CC Upon ligand binding, such as oxLDL or amyloid-beta 42, interacts with
CC the heterodimer TLR4:TLR6, the complex is internalized and triggers
CC inflammatory response, leading to NF-kappa-B-dependent production of
CC CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5
CC cytokine, via TICAM1 signaling pathway, as well as IL1B secretion,
CC through the priming and activation of the NLRP3 inflammasome (By
CC similarity) (PubMed:20037584). Selective and nonredundant sensor of
CC microbial diacylated lipopeptide that signal via TLR2:TLR6 heterodimer,
CC this cluster triggers signaling from the cell surface, leading to the
CC NF-kappa-B-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) (PubMed:16880211). {ECO:0000250|UniProtKB:Q07969,
CC ECO:0000250|UniProtKB:Q08857, ECO:0000269|PubMed:16880211,
CC ECO:0000269|PubMed:18353783, ECO:0000269|PubMed:18753675,
CC ECO:0000269|PubMed:20037584, ECO:0000269|PubMed:21395585,
CC ECO:0000269|PubMed:21610069, ECO:0000269|PubMed:22240721,
CC ECO:0000269|PubMed:25822988, ECO:0000305|PubMed:19471024}.
CC -!- FUNCTION: (Microbial infection) Directly mediates cytoadherence of
CC Plasmodium falciparum parasitized erythrocytes and the internalization
CC of particles independently of TLR signaling.
CC {ECO:0000269|PubMed:10890433, ECO:0000269|PubMed:12506336,
CC ECO:0000269|PubMed:19864601}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoate(out) = butanoate(in); Xref=Rhea:RHEA:45248,
CC ChEBI:CHEBI:17968; Evidence={ECO:0000269|PubMed:21395585};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45249;
CC Evidence={ECO:0000269|PubMed:21395585};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate(out) = (9Z)-octadecenoate(in);
CC Xref=Rhea:RHEA:33655, ChEBI:CHEBI:30823;
CC Evidence={ECO:0000269|PubMed:21395585};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33656;
CC Evidence={ECO:0000269|PubMed:21395585};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate(out) = (9Z,12Z)-
CC octadecadienoate(in); Xref=Rhea:RHEA:45264, ChEBI:CHEBI:30245;
CC Evidence={ECO:0000269|PubMed:21395585};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45265;
CC Evidence={ECO:0000269|PubMed:21395585};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=tetradecanoate(out) = tetradecanoate(in);
CC Xref=Rhea:RHEA:45252, ChEBI:CHEBI:30807;
CC Evidence={ECO:0000269|PubMed:21395585};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45253;
CC Evidence={ECO:0000269|PubMed:21395585};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoate(out) = hexadecanoate(in); Xref=Rhea:RHEA:45256,
CC ChEBI:CHEBI:7896; Evidence={ECO:0000269|PubMed:21395585};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45257;
CC Evidence={ECO:0000269|PubMed:21395585};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=tetracosanoate(out) = tetracosanoate(in);
CC Xref=Rhea:RHEA:45260, ChEBI:CHEBI:31014;
CC Evidence={ECO:0000269|PubMed:21395585};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45261;
CC Evidence={ECO:0000269|PubMed:21395585};
CC -!- SUBUNIT: Interacts with THBS1 and THBS2; the interactions mediate the
CC THBS antiangiogenic activity (PubMed:1371676). Upon interaction with a
CC ligand, such as oxidized low-density lipoprotein (oxLDL) or amyloid-
CC beta 42, rapidly forms a complex with TLR4 and TLR6; the complex is
CC internalized and triggers an inflammatory signal. Through its C-
CC terminus, interacts with PTK2, PXN and LYN, but not with SRC. LYN
CC kinase activity is required for facilitating TLR4:TLR6
CC heterodimerization and signal initiation (PubMed:1371676,
CC PubMed:20037584). Upon interaction with ligands such as diacylated
CC lipopeptides, interacts with the TLR2:TLR6 heterodimer
CC (PubMed:16880211). Interacts with CD9, CD81, FCER1G, ITGB2 and/or
CC ITGB2; forming a membrane heteromeric complex required for the
CC internalization of CD36 and its ligands (By similarity).
