ID CD36_HUMAN Reviewed; 472 AA. AC P16671; D9IX66; D9IX67; D9IX68; D9IX69; Q13966; Q16093; Q8TCV7; AC Q9BPZ8; Q9BQC2; Q9BZM8; Q9BZN3; Q9BZN4; Q9BZN5; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 11-NOV-2015, entry version 174. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 RT parasitized 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 RT of the 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; 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 RP TRP-386 AND ILE-470. RA Wu G.-G., Curtis B.R., He B.-R., Zhou Z.-L., Zhou Y., Yang Y.-L., RA Li H.-Y., 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., RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., RA 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., RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., RA Waterston R.H., 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 RT project: 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; 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 RT the 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 RT 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 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 [17] 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 [18] 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 RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [19] 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., RA Halle A., Rayner K.J., Boyer L., Zhong R., Frazier W.A., RA Lacy-Hulbert A., El Khoury J., Golenbock D.T., Moore K.J.; RT "CD36 ligands promote sterile inflammation through assembly of a Toll- RT like receptor 4 and 6 heterodimer."; RL Nat. Immunol. 11:155-161(2010). RN [20] 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., RA Ayoub D., 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 [21] 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 RT substitution (proline90-->serine) in CD36 cDNA accounts for CD36 RT deficiency."; RL J. Clin. Invest. 95:1040-1046(1995). RN [22] 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 RT of human genes."; RL Nat. Genet. 22:231-238(1999). RN [23] RP ERRATUM. 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 [24] 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 [25] 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., RA Kodama M., 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 [26] 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 RT malaria."; RL Am. J. Hum. Genet. 72:364-374(2003). RN [27] 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., RA Johnstone M.T., Abumrad N.A., Avogaro A., Trischitta V., Doria A.; RT "A common haplotype at the CD36 locus is associated with high free RT fatty acid levels and increased cardiovascular risk in Caucasians."; RL Hum. Mol. Genet. 13:2197-2205(2004). RN [28] RP ERRATUM. 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., RA Johnstone M.T., Abumrad N.A., Avogaro A., Trischitta V., Doria A.; RL Hum. Mol. Genet. 14:3973-3973(2005). CC -!- FUNCTION: Binds to collagen, thrombospondin, anionic phospholipids CC and oxidized low-density lipoprotein (oxLDL). May function as a CC cell adhesion molecule. Directly mediates cytoadherence of CC Plasmodium falciparum parasitized erythrocytes. Binds long chain CC fatty acids and may function in the transport and/or as a CC regulator of fatty acid transport. Receptor for thombospondins, CC THBS1 AND THBS2, mediating their antiangiogenic effects. As a CC coreceptor for TLR4-TLR6 heterodimer, promotes inflammation in CC monocytes/macrophages. Upon ligand binding, such as oxLDL or CC amyloid-beta 42, rapidly induces the formation of a heterodimer of CC TLR4 and TLR6, which is internalized and triggers inflammatory CC response, leading to NF-kappa-B-dependent production of CXCL1, CC CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 CC cytokine, via TICAM1 signaling pathway, as well as IL1B secretion. CC {ECO:0000269|PubMed:10890433, ECO:0000269|PubMed:12506336, CC ECO:0000269|PubMed:20037584}. CC -!