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Platelet glycoprotein 4 (Fatty acid translocase) (FAT) (Glycoprotein IIIb) (GPIIIB) (Leukocyte differentiation antigen CD36) (PAS IV) (PAS-4) (Platelet collagen receptor) (Platelet glycoprotein IV) (GPIV) (Thrombospondin receptor) (CD antigen CD36)

 CD36_HUMAN              Reviewed;         472 AA.
P16671; D9IX66; D9IX67; D9IX68; D9IX69; Q13966; Q16093; Q8TCV7;
Q9BPZ8; Q9BQC2; Q9BZM8; Q9BZN3; Q9BZN4; Q9BZN5;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
30-AUG-2017, entry version 191.
RecName: Full=Platelet glycoprotein 4;
AltName: Full=Fatty acid translocase;
Short=FAT;
AltName: Full=Glycoprotein IIIb;
Short=GPIIIB;
AltName: Full=Leukocyte differentiation antigen CD36;
AltName: Full=PAS IV;
AltName: Full=PAS-4;
AltName: Full=Platelet collagen receptor;
AltName: Full=Platelet glycoprotein IV;
Short=GPIV;
AltName: Full=Thrombospondin receptor;
AltName: CD_antigen=CD36;
Name=CD36; Synonyms=GP3B, GP4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=2473841; DOI=10.1016/0092-8674(89)90406-6;
Oquendo P., Hundt E., Lawler J., Seed B.;
"CD36 directly mediates cytoadherence of Plasmodium falciparum
parasitized erythrocytes.";
Cell 58:95-101(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Sugimoto Y., Tsuruo T.;
Submitted (AUG-1992) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=7693552; DOI=10.1016/0378-1119(93)90639-K;
Taylor K.T., Tang Y., Sobieski D.A., Lipsky R.H.;
"Characterization of two alternatively spliced 5'-untranslated exons
of the human CD36 gene in different cell types.";
Gene 133:205-212(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Platelet;
PubMed=7505064;
Wyler B., Daviet L., Bortkiewicz H., Bordet J.C., McGregor J.L.;
"Cloning of the cDNA encoding human platelet CD36: comparison to PCR
amplified fragments of monocyte, endothelial and HEL cells.";
Thromb. Haemost. 70:500-505(1993).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7518447;
Armesilla A.L., Vega M.A.;
"Structural organization of the gene for human CD36 glycoprotein.";
J. Biol. Chem. 269:18985-18991(1994).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), AND VARIANTS
TRP-386 AND ILE-470.
Wu G.-G., Curtis B.R., He B.-R., Zhou Z.-L., Zhou Y., Yang Y.-L.,
Li H.-Y., Shen W.-D., Liu J.-L., Zhao T.-M.;
"Frequency of CD36 deficiency and identification of novel CD36 gene
mutations in the Chinese population.";
Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skeletal muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PROTEIN SEQUENCE OF 2-37, AND GLYCOSYLATION.
TISSUE=Platelet;
PubMed=2468669;
Tandon N.N., Lipsky R.H., Burgess W.H., Jamieson G.A.;
"Isolation and characterization of platelet glycoprotein IV (CD36).";
J. Biol. Chem. 264:7570-7575(1989).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-203; 274-375 AND 419-472, AND
VARIANTS LYS-123; ALA-174; ASN-232 INS AND THR-271.
PubMed=11668637; DOI=10.1002/humu.1215;
Gelhaus A., Scheding A., Browne E., Burchard G.D., Horstmann R.D.;
"Variability of the CD36 gene in West Africa.";
Hum. Mutat. 18:444-450(2001).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 144-203 (ISOFORM 1/2).
PubMed=7503937; DOI=10.1006/geno.1993.1401;
Fernandez-Ruiz E., Armesilla A.L., Sanchez-Madrid F., Vega M.A.;
"Gene encoding the collagen type I and thrombospondin receptor CD36 is
located on chromosome 7q11.2.";
Genomics 17:759-761(1993).
[13]
PROTEIN SEQUENCE OF 261-273 AND 369-385.
TISSUE=Adipocyte;
PubMed=15242332; DOI=10.1042/BJ20040647;
Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.;
"Vectorial proteomics reveal targeting, phosphorylation and specific
fragmentation of polymerase I and transcript release factor (PTRF) at
the surface of caveolae in human adipocytes.";
Biochem. J. 383:237-248(2004).