CC {ECO:0000250|UniProtKB:Q08857, ECO:0000269|PubMed:1371676,
CC ECO:0000269|PubMed:16880211, ECO:0000269|PubMed:20037584}.
CC -!- SUBUNIT: (Microbial infection) Binds to Plasmodium falciparum EMP1.
CC {ECO:0000269|PubMed:27667267}.
CC -!- INTERACTION:
CC P16671; P05067: APP; NbExp=3; IntAct=EBI-2808214, EBI-77613;
CC P16671; P07948: LYN; NbExp=3; IntAct=EBI-2808214, EBI-79452;
CC P16671; PRO_0000035842 [P07996]: THBS1; NbExp=2; IntAct=EBI-2808214, EBI-13915509;
CC P16671; P13051-2: UNG; NbExp=3; IntAct=EBI-2808214, EBI-25834258;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16880211,
CC ECO:0000269|PubMed:32958780}; Multi-pass membrane protein
CC {ECO:0000255}. Membrane raft {ECO:0000269|PubMed:16880211}. Golgi
CC apparatus {ECO:0000269|PubMed:16880211}. Apical cell membrane
CC {ECO:0000250|UniProtKB:Q08857}. Note=Upon ligand-binding, internalized
CC through dynamin-dependent endocytosis. {ECO:0000269|PubMed:20037584}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P16671-1; Sequence=Displayed;
CC Name=2; Synonyms=ex8-del;
CC IsoId=P16671-2; Sequence=VSP_055978, VSP_055979;
CC Name=3; Synonyms=ex6-7-del;
CC IsoId=P16671-3; Sequence=VSP_055977;
CC Name=4; Synonyms=ex4-del;
CC IsoId=P16671-4; Sequence=VSP_055976;
CC -!- PTM: N-glycosylated and O-glycosylated with a ratio of 2:1.
CC {ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:18780401,
CC ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:2468669}.
CC -!- PTM: Palmitoylated by ZDHHC5. Palmitoylation is required for proper
CC localization at the plasma membrane. {ECO:0000269|PubMed:32958780}.
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 -!- POLYMORPHISM: Genetic variations in CD36 are involved in susceptibility
CC to malaria and influence the severity and outcome of malaria infection
CC [MIM:611162].
CC -!- DISEASE: Platelet glycoprotein IV deficiency (PG4D) [MIM:608404]: A
CC disorder characterized by macrothrombocytopenia without notable
CC hemostatic problems and bleeding tendency. Platelet glycoprotein IV
CC deficiency can be divided into 2 subgroups. The type I phenotype is
CC characterized by platelets and monocytes/macrophages exhibiting
CC complete CD36 deficiency. The type II phenotype lacks the surface
CC expression of CD36 in platelets, but expression in
CC monocytes/macrophages is near normal. {ECO:0000269|PubMed:11950861,
CC ECO:0000269|PubMed:7533783}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. Patients also have
CC postprandial hypertriglyceridemia, insulin resistance and hypertension
CC increasing atherosclerotic risk. {ECO:0000269|PubMed:18753675}.
CC -!- DISEASE: Coronary heart disease 7 (CHDS7) [MIM:610938]: A
CC multifactorial disease characterized by an imbalance between myocardial
CC functional requirements and the capacity of the coronary vessels to
CC supply sufficient blood flow. Decreased capacity of the coronary
CC vessels is often associated with thickening and loss of elasticity of
CC the coronary arteries. {ECO:0000269|PubMed:15282206}. Note=Disease
CC susceptibility is associated with variants affecting the gene
CC represented in this entry.