- SUBUNIT: Interacts with THBS1 and THBS2; the interactions mediate CC the THBS antiangiogenic activity. Upon interaction with a ligand, CC such as oxidized low-density lipoprotein (oxLDL) or amyloid-beta CC 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. CC {ECO:0000269|PubMed:1371676, ECO:0000269|PubMed:20037584}. CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC Note=Upon ligand-binding, internalized through dynamin-dependent CC 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 -!- POLYMORPHISM: Genetic variations in CD36 are involved in CC susceptibility to malaria and influence the severity and outcome CC of malaria infection [MIM:611162]. CC -!- DISEASE: Platelet glycoprotein IV deficiency (PG4D) [MIM:608404]: CC A disorder characterized by macrothrombocytopenia without notable CC hemostatic problems and bleeding tendency. Platelet glycoprotein CC IV deficiency can be divided into 2 subgroups. The type I CC phenotype is characterized by platelets and monocytes/macrophages CC exhibiting complete CD36 deficiency. The type II phenotype lacks CC the surface expression of CD36 in platelets, but expression in CC monocytes/macrophages is near normal. CC {ECO:0000269|PubMed:11950861, ECO:0000269|PubMed:7533783}. CC Note=The disease is caused by mutations affecting the gene CC represented in this entry. CC -!- DISEASE: Coronary heart disease 7 (CHDS7) [MIM:610938]: A CC multifactorial disease characterized by an imbalance between CC myocardial functional requirements and the capacity of the CC coronary vessels to supply sufficient blood flow. Decreased CC capacity of the coronary vessels is often associated with CC thickening and loss of elasticity of the coronary arteries. CC {ECO:0000269|PubMed:15282206}. Note=Disease susceptibility is CC associated with variations affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the CD36 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAM14636.2; Type=Frameshift; Positions=53; 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. [P16671-1] DR RefSeq; XP_005250771.1; XM_005250714.1. [P16671-1] DR RefSeq; XP_005250772.1; XM_005250715.3. [P16671-1] DR RefSeq; XP_011515009.1; XM_011516707.1. [P16671-1] DR UniGene; Hs.120949; -. DR ProteinModelPortal; P16671; -. DR SMR; P16671; 38-434. DR BioGrid; 107386; 18. DR IntAct; P16671; 7. DR STRING; 9606.ENSP00000308165; -. DR ChEMBL; CHEMBL1744526; -. DR TCDB; 9.B.39.1.4; the long chain fatty acid translocase (lcfat) family. DR PhosphoSite; P16671; -. DR BioMuta; CD36; -. DR DMDM; 115982; -. DR MaxQB; P16671; -. DR PaxDb; P16671; -. DR PRIDE; P16671; -. DR DNASU; 948; -. DR Ensembl; ENST00000309881; ENSP00000308165; ENSG00000135218. [P16671-1] DR Ensembl; ENST00000394788; ENSP00000378268; ENSG00000135218. [P16671-1] DR Ensembl; ENST00000432207; ENSP00000411411; ENSG00000135218. [P16671-1] DR Ensembl; ENST00000433696; ENSP00000401863; ENSG00000135218. [P16671-3] DR Ensembl; ENST00000435819; ENSP00000399421; ENSG00000135218. [P16671-1] DR Ensembl; ENST00000447544; ENSP00000415743; ENSG00000135218. [P16671-1] DR Ensembl; ENST00000538969; ENSP00000439543; ENSG00000135218. [P16671-4] DR Ensembl; ENST00000544133; ENSP00000441956; ENSG00000135218. [P16671-2] DR GeneID; 948; -. DR KEGG; hsa:948; -. DR UCSC; uc003uhc.3; human. [P16671-1] DR CTD; 948; -. DR GeneCards; CD36; -. DR HGNC; HGNC:1663; CD36. DR HPA; CAB025866; -. DR HPA; HPA002018; -. 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 PharmGKB; PA26212; -. DR eggNOG; KOG3776; Eukaryota. DR eggNOG; ENOG410XS17; LUCA. DR GeneTree; ENSGT00530000062927; -. DR HOVERGEN; HBG002754; -. DR InParanoid; P16671; -. DR KO; K06259; -. DR OMA; NTVSFLQ; -. DR OrthoDB; EOG79SDWX; -. DR PhylomeDB; P16671; -. DR TreeFam; TF317925; -. DR Reactome; R-HSA-114608; Platelet degranulation. DR Reactome; R-HSA-1236973; Cross-presentation of particulate exogenous antigens (phagosomes). DR Reactome; R-HSA-166058; MyD88:Mal 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-5602498; MyD88 deficiency (TLR2/4). DR Reactome; R-HSA-5603041; IRAK4 deficiency (TLR2/4). DR ChiTaRS; CD36; human. DR GeneWiki; CD36; -. DR GenomeRNAi; 948; -. DR NextBio; 35495887; -. DR PRO; PR:P16671; -. DR Proteomes; UP000005640; Chromosome 7. DR Bgee; P16671; -. DR ExpressionAtlas; P16671; baseline and differential. DR Genevisible; P16671; HS. DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL. 