[14]
INTERACTION WITH THBS1 AND THBS2.
PubMed=1371676; DOI=10.1016/0006-291X(92)91860-S;
Asch A.S., Silbiger S., Heimer E., Nachman R.L.;
"Thrombospondin sequence motif (CSVTCG) is responsible for CD36
binding.";
Biochem. Biophys. Res. Commun. 182:1208-1217(1992).
[15]
PALMITOYLATION AT CYS-3; CYS-7; CYS-464 AND CYS-466.
PubMed=8798390; DOI=10.1074/jbc.271.37.22315;
Tao N., Wagner S.J., Lublin D.M.;
"CD36 is palmitoylated on both N- and C-terminal cytoplasmic tails.";
J. Biol. Chem. 271:22315-22320(1996).
[16]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TLR2 AND TLR6.
PubMed=16880211; DOI=10.1074/jbc.M602794200;
Triantafilou M., Gamper F.G., Haston R.M., Mouratis M.A., Morath S.,
Hartung T., Triantafilou K.;
"Membrane sorting of toll-like receptor (TLR)-2/6 and TLR2/1
heterodimers at the cell surface determines heterotypic associations
with CD36 and intracellular targeting.";
J. Biol. Chem. 281:31002-31011(2006).
[17]
FUNCTION, UBIQUITINATION AT LYS-469 AND LYS-472, AND MUTAGENESIS OF
469-LYS--LYS-472.
PubMed=18353783; DOI=10.1074/jbc.M800008200;
Smith J., Su X., El-Maghrabi R., Stahl P.D., Abumrad N.A.;
"Opposite regulation of CD36 ubiquitination by fatty acids and
insulin: effects on fatty acid uptake.";
J. Biol. Chem. 283:13578-13585(2008).
[18]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-417.
TISSUE=Platelet;
PubMed=16263699; DOI=10.1074/mcp.M500324-MCP200;
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
"Elucidation of N-glycosylation sites on human platelet proteins: a
glycoproteomic approach.";
Mol. Cell. Proteomics 5:226-233(2006).
[19]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-321.
TISSUE=Milk;
PubMed=18780401; DOI=10.1002/pmic.200701057;
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
"Identification of N-linked glycoproteins in human milk by hydrophilic
interaction liquid chromatography and mass spectrometry.";
Proteomics 8:3833-3847(2008).
[20]
FUNCTION (MICROBIAL INFECTION).
PubMed=19864601; DOI=10.4049/jimmunol.0901374;
Erdman L.K., Cosio G., Helmers A.J., Gowda D.C., Grinstein S.,
Kain K.C.;
"CD36 and TLR interactions in inflammation and phagocytosis:
implications for malaria.";
J. Immunol. 183:6452-6459(2009).
[21]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-205 AND ASN-417.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[22]
REVIEW OF FUNCTION.
PubMed=19471024; DOI=10.1126/scisignal.272re3;
Silverstein R.L., Febbraio M.;
"CD36, a scavenger receptor involved in immunity, metabolism,
angiogenesis, and behavior.";
Sci. Signal. 2:RE3-RE3(2009).
[23]
FUNCTION, INTERACTION WITH LYN; PTK2; PXN; TLR4 AND TLR6, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF 462-SER--LYS-473; TYR-463 AND CYS-464.
PubMed=20037584; DOI=10.1038/ni.1836;
Stewart C.R., Stuart L.M., Wilkinson K., van Gils J.M., Deng J.,
Halle A., Rayner K.J., Boyer L., Zhong R., Frazier W.A.,
Lacy-Hulbert A., El Khoury J., Golenbock D.T., Moore K.J.;
"CD36 ligands promote sterile inflammation through assembly of a Toll-
like receptor 4 and 6 heterodimer.";
Nat. Immunol. 11:155-161(2010).
[24]
FUNCTION, UBIQUITINATION AT LYS-469 AND LYS-472, AND MUTAGENESIS OF
469-LYS--LYS-472.
PubMed=21610069; DOI=10.1074/jbc.M111.233551;
Tran T.T., Poirier H., Clement L., Nassir F., Pelsers M.M., Petit V.,
Degrace P., Monnot M.C., Glatz J.F., Abumrad N.A., Besnard P.,
Niot I.;
"Luminal lipid regulates CD36 levels and downstream signaling to
stimulate chylomicron synthesis.";
J. Biol. Chem. 286:25201-25210(2011).
[25]
FUNCTION.
PubMed=22240721; DOI=10.1038/oby.2011.374;
Keller K.L., Liang L.C., Sakimura J., May D., van Belle C., Breen C.,
Driggin E., Tepper B.J., Lanzano P.C., Deng L., Chung W.K.;
"Common variants in the CD36 gene are associated with oral fat
perception, fat preferences, and obesity in African Americans.";
Obesity 20:1066-1073(2012).
[26]
FUNCTION.
PubMed=25822988; DOI=10.1017/S0007114515000343;
Mrizak I., Sery O., Plesnik J., Arfa A., Fekih M., Bouslema A.,
Zaouali M., Tabka Z., Khan N.A.;
"The A allele of cluster of differentiation 36 (CD36) SNP 1761667
associates with decreased lipid taste perception in obese Tunisian
women.";
Br. J. Nutr. 113:1330-1337(2015).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[28]
VARIANT PG4D SER-90.
PubMed=7533783; DOI=10.1172/JCI117749;
Kashiwagi H., Tomiyama Y., Honda S., Kosugi S., Shiraga M., Nagao N.,
Sekiguchi S., Kanayama Y., Kurata Y., Matsuzawa Y.;
"Molecular basis of CD36 deficiency. Evidence that a 478C-->T
substitution (proline90-->serine) in CD36 cDNA accounts for CD36
deficiency.";
J. Clin. Invest. 95:1040-1046(1995).
[29]
VARIANT PHE-154.
PubMed=10391209; DOI=10.1038/10290;
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
"Characterization of single-nucleotide polymorphisms in coding regions
of human genes.";
Nat. Genet. 22:231-238(1999).
[30]
ERRATUM.
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
Nat. Genet. 23:373-373(1999).
[31]
ROLE IN MALARIA INFECTION.
PubMed=10890433; DOI=10.1038/35016636;
Aitman T.J., Cooper L.D., Norsworthy P.J., Wahid F.N., Gray J.K.,
Curtis B.R., McKeigue P.M., Kwiatkowski D., Greenwood B.M., Snow R.W.,
Hill A.V., Scott J.;
"Malaria susceptibility and CD36 mutation.";
Nature 405:1015-1016(2000).
[32]
VARIANTS PG4D SER-90; LEU-254 AND LEU-413.
PubMed=11950861; DOI=10.1136/jmg.39.4.286;
Hanawa H., Watanabe K., Nakamura T., Ogawa Y., Toba K., Fuse I.,
Kodama M., Kato K., Fuse K., Aizawa Y.;
"Identification of cryptic splice site, exon skipping, and novel point
mutations in type I CD36 deficiency.";
J. Med. Genet. 39:286-291(2002).
[33]
VARIANT LEU-127, AND ROLE IN MALARIA INFECTION.
PubMed=12506336; DOI=10.1086/346091;
Omi K., Ohashi J., Patarapotikul J., Hananantachai H., Naka I.,
Looareesuwan S., Tokunaga K.;
"CD36 polymorphism is associated with protection from cerebral
malaria.";
Am. J. Hum. Genet. 72:364-374(2003).
[34]
INVOLVEMENT IN CHDS7.
PubMed=15282206; DOI=10.1093/hmg/ddh233;
Ma X., Bacci S., Mlynarski W., Gottardo L., Soccio T., Menzaghi C.,
Iori E., Lager R.A., Shroff A.R., Gervino E.V., Nesto R.W.,
Johnstone M.T., Abumrad N.A., Avogaro A., Trischitta V., Doria A.;
"A common haplotype at the CD36 locus is associated with high free
fatty acid levels and increased cardiovascular risk in Caucasians.";
Hum. Mol. Genet. 13:2197-2205(2004).
[35]
ERRATUM.
Ma X., Bacci S., Mlynarski W., Gottardo L., Soccio T., Menzaghi C.,
Iori E., Lager R.A., Shroff A.R., Gervino E.V., Nesto R.W.,
Johnstone M.T., Abumrad N.A., Avogaro A., Trischitta V., Doria A.;
Hum. Mol. Genet. 14:3973-3973(2005).
[36]
INVOLVEMENT IN PG4D, AND FUNCTION.
PubMed=18753675; DOI=10.1194/jlr.P700032-JLR200;
Masuda D., Hirano K., Oku H., Sandoval J.C., Kawase R.,
Yuasa-Kawase M., Yamashita Y., Takada M., Tsubakio-Yamamoto K.,
Tochino Y., Koseki M., Matsuura F., Nishida M., Kawamoto T.,
Ishigami M., Hori M., Shimomura I., Yamashita S.;
"Chylomicron remnants are increased in the postprandial state in CD36
deficiency.";
J. Lipid Res. 50:999-1011(2009).
[37] {ECO:0000244|PDB:5LGD}
X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS), AND INTERACTION WITH
PLASMODIUM FALCIPARUM EMP1.
PubMed=27667267; DOI=10.1038/ncomms12837;
Hsieh F.L., Turner L., Bolla J.R., Robinson C.V., Lavstsen T.,
Higgins M.K.;
"The structural basis for CD36 binding by the malaria parasite.";
Nat. Commun. 7:12837-12837(2016).
-!- FUNCTION: Multifunctional glycoprotein that acts as receptor for a
broad range of ligands. Ligands can be of proteinaceous nature
like thrombospondin, fibronectin, collagen or amyloid-beta as well
as of lipidic nature such as oxidized low-density lipoprotein
(oxLDL), anionic phospholipids, long-chain fatty acids and
bacterial diacylated lipopeptides. They are generally multivalent
and can therefore engage multiple receptors simultaneously, the
resulting formation of CD36 clusters initiates signal transduction
and internalization of receptor-ligand complexes. The dependency
on coreceptor signaling is strongly ligand specific. Cellular
responses to these ligands are involved in angiogenesis,
inflammatory response, fatty acid metabolism, taste and dietary
fat processing in the intestine (Probable). Binds long-chain fatty
acids and facilitates their transport into cells, thus
participating in muscle lipid utilization, adipose energy storage,
and gut fat absorption (By similarity) (PubMed:18353783,
PubMed:21610069). In the small intestine, plays a role in proximal
absorption of dietary fatty acid and cholesterol for optimal
chylomicron formation, possibly through the activation of MAPK1/3
(ERK1/2) signaling pathway (By similarity) (PubMed:18753675).
Involved in oral fat perception and preferences (PubMed:22240721,
PubMed:25822988). Detection into the tongue of long-chain fatty
acids leads to a rapid and sustained rise in flux and protein
content of pancreatobiliary secretions (By similarity). In taste
receptor cells, mediates the induction of an increase in
intracellular calcium levels by long-chain fatty acids, leading to
the activation of the gustatory neurons in the nucleus of the
solitary tract (By similarity). Important factor in both
ventromedial hypothalamus neuronal sensing of long-chain fatty
acid and the regulation of energy and glucose homeostasis (By
similarity). Receptor for thombospondins, THBS1 and THBS2,
mediating their antiangiogenic effects (By similarity). As a
coreceptor for TLR4:TLR6 heterodimer, promotes inflammation in
monocytes/macrophages. Upon ligand binding, such as oxLDL or
amyloid-beta 42, interacts with the heterodimer TLR4:TLR6, the
complex is internalized and triggers inflammatory response,
leading to NF-kappa-B-dependent production of CXCL1, CXCL2 and
CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine,
via TICAM1 signaling pathway, as well as IL1B secretion, through
the priming and activation of the NLRP3 inflammasome (By
similarity) (PubMed:20037584). Selective and nonredundant sensor
of microbial diacylated lipopeptide that signal via TLR2:TLR6
heterodimer, this cluster triggers signaling from the cell
surface, leading to the NF-kappa-B-dependent production of TNF,
via MYD88 signaling pathway and subsequently is targeted to the
Golgi in a lipid-raft dependent pathway (By similarity)
(PubMed:16880211). {ECO:0000250|UniProtKB:Q07969,
ECO:0000250|UniProtKB:Q08857, ECO:0000269|PubMed:16880211,
ECO:0000269|PubMed:18353783, ECO:0000269|PubMed:18753675,
ECO:0000269|PubMed:20037584, ECO:0000269|PubMed:21610069,
ECO:0000269|PubMed:22240721, ECO:0000269|PubMed:25822988,
ECO:0000305|PubMed:19471024}.
-!- FUNCTION: (Microbial infection) Directly mediates cytoadherence of
Plasmodium falciparum parasitized erythrocytes and the
internalization of particles independently of TLR signaling.
{ECO:0000269|PubMed:10890433, ECO:0000269|PubMed:12506336,
ECO:0000269|PubMed:19864601}.
-!- SUBUNIT: Interacts with THBS1 and THBS2; the interactions mediate
the THBS antiangiogenic activity (PubMed:1371676). Upon
interaction with a ligand, such as oxidized low-density
lipoprotein (oxLDL) or amyloid-beta 42, rapidly forms a complex
with TLR4 and TLR6; the complex is internalized and triggers an
inflammatory signal. Through its C-terminus, interacts with PTK2,
PXN and LYN, but not with SRC. LYN kinase activity is required for
facilitating TLR4:TLR6 heterodimerization and signal initiation
(PubMed:1371676, PubMed:20037584). Upon interaction with ligands
such as diacylated lipopeptides, interacts with the TLR2:TLR6
heterodimer (PubMed:16880211). Interacts with CD9, CD81, FCER1G,
ITGB2 and/or ITGB2; forming a membrane heteromeric complex
required for the internalization of CD36 and its ligands (By
similarity). {ECO:0000250|UniProtKB:Q08857,
ECO:0000269|PubMed:1371676, ECO:0000269|PubMed:16880211,
ECO:0000269|PubMed:20037584}.
-!- SUBUNIT: (Microbial infection) Binds to Plasmodium falciparum
EMP1. {ECO:0000269|PubMed:27667267}.
-!- INTERACTION:
P07948:LYN; NbExp=3; IntAct=EBI-2808214, EBI-79452;
P07996:THBS1; NbExp=2; IntAct=EBI-2808214, EBI-13915509;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16880211};
Multi-pass membrane protein {ECO:0000255}. Membrane raft
{ECO:0000269|PubMed:16880211}. Golgi apparatus
{ECO:0000269|PubMed:16880211}. Apical cell membrane
{ECO:0000250|UniProtKB:Q08857}. Note=Upon ligand-binding,
internalized through dynamin-dependent endocytosis.
{ECO:0000269|PubMed:20037584}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=P16671-1; Sequence=Displayed;
Name=2; Synonyms=ex8-del;
IsoId=P16671-2; Sequence=VSP_055978, VSP_055979;
Name=3; Synonyms=ex6-7-del;
IsoId=P16671-3; Sequence=VSP_055977;
Name=4; Synonyms=ex4-del;
IsoId=P16671-4; Sequence=VSP_055976;
-!- PTM: N-glycosylated and O-glycosylated with a ratio of 2:1.
{ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:18780401,
ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:2468669}.
-!- PTM: Ubiquitinated at Lys-469 and Lys-472. Ubiquitination is
induced by fatty acids such as oleic acid and leads to degradation
by the proteasome (PubMed:21610069, PubMed:18353783).
Ubiquitination and degradation are inhibited by insulin which
blocks the effect of fatty acids (PubMed:18353783).
{ECO:0000269|PubMed:18353783, ECO:0000269|PubMed:21610069}.
-!- POLYMORPHISM: Genetic variations in CD36 are involved in
susceptibility to malaria and influence the severity and outcome
of malaria infection [MIM:611162].
-!- DISEASE: Platelet glycoprotein IV deficiency (PG4D) [MIM:608404]:
A disorder characterized by macrothrombocytopenia without notable
hemostatic problems and bleeding tendency. Platelet glycoprotein
IV deficiency can be divided into 2 subgroups. The type I
phenotype is characterized by platelets and monocytes/macrophages
exhibiting complete CD36 deficiency. The type II phenotype lacks
the surface expression of CD36 in platelets, but expression in
monocytes/macrophages is near normal.
{ECO:0000269|PubMed:11950861, ECO:0000269|PubMed:7533783}.
Note=The disease is caused by mutations affecting the gene
represented in this entry. Patients also have postprandial
hypertriglyceridemia, insulin resistance and hypertension
increasing atherosclerotic risk. {ECO:0000269|PubMed:18753675}.
-!- DISEASE: Coronary heart disease 7 (CHDS7) [MIM:610938]: A
multifactorial disease characterized by an imbalance between
myocardial functional requirements and the capacity of the
coronary vessels to supply sufficient blood flow. Decreased
capacity of the coronary vessels is often associated with
thickening and loss of elasticity of the coronary arteries.
{ECO:0000269|PubMed:15282206}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the CD36 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAM14636.2; Type=Frameshift; Positions=53; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=CD36 entry;
URL="https://en.wikipedia.org/wiki/CD36";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/cd36/";
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EMBL; M24795; AAA35534.1; -; mRNA.
EMBL; M98398; AAA58412.1; -; mRNA.
EMBL; M98399; AAA58413.1; -; mRNA.
EMBL; L06850; AAA16068.1; -; mRNA.
EMBL; S67532; AAD13993.1; -; mRNA.
EMBL; Z32770; CAA83662.1; -; Genomic_DNA.
EMBL; Z32754; CAA83662.1; JOINED; Genomic_DNA.
EMBL; Z32755; CAA83662.1; JOINED; Genomic_DNA.
EMBL; Z32756; CAA83662.1; JOINED; Genomic_DNA.
EMBL; Z32757; CAA83662.1; JOINED; Genomic_DNA.
EMBL; Z32758; CAA83662.1; JOINED; Genomic_DNA.
EMBL; Z32759; CAA83662.1; JOINED; Genomic_DNA.
EMBL; Z32760; CAA83662.1; JOINED; Genomic_DNA.
EMBL; Z32761; CAA83662.1; JOINED; Genomic_DNA.
EMBL; Z32762; CAA83662.1; JOINED; Genomic_DNA.
EMBL; Z32763; CAA83662.1; JOINED; Genomic_DNA.
EMBL; Z32764; CAA83662.1; JOINED; Genomic_DNA.
EMBL; AY095373; AAM14636.2; ALT_FRAME; Genomic_DNA.
EMBL; HM217023; ADI80543.1; -; mRNA.
EMBL; HM217024; ADI80544.1; -; mRNA.
EMBL; HM217025; ADI80545.1; -; mRNA.
EMBL; HM217026; ADI80546.1; -; mRNA.
EMBL; AC004862; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC073182; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC073850; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC092108; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC124834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC008406; AAH08406.1; -; mRNA.
EMBL; AF300626; AAG60625.1; -; Genomic_DNA.
EMBL; AF300627; AAG60626.1; -; Genomic_DNA.
EMBL; AF300628; AAG60627.1; -; Genomic_DNA.
EMBL; AF300633; AAG60632.1; -; Genomic_DNA.
EMBL; AF300634; AAG60633.1; -; Genomic_DNA.
EMBL; AF300635; AAG60634.1; -; Genomic_DNA.
EMBL; AF300639; AAG60638.1; -; Genomic_DNA.
EMBL; AF300640; AAG60639.1; -; Genomic_DNA.
EMBL; S67044; AAB28992.1; -; mRNA.
EMBL; Z22924; CAA80504.1; -; Genomic_DNA.
CCDS; CCDS34673.1; -. [P16671-1]
CCDS; CCDS78249.1; -. [P16671-3]
CCDS; CCDS78250.1; -. [P16671-4]
PIR; A54870; A54870.
RefSeq; NP_000063.2; NM_000072.3. [P16671-1]
RefSeq; NP_001001547.1; NM_001001547.2. [P16671-1]
RefSeq; NP_001001548.1; NM_001001548.2. [P16671-1]
RefSeq; NP_001120915.1; NM_001127443.1. [P16671-1]
RefSeq; NP_001120916.1; NM_001127444.1. [P16671-1]
RefSeq; NP_001276837.1; NM_001289908.1. [P16671-3]
RefSeq; NP_001276838.1; NM_001289909.1. [P16671-4]
RefSeq; NP_001276840.1; NM_001289911.1.
RefSeq; XP_005250770.1; XM_005250713.1. [P16671-1]
RefSeq; XP_005250771.1; XM_005250714.1. [P16671-1]
RefSeq; XP_005250772.1; XM_005250715.4. [P16671-1]
UniGene; Hs.120949; -.
PDB; 5LGD; X-ray; 2.07 A; A=1-472.
PDBsum; 5LGD; -.
ProteinModelPortal; P16671; -.
SMR; P16671; -.
BioGrid; 107386; 19.
IntAct; P16671; 13.
STRING; 9606.ENSP00000308165; -.
ChEMBL; CHEMBL1744526; -.
SwissLipids; SLP:000001098; -.
TCDB; 9.B.39.1.4; the long chain fatty acid translocase (lcfat) family.
iPTMnet; P16671; -.
PhosphoSitePlus; P16671; -.
SwissPalm; P16671; -.
BioMuta; CD36; -.
DMDM; 115982; -.
MaxQB; P16671; -.
PaxDb; P16671; -.
PeptideAtlas; P16671; -.
PRIDE; P16671; -.
DNASU; 948; -.
Ensembl; ENST00000309881; ENSP00000308165; ENSG00000135218. [P16671-1]
Ensembl; ENST00000394788; ENSP00000378268; ENSG00000135218. [P16671-1]
Ensembl; ENST00000432207; ENSP00000411411; ENSG00000135218. [P16671-1]
Ensembl; ENST00000433696; ENSP00000401863; ENSG00000135218. [P16671-3]
Ensembl; ENST00000435819; ENSP00000399421; ENSG00000135218. [P16671-1]
Ensembl; ENST00000447544; ENSP00000415743; ENSG00000135218. [P16671-1]
Ensembl; ENST00000538969; ENSP00000439543; ENSG00000135218. [P16671-4]
Ensembl; ENST00000544133; ENSP00000441956; ENSG00000135218. [P16671-2]
GeneID; 948; -.
KEGG; hsa:948; -.
UCSC; uc003uhc.4; human. [P16671-1]
CTD; 948; -.
DisGeNET; 948; -.
GeneCards; CD36; -.
HGNC; HGNC:1663; CD36.
HPA; CAB025866; -.
HPA; HPA002018; -.
MalaCards; CD36; -.
MIM; 173510; gene.
MIM; 248310; phenotype.
MIM; 608404; phenotype.
MIM; 610938; phenotype.
MIM; 611162; phenotype.
neXtProt; NX_P16671; -.
OpenTargets; ENSG00000135218; -.
PharmGKB; PA26212; -.
eggNOG; KOG3776; Eukaryota.
eggNOG; ENOG410XS17; LUCA.
GeneTree; ENSGT00530000062927; -.
HOVERGEN; HBG002754; -.
InParanoid; P16671; -.
KO; K06259; -.
OMA; NVTQDPE; -.
OrthoDB; EOG091G0CH9; -.
PhylomeDB; P16671; -.
TreeFam; TF317925; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-1236973; Cross-presentation of particulate exogenous antigens (phagosomes).
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-166058; MyD88:Mal cascade initiated on plasma membrane.
Reactome; R-HSA-168188; Toll Like Receptor TLR6:TLR2 Cascade.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-3000471; Scavenging by Class B Receptors.
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
Reactome; R-HSA-5602498; MyD88 deficiency (TLR2/4).
Reactome; R-HSA-5603041; IRAK4 deficiency (TLR2/4).
Reactome; R-HSA-5686938; Regulation of TLR by endogenous ligand.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SIGNOR; P16671; -.
ChiTaRS; CD36; human.
GeneWiki; CD36; -.
GenomeRNAi; 948; -.
PRO; PR:P16671; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000135218; -.
ExpressionAtlas; P16671; baseline and differential.
Genevisible; P16671; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0031526; C:brush border membrane; ISS:UniProtKB.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:BHF-UCL.
GO; GO:0005622; C:intracellular; IPI:ARUK-UCL.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
GO; GO:0045335; C:phagocytic vesicle; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0031092; C:platelet alpha granule membrane; TAS:Reactome.
GO; GO:0043235; C:receptor complex; IPI:ARUK-UCL.
GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
GO; GO:0001540; F:amyloid-beta binding; TAS:ARUK-UCL.
GO; GO:0008035; F:high-density lipoprotein particle binding; IEA:Ensembl.
GO; GO:0008289; F:lipid binding; IDA:BHF-UCL.
GO; GO:0071813; F:lipoprotein particle binding; IDA:UniProtKB.
GO; GO:0070892; F:lipoteichoic acid receptor activity; IEA:Ensembl.
GO; GO:0030169; F:low-density lipoprotein particle binding; IDA:BHF-UCL.
GO; GO:0005041; F:low-density lipoprotein receptor activity; IMP:BHF-UCL.
GO; GO:0005044; F:scavenger receptor activity; TAS:ARUK-UCL.
GO; GO:0070053; F:thrombospondin receptor activity; ISS:BHF-UCL.
GO; GO:0035325; F:Toll-like receptor binding; IPI:ARUK-UCL.
GO; GO:0050431; F:transforming growth factor beta binding; ISS:BHF-UCL.
GO; GO:1990000; P:amyloid fibril formation; ISS:UniProtKB.
GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0043277; P:apoptotic cell clearance; IEA:Ensembl.
GO; GO:0007596; P:blood coagulation; TAS:ProtInc.
GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:Ensembl.
GO; GO:1904646; P:cellular response to amyloid-beta; IGI:ARUK-UCL.
GO; GO:0071726; P:cellular response to diacyl bacterial lipopeptide; IDA:UniProtKB.
GO; GO:0071447; P:cellular response to hydroperoxide; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0071223; P:cellular response to lipoteichoic acid; IEA:Ensembl.
GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISS:UniProtKB.
GO; GO:0019934; P:cGMP-mediated signaling; IDA:BHF-UCL.
GO; GO:0070508; P:cholesterol import; ISS:UniProtKB.
GO; GO:0030301; P:cholesterol transport; ISS:BHF-UCL.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
GO; GO:0050702; P:interleukin-1 beta secretion; ISS:UniProtKB.
GO; GO:0050892; P:intestinal absorption; ISS:UniProtKB.
GO; GO:0030299; P:intestinal cholesterol absorption; ISS:UniProtKB.
GO; GO:0006629; P:lipid metabolic process; NAS:ProtInc.
GO; GO:0019915; P:lipid storage; IMP:BHF-UCL.
GO; GO:0042953; P:lipoprotein transport; IMP:BHF-UCL.
GO; GO:0044539; P:long-chain fatty acid import; IDA:UniProtKB.
GO; GO:0034383; P:low-density lipoprotein particle clearance; IMP:BHF-UCL.
GO; GO:0055096; P:low-density lipoprotein particle mediated signaling; IEA:Ensembl.
GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0044130; P:negative regulation of growth of symbiont in host; IEA:Ensembl.
GO; GO:0042992; P:negative regulation of transcription factor import into nucleus; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0007263; P:nitric oxide mediated signal transduction; IDA:BHF-UCL.
GO; GO:0006910; P:phagocytosis, recognition; IEA:Ensembl.
GO; GO:0034381; P:plasma lipoprotein particle clearance; ISS:BHF-UCL.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0030194; P:positive regulation of blood coagulation; IEA:Ensembl.
GO; GO:2000334; P:positive regulation of blood microparticle formation; IEA:Ensembl.
GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IDA:BHF-UCL.
GO; GO:0010886; P:positive regulation of cholesterol storage; IEA:Ensembl.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; ISS:ARUK-UCL.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0032735; P:positive regulation of interleukin-12 production; IEA:Ensembl.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
GO; GO:0060907; P:positive regulation of macrophage cytokine production; IEA:Ensembl.
GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IMP:BHF-UCL.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IGI:ARUK-UCL.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISS:ARUK-UCL.
GO; GO:1900227; P:positive regulation of NLRP3 inflammasome complex assembly; ISS:UniProtKB.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; IEA:Ensembl.
GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; ISS:ARUK-UCL.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
GO; GO:2000505; P:regulation of energy homeostasis; ISS:UniProtKB.
GO; GO:0019216; P:regulation of lipid metabolic process; TAS:Reactome.
GO; GO:0043497; P:regulation of protein heterodimerization activity; IMP:ARUK-UCL.
GO; GO:2000121; P:regulation of removal of superoxide radicals; IEA:Ensembl.
GO; GO:0034121; P:regulation of toll-like receptor signaling pathway; IGI:ARUK-UCL.
GO; GO:0070542; P:response to fatty acid; ISS:UniProtKB.
GO; GO:0070543; P:response to linoleic acid; ISS:UniProtKB.
GO; GO:0033993; P:response to lipid; ISS:UniProtKB.
GO; GO:0035634; P:response to stilbenoid; IEA:Ensembl.
GO; GO:0050909; P:sensory perception of taste; ISS:UniProtKB.
GO; GO:0002224; P:toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0038124; P:toll-like receptor TLR6:TLR2 signaling pathway; TAS:Reactome.
GO; GO:0034197; P:triglyceride transport; ISS:UniProtKB.
InterPro; IPR005428; CD36