CC -!- SIMILARITY: Belongs to the CD36 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM14636.2; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=CD36 entry;
CC URL="https://en.wikipedia.org/wiki/CD36";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/cd36/";
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; M24795; AAA35534.1; -; mRNA.
DR EMBL; M98398; AAA58412.1; -; mRNA.
DR EMBL; M98399; AAA58413.1; -; mRNA.
DR EMBL; L06850; AAA16068.1; -; mRNA.
DR EMBL; S67532; AAD13993.1; -; mRNA.
DR EMBL; Z32770; CAA83662.1; -; Genomic_DNA.
DR EMBL; Z32754; CAA83662.1; JOINED; Genomic_DNA.
DR EMBL; Z32755; CAA83662.1; JOINED; Genomic_DNA.
DR EMBL; Z32756; CAA83662.1; JOINED; Genomic_DNA.
DR EMBL; Z32757; CAA83662.1; JOINED; Genomic_DNA.
DR EMBL; Z32758; CAA83662.1; JOINED; Genomic_DNA.
DR EMBL; Z32759; CAA83662.1; JOINED; Genomic_DNA.
DR EMBL; Z32760; CAA83662.1; JOINED; Genomic_DNA.
DR EMBL; Z32761; CAA83662.1; JOINED; Genomic_DNA.
DR EMBL; Z32762; CAA83662.1; JOINED; Genomic_DNA.
DR EMBL; Z32763; CAA83662.1; JOINED; Genomic_DNA.
DR EMBL; Z32764; CAA83662.1; JOINED; Genomic_DNA.
DR EMBL; AY095373; AAM14636.2; ALT_FRAME; Genomic_DNA.
DR EMBL; HM217023; ADI80543.1; -; mRNA.
DR EMBL; HM217024; ADI80544.1; -; mRNA.
DR EMBL; HM217025; ADI80545.1; -; mRNA.
DR EMBL; HM217026; ADI80546.1; -; mRNA.
DR EMBL; AC004862; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073182; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073850; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092108; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008406; AAH08406.1; -; mRNA.
DR EMBL; AF300626; AAG60625.1; -; Genomic_DNA.
DR EMBL; AF300627; AAG60626.1; -; Genomic_DNA.
DR EMBL; AF300628; AAG60627.1; -; Genomic_DNA.
DR EMBL; AF300633; AAG60632.1; -; Genomic_DNA.
DR EMBL; AF300634; AAG60633.1; -; Genomic_DNA.
DR EMBL; AF300635; AAG60634.1; -; Genomic_DNA.
DR EMBL; AF300639; AAG60638.1; -; Genomic_DNA.
DR EMBL; AF300640; AAG60639.1; -; Genomic_DNA.
DR EMBL; S67044; AAB28992.1; -; mRNA.
DR EMBL; Z22924; CAA80504.1; -; Genomic_DNA.
DR CCDS; CCDS34673.1; -. [P16671-1]
DR CCDS; CCDS78249.1; -. [P16671-3]
DR CCDS; CCDS78250.1; -. [P16671-4]
DR PIR; A54870; A54870.
DR RefSeq; NP_000063.2; NM_000072.3. [P16671-1]
DR RefSeq; NP_001001547.1; NM_001001547.2. [P16671-1]
DR RefSeq; NP_001001548.1; NM_001001548.2. [P16671-1]
DR RefSeq; NP_001120915.1; NM_001127443.1. [P16671-1]
DR RefSeq; NP_001120916.1; NM_001127444.1. [P16671-1]
DR RefSeq; NP_001276837.1; NM_001289908.1. [P16671-3]
DR RefSeq; NP_001276838.1; NM_001289909.1. [P16671-4]
DR RefSeq; NP_001276840.1; NM_001289911.1.
DR RefSeq; XP_005250770.1; XM_005250713.1.
DR RefSeq; XP_005250771.1; XM_005250714.1.
DR RefSeq; XP_005250772.1; XM_005250715.4. [P16671-1]
DR PDB; 5LGD; X-ray; 2.07 A; A=1-472.
DR PDBsum; 5LGD; -.
DR AlphaFoldDB; P16671; -.
DR SMR; P16671; -.
DR BioGRID; 107386; 40.
DR IntAct; P16671; 20.
DR STRING; 9606.ENSP00000399421; -.
DR BindingDB; P16671; -.
DR ChEMBL; CHEMBL1744526; -.
DR SwissLipids; SLP:000001098; -.
DR TCDB; 9.B.39.1.4; the long chain fatty acid translocase (lcfat) family.
DR GlyConnect; 1611; 20 N-Linked glycans (3 sites).
DR GlyGen; P16671; 12 sites, 17 N-linked glycans (3 sites), 1 O-linked glycan (2 sites).
DR iPTMnet; P16671; -.
DR PhosphoSitePlus; P16671; -.
DR SwissPalm; P16671; -.
DR BioMuta; CD36; -.
DR DMDM; 115982; -.
DR jPOST; P16671; -.
DR MassIVE; P16671; -.
DR MaxQB; P16671; -.
DR PaxDb; P16671; -.
DR PeptideAtlas; P16671; -.
DR PRIDE; P16671; -.
DR ProteomicsDB; 15177; -.
DR ProteomicsDB; 15178; -.
DR ProteomicsDB; 53392; -. [P16671-1]
DR Antibodypedia; 659; 1753 antibodies from 49 providers.
DR DNASU; 948; -.
DR Ensembl; ENST00000309881.11; ENSP00000308165.7; ENSG00000135218.19. [P16671-1]
DR Ensembl; ENST00000394788.7; ENSP00000378268.3; ENSG00000135218.19. [P16671-1]
DR Ensembl; ENST00000432207.5; ENSP00000411411.1; ENSG00000135218.19. [P16671-1]
DR Ensembl; ENST00000433696.6; ENSP00000401863.2; ENSG00000135218.19. [P16671-3]
DR Ensembl; ENST00000435819.5; ENSP00000399421.1; ENSG00000135218.19. [P16671-1]
DR Ensembl; ENST00000447544.7; ENSP00000415743.2; ENSG00000135218.19. [P16671-1]
DR Ensembl; ENST00000538969.5; ENSP00000439543.1; ENSG00000135218.19. [P16671-4]
DR Ensembl; ENST00000544133.5; ENSP00000441956.1; ENSG00000135218.19. [P16671-2]
DR GeneID; 948; -.
DR KEGG; hsa:948; -.
DR MANE-Select; ENST00000447544.7; ENSP00000415743.2; NM_001001548.3; NP_001001548.1.
DR UCSC; uc003uhc.4; human. [P16671-1]
DR CTD; 948; -.
DR DisGeNET; 948; -.
DR GeneCards; CD36; -.
DR HGNC; HGNC:1663; CD36.
DR HPA; ENSG00000135218; Tissue enhanced (adipose).
DR MalaCards; CD36; -.
DR MIM; 173510; gene.
DR MIM; 248310; phenotype.
DR MIM; 608404; phenotype.
DR MIM; 610938; phenotype.
DR MIM; 611162; phenotype.
DR neXtProt; NX_P16671; -.
DR OpenTargets; ENSG00000135218; -.
DR PharmGKB; PA26212; -.
DR VEuPathDB; HostDB:ENSG00000135218; -.
DR eggNOG; KOG3776; Eukaryota.
DR GeneTree; ENSGT00940000153372; -.
DR HOGENOM; CLU_019853_0_0_1; -.
DR InParanoid; P16671; -.
DR OMA; NCTIAGV; -.
DR OrthoDB; 1106566at2759; -.
DR PhylomeDB; P16671; -.
DR TreeFam; TF317925; -.
DR PathwayCommons; P16671; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-1236973; Cross-presentation of particulate exogenous antigens (phagosomes).
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR Reactome; R-HSA-166058; MyD88:MAL(TIRAP) cascade initiated on plasma membrane.
DR Reactome; R-HSA-168188; Toll Like Receptor TLR6:TLR2 Cascade.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-3000471; Scavenging by Class B Receptors.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR Reactome; R-HSA-434313; Intracellular metabolism of fatty acids regulates insulin secretion.
DR Reactome; R-HSA-5602498; MyD88 deficiency (TLR2/4).
DR Reactome; R-HSA-5603041; IRAK4 deficiency (TLR2/4).
DR Reactome; R-HSA-5686938; Regulation of TLR by endogenous ligand.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P16671; -.
DR SIGNOR; P16671; -.
DR BioGRID-ORCS; 948; 9 hits in 1068 CRISPR screens.
DR ChiTaRS; CD36; human.
DR GeneWiki; CD36; -.
DR GenomeRNAi; 948; -.
DR Pharos; P16671; Tbio.
DR PRO; PR:P16671; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P16671; protein.
DR Bgee; ENSG00000135218; Expressed in adipose tissue of abdominal region and 170 other tissues.
DR ExpressionAtlas; P16671; baseline and differential.
DR Genevisible; P16671; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031526; C:brush border membrane; ISS:UniProtKB.
DR GO; GO:0005901; C:caveola; IBA:GO_Central.
DR GO; GO:0071944; C:cell periphery; IDA:ARUK-UCL.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:BHF-UCL.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0031092; C:platelet alpha granule membrane; TAS:Reactome.
DR GO; GO:0043235; C:receptor complex; IPI:ARUK-UCL.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0001540; F:amyloid-beta binding; IDA:ARUK-UCL.
DR GO; GO:0008035; F:high-density lipoprotein particle binding; IEA:Ensembl.
DR GO; GO:0008289; F:lipid binding; IDA:BHF-UCL.
DR GO; GO:0071813; F:lipoprotein particle binding; IDA:UniProtKB.
DR GO; GO:0070892; F:lipoteichoic acid immune receptor activity; IEA:Ensembl.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; IMP:ARUK-UCL.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; IDA: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; IDA:ARUK-UCL.
DR GO; GO:0150025; F:oxidised low-density lipoprotein particle receptor activity; IMP:ARUK-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:ARUK-UCL.
DR GO; GO:0005044; F:scavenger receptor activity; IMP:ARUK-UCL.
DR GO; GO:0015636; F:short-chain fatty acid transmembrane transporter activity; IMP:ARUK-UCL.
DR GO; GO:0070053; F:thrombospondin receptor activity; ISS:BHF-UCL.
DR GO; GO:0035325; F:Toll-like receptor binding; IPI:ARUK-UCL.
DR GO; GO:0050431; F:transforming growth factor beta binding; ISS: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; IEA:Ensembl.
DR GO; GO:0007596; P:blood coagulation; TAS:ProtInc.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:Ensembl.
DR GO; GO:1904646; P:cellular response to amyloid-beta; IGI:ARUK-UCL.
DR GO; GO:0071726; P:cellular response to diacyl bacterial lipopeptide; IDA:UniProtKB.
DR GO; GO:0071447; P:cellular response to hydroperoxide; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0071223; P:cellular response to lipoteichoic acid; IEA:Ensembl.
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; IMP:ARUK-UCL.
DR GO; GO:0019934; P:cGMP-mediated signaling; IDA:BHF-UCL.
DR GO; GO:0070508; P:cholesterol import; ISS:UniProtKB.
DR GO; GO:0030301; P:cholesterol transport; ISS:BHF-UCL.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
DR GO; GO:0097009; P:energy homeostasis; ISS:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; TAS:ARUK-UCL.
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:0006629; P:lipid metabolic process; NAS:ProtInc.
DR GO; GO:0019915; P:lipid storage; IMP:BHF-UCL.
DR GO; GO:1990379; P:lipid transport across blood-brain barrier; IMP:ARUK-UCL.
DR GO; GO:0042953; P:lipoprotein transport; IMP:BHF-UCL.
DR GO; GO:0015911; P:long-chain fatty acid import across plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0044539; P:long-chain fatty acid import into cell; IDA:UniProtKB.
DR GO; GO:0015909; P:long-chain fatty acid transport; IMP:ARUK-UCL.
DR GO; GO:0034383; P:low-density lipoprotein particle clearance; IMP:BHF-UCL.
DR GO; GO:0055096; P:low-density lipoprotein particle mediated signaling; IEA:Ensembl.
DR GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0007263; P:nitric oxide mediated signal transduction; IDA:BHF-UCL.
DR GO; GO:0150024; P:oxidised low-density lipoprotein particle clearance; IMP:ARUK-UCL.
DR GO; GO:0006911; P:phagocytosis, engulfment; TAS:ARUK-UCL.
DR GO; GO:0006910; P:phagocytosis, recognition; IEA:Ensembl.
DR GO; GO:0034381; P:plasma lipoprotein particle clearance; ISS:BHF-UCL.
DR GO; GO:0030194; P:positive regulation of blood coagulation; IEA:Ensembl.
DR GO; GO:2000334; P:positive regulation of blood microparticle formation; IEA:Ensembl.
DR GO; GO:0010942; P:positive regulation of cell death; IMP:ARUK-UCL.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IDA:BHF-UCL.
DR GO; GO:0010886; P:positive regulation of cholesterol storage; IEA:Ensembl.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
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; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:ARUK-UCL.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
DR GO; GO:0060907; P:positive regulation of macrophage cytokine production; IEA:Ensembl.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IMP:BHF-UCL.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IGI:ARUK-UCL.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISS:ARUK-UCL.
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; IEA:Ensembl.
DR GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; IEA:Ensembl.
DR GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; ISS:ARUK-UCL.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
DR GO; GO:0002532; P:production of molecular mediator involved in inflammatory response; TAS:ARUK-UCL.
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; ISS:ARUK-UCL.
DR GO; GO:0031664; P:regulation of lipopolysaccharide-mediated signaling pathway; TAS:ARUK-UCL.
DR GO; GO:0043254; P:regulation of protein-containing complex assembly; IMP:ARUK-UCL.
DR GO; GO:2000121; P:regulation of removal of superoxide radicals; IEA:Ensembl.
DR GO; GO:0034121; P:regulation of toll-like receptor signaling pathway; IGI:ARUK-UCL.
DR GO; GO:0070542; P:response to fatty acid; ISS:UniProtKB.
DR GO; GO:0070543; P:response to linoleic acid; ISS:UniProtKB.
DR GO; GO:0033993; P:response to lipid; ISS:UniProtKB.
DR GO; GO:0035634; P:response to stilbenoid; IEA:Ensembl.
DR GO; GO:0050909; P:sensory perception of taste; ISS:UniProtKB.
DR GO; GO:0015912; P:short-chain fatty acid transport; IMP:ARUK-UCL.
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 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Direct protein sequencing; Disease variant; 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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2468669"
FT CHAIN 2..472
FT /note="Platelet glycoprotein 4"
FT /id="PRO_0000144151"
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:0000269|PubMed:1371676"
FT REGION 460..472
FT /note="Interaction with PTK2, PXN and LYN"
FT /evidence="ECO:0000269|PubMed:20037584"
FT SITE 463
FT /note="Critical for TLR4-TLR6 dimerization and signaling"
FT /evidence="ECO:0000269|PubMed:20037584"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:8798390"
FT LIPID 7
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:8798390"
FT LIPID 464
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:8798390"
FT LIPID 466
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:8798390"
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 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
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:0000269|PubMed:18780401"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16263699,
FT ECO:0000269|PubMed:19159218"
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:0000305|PubMed:18353783,
FT ECO:0000305|PubMed:21610069"
FT CROSSLNK 472
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000305|PubMed:18353783,
FT ECO:0000305|PubMed:21610069"
FT VAR_SEQ 144..203
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_055976"
FT VAR_SEQ 234..272
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_055977"
FT VAR_SEQ 274..288
FT /note="SIYAVFESDVNLKGI -> ETCVHFTSSFSVCKS (in isoform 2)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_055978"
FT VAR_SEQ 289..472
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_055979"
FT VARIANT 90
FT /note="P -> S (in PG4D; type I; degradation in the
FT cytoplasm due to defects in maturation; dbSNP:rs75326924)"
FT /evidence="ECO:0000269|PubMed:11950861,
FT ECO:0000269|PubMed:7533783"
FT /id="VAR_017913"
FT VARIANT 123
FT /note="E -> K (in individuals from a malaria endemic area
FT in West Africa; dbSNP:rs183461468)"
FT /evidence="ECO:0000269|PubMed:11668637"
FT /id="VAR_017914"
FT VARIANT 127
FT /note="S -> L (in dbSNP:rs201765331)"
FT /evidence="ECO:0000269|PubMed:12506336"
FT /id="VAR_019049"
FT VARIANT 154
FT /note="V -> F (in dbSNP:rs5957)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_013918"
FT VARIANT 174
FT /note="T -> A (in individuals from a malaria endemic area
FT in West Africa; dbSNP:rs756525492)"
FT /evidence="ECO:0000269|PubMed:11668637"
FT /id="VAR_017915"
FT VARIANT 232
FT /note="G -> GN (in individuals from a malaria endemic area
FT in West Africa)"
FT /evidence="ECO:0000269|PubMed:11668637"
FT /id="VAR_017916"
FT VARIANT 254
FT /note="F -> L (in PG4D; type I; dbSNP:rs142186404)"
FT /evidence="ECO:0000269|PubMed:11950861"
FT /id="VAR_017917"
FT VARIANT 271
FT /note="I -> T (in individuals from a malaria endemic area
FT in West Africa; dbSNP:rs370072057)"
FT /evidence="ECO:0000269|PubMed:11668637"
FT /id="VAR_017918"
FT VARIANT 386
FT /note="R -> W (in dbSNP:rs148910227)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_071161"
FT VARIANT 413
FT /note="I -> L (in PG4D; type I; dbSNP:rs121918035)"
FT /evidence="ECO:0000269|PubMed:11950861"
FT /id="VAR_017919"
FT VARIANT 470
FT /note="T -> I (in dbSNP:rs200771788)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_071162"
FT MUTAGEN 462..472
FT /note="SYCACRSKTIK->AAAAAAAAAAA: No effect on cell surface
FT location. Loss of oxLDL-induced NF-kappa-B activation."
FT /evidence="ECO:0000269|PubMed:20037584"
FT MUTAGEN 463
FT /note="Y->A: No effect on cell surface location. Loss of
FT oxLDL-induced NF-kappa-B activation. Loss of complex
FT formation with TLR4 and TLR6."
FT /evidence="ECO:0000269|PubMed:20037584"
FT MUTAGEN 464
FT /note="C->S: No effect on cell surface location, nor on
FT oxLDL-induced NF-kappa-B activation."
FT /evidence="ECO:0000269|PubMed:20037584"
FT MUTAGEN 469..472
FT /note="KTIK->ATIA: Abolishes ubiquitination induced by
FT lipids. Enhances fatty acid uptake."
FT /evidence="ECO:0000269|PubMed:18353783,
FT ECO:0000269|PubMed:21610069"
FT CONFLICT 44
FT /note="L -> R (in Ref. 4; AAD13993)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="Y -> D (in Ref. 4; AAD13993)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="E -> Q (in Ref. 3; AAA16068 and 13; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:5LGD"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:5LGD"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:5LGD"
FT STRAND 61..71
FT /evidence="ECO:0007829|PDB:5LGD"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:5LGD"
FT STRAND 83..96
FT /evidence="ECO:0007829|PDB:5LGD"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:5LGD"
FT TURN 107..110
FT /evidence="ECO:0007829|PDB:5LGD"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:5LGD"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:5LGD"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:5LGD"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:5LGD"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:5LGD"
FT HELIX 140..148
FT /evidence="ECO:0007829|PDB:5LGD"
FT HELIX 152..164
FT /evidence="ECO:0007829|PDB:5LGD"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:5LGD"
FT HELIX 175..180
FT /evidence="ECO:0007829|PDB:5LGD"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:5LGD"
FT STRAND 208..215
FT /evidence="ECO:0007829|PDB:5LGD"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:5LGD"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:5LGD"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:5LGD"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:5LGD"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:5LGD"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:5LGD"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:5LGD"
FT TURN 269..272
FT /evidence="ECO:0007829|PDB:5LGD"
FT STRAND 273..285
FT /evidence="ECO:0007829|PDB:5LGD"
FT STRAND 288..294
FT /evidence="ECO:0007829|PDB:5LGD"
FT HELIX 297..300
FT /evidence="ECO:0007829|PDB:5LGD"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:5LGD"
FT HELIX 307..312
FT /evidence="ECO:0007829|PDB:5LGD"
FT TURN 317..323
FT /evidence="ECO:0007829|PDB:5LGD"
FT STRAND 326..329
FT /evidence="ECO:0007829|PDB:5LGD"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:5LGD"
FT TURN 334..336
FT /evidence="ECO:0007829|PDB:5LGD"
FT STRAND 339..342
FT /evidence="ECO:0007829|PDB:5LGD"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:5LGD"
FT HELIX 351..354
FT /evidence="ECO:0007829|PDB:5LGD"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:5LGD"
FT HELIX 364..367
FT /evidence="ECO:0007829|PDB:5LGD"
FT STRAND 370..373
FT /evidence="ECO:0007829|PDB:5LGD"
FT TURN 375..377
FT /evidence="ECO:0007829|PDB:5LGD"
FT STRAND 379..393
FT /evidence="ECO:0007829|PDB:5LGD"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:5LGD"
FT STRAND 409..421
FT /evidence="ECO:0007829|PDB:5LGD"
FT HELIX 424..433
FT /evidence="ECO:0007829|PDB:5LGD"
SQ SEQUENCE 472 AA; 53053 MW; 543E748259A094FA CRC64;
MGCDRNCGLI AGAVIGAVLA VFGGILMPVG DLLIQKTIKK QVVLEEGTIA FKNWVKTGTE
VYRQFWIFDV QNPQEVMMNS SNIQVKQRGP YTYRVRFLAK ENVTQDAEDN TVSFLQPNGA
IFEPSLSVGT EADNFTVLNL AVAAASHIYQ NQFVQMILNS LINKSKSSMF QVRTLRELLW
GYRDPFLSLV PYPVTTTVGL FYPYNNTADG VYKVFNGKDN ISKVAIIDTY KGKRNLSYWE
SHCDMINGTD AASFPPFVEK SQVLQFFSSD ICRSIYAVFE SDVNLKGIPV YRFVLPSKAF
ASPVENPDNY CFCTEKIISK NCTSYGVLDI SKCKEGRPVY ISLPHFLYAS PDVSEPIDGL
NPNEEEHRTY LDIEPITGFT LQFAKRLQVN LLVKPSEKIQ VLKNLKRNYI VPILWLNETG
TIGDEKANMF RSQVTGKINL LGLIEMILLS VGVVMFVAFM ISYCACRSKT IK