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; IDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl. 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; IEA:Ensembl. 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: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 receptor activity; IEA:Ensembl. DR GO; GO:0030169; F:low-density lipoprotein particle binding; IDA:BHF-UCL. DR GO; GO:0005041; F:low-density lipoprotein receptor activity; IMP:BHF-UCL. DR GO; GO:0070053; F:thrombospondin receptor activity; ISS:BHF-UCL. DR GO; GO:0050431; F:transforming growth factor beta binding; ISS:BHF-UCL. DR GO; GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome. DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0043277; P:apoptotic cell clearance; IEA:Ensembl. DR GO; GO:0007596; P:blood coagulation; TAS:Reactome. DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc. DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:Ensembl. DR GO; GO:0044255; P:cellular lipid metabolic process; TAS:Reactome. DR GO; GO:0071221; P:cellular response to bacterial lipopeptide; IEA:Ensembl. 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:0019934; P:cGMP-mediated signaling; IDA:BHF-UCL. 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:0045087; P:innate immune response; TAS:Reactome. DR GO; GO:0006629; P:lipid metabolic process; NAS:ProtInc. DR GO; GO:0019915; P:lipid storage; IMP:BHF-UCL. DR GO; GO:0042953; P:lipoprotein transport; IMP:BHF-UCL. DR GO; GO:0044539; P:long-chain fatty acid import; IDA:UniProtKB. 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:0002755; P:MyD88-dependent toll-like receptor signaling pathway; TAS:Reactome. DR GO; GO:0044130; P:negative regulation of growth of symbiont in host; IEA:Ensembl. DR GO; GO:0042992; P:negative regulation of transcription factor import into nucleus; IEA:Ensembl. DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl. DR GO; GO:0007263; P:nitric oxide mediated signal transduction; IDA:BHF-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:0030168; P:platelet activation; TAS:Reactome. DR GO; GO:0002576; P:platelet degranulation; TAS:Reactome. 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: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:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl. 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:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl. 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:2000379; P:positive regulation of reactive oxygen species metabolic process; IEA:Ensembl. DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl. DR GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome. DR GO; GO:2000121; P:regulation of removal of superoxide radicals; IEA:Ensembl. DR GO; GO:0035634; P:response to stilbenoid; IEA:Ensembl. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0034134; P:toll-like receptor 2 signaling pathway; TAS:Reactome. DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; TAS:Reactome. DR GO; GO:0002224; P:toll-like receptor signaling pathway; TAS:Reactome. DR GO; GO:0038123; P:toll-like receptor TLR1:TLR2 signaling pathway; TAS:Reactome. DR GO; GO:0038124; P:toll-like receptor TLR6:TLR2 signaling pathway; TAS:Reactome. DR InterPro; IPR002159; CD36. DR InterPro; IPR005428; CD36_antigen. DR PANTHER; PTHR11923; PTHR11923; 1. DR Pfam; PF01130; CD36; 1. DR PRINTS; PR01610; CD36ANTIGEN. DR PRINTS; PR01609; CD36FAMILY. PE 1: Evidence at protein level; KW Alternative splicing; Cell adhesion; Cell membrane; Complete proteome; KW Direct protein sequencing; Disease mutation; Disulfide bond; KW Glycoprotein; Lipoprotein; Membrane; Palmitate; Polymorphism; KW Receptor; Reference proteome; Transmembrane; Transmembrane helix; KW Transport. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2468669}. FT CHAIN 2 472 Platelet glycoprotein 4. FT /FTId=PRO_0000144151. FT TOPO_DOM 2 7 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 8 29 Helical. {ECO:0000255}. FT TOPO_DOM 30 439 Extracellular. {ECO:0000255}. FT TRANSMEM 440 461 Helical. {ECO:0000255}. FT TOPO_DOM 462 472 Cytoplasmic. {ECO:0000255}. FT REGION 93 120 Required for interaction with FT thrombospondins, THBS1 and THBS2. FT REGION 460 472 Interaction with PTK2, PXN and LYN. FT {ECO:0000269|PubMed:20037584}. FT SITE 463 463 Critical for TLR4-TLR6 dimerization and FT signaling. {ECO:0000269|PubMed:20037584}. FT LIPID 3 3 S-palmitoyl cysteine. FT {ECO:0000269|PubMed:8798390}. FT LIPID 7 7 S-palmitoyl cysteine. FT {ECO:0000269|PubMed:8798390}. FT LIPID 464 464 S-palmitoyl cysteine. FT {ECO:0000269|PubMed:8798390}. FT LIPID 466 466 S-palmitoyl cysteine. FT {ECO:0000269|PubMed:8798390}. FT CARBOHYD 79 79 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 102 102 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 134 134 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 163 163 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 205 205 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:19159218}. FT CARBOHYD 220 220 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 235 235 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 247 247 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 321 321 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:18780401}. FT CARBOHYD 417 417 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:16263699, FT ECO:0000269|PubMed:19159218}. FT DISULFID 243 311 {ECO:0000250}. FT DISULFID 272 333 {ECO:0000250}. FT DISULFID 313 322 {ECO:0000250}. FT VAR_SEQ 144 203 Missing (in isoform 4). FT {ECO:0000303|Ref.7}. FT /FTId=VSP_055976. FT VAR_SEQ 234 272 Missing (in isoform 3). FT {ECO:0000303|Ref.7}. FT /FTId=VSP_055977. FT VAR_SEQ 274 288 SIYAVFESDVNLKGI -> ETCVHFTSSFSVCKS (in FT isoform 2). {ECO:0000303|Ref.7}. FT /FTId=VSP_055978. FT VAR_SEQ 289 472 Missing (in isoform 2). FT {ECO:0000303|Ref.7}. FT /FTId=VSP_055979. FT VARIANT 90 90 P -> S (in PG4D; type I; degradation in FT the cytoplasm due to defects in FT maturation; dbSNP:rs3765187). FT {ECO:0000269|PubMed:11950861, FT ECO:0000269|PubMed:7533783}. FT /FTId=VAR_017913. FT VARIANT 123 123 E -> K (in individuals from a malaria FT endemic area in West Africa; FT dbSNP:rs183461468). FT {ECO:0000269|PubMed:11668637}. FT /FTId=VAR_017914. FT VARIANT 127 127 S -> L (in dbSNP:rs201765331). FT {ECO:0000269|PubMed:12506336}. FT /FTId=VAR_019049. FT VARIANT 154 154 V -> F (in dbSNP:rs5957). FT {ECO:0000269|PubMed:10391209}. FT /FTId=VAR_013918. FT VARIANT 174 174 T -> A (in individuals from a malaria FT endemic area in West Africa). FT {ECO:0000269|PubMed:11668637}. FT /FTId=VAR_017915. FT VARIANT 232 232 G -> GN (in individuals from a malaria FT endemic area in West Africa). FT {ECO:0000269|PubMed:11668637}. FT /FTId=VAR_017916. FT VARIANT 254 254 F -> L (in PG4D; type I; FT dbSNP:rs142186404). FT {ECO:0000269|PubMed:11950861}. FT /FTId=VAR_017917. FT VARIANT 271 271 I -> T (in individuals from a malaria FT endemic area in West Africa). FT {ECO:0000269|PubMed:11668637}. FT /FTId=VAR_017918. FT VARIANT 386 386 R -> W (in dbSNP:rs148910227). FT {ECO:0000269|Ref.7}. FT /FTId=VAR_071161. FT VARIANT 413 413 I -> L (in PG4D; type I). FT {ECO:0000269|PubMed:11950861}. FT /FTId=VAR_017919. FT VARIANT 470 470 T -> I (in dbSNP:rs200771788). FT {ECO:0000269|Ref.7}. FT /FTId=VAR_071162. FT MUTAGEN 462 472 SYCACRSKTIK->AAAAAAAAAAA: No effect on FT cell surface location. Loss of oxLDL- FT induced NF-kappa-B activation. FT {ECO:0000269|PubMed:20037584}. FT MUTAGEN 463 463 Y->A: No effect on cell surface location. FT Loss of oxLDL-induced NF-kappa-B FT activation. Loss of complex formation FT with TLR4 and TLR6. FT {ECO:0000269|PubMed:20037584}. FT MUTAGEN 464 464 C->S: No effect on cell surface location, FT nor on oxLDL-induced NF-kappa-B FT activation. FT {ECO:0000269|PubMed:20037584}. FT CONFLICT 44 44 L -> R (in Ref. 4; AAD13993). FT {ECO:0000305}. FT CONFLICT 238 238 Y -> D (in Ref. 4; AAD13993). FT {ECO:0000305}. FT CONFLICT 374 374 E -> Q (in Ref. 3; AAA16068 and 13; AA FT sequence). {ECO:0000305}. 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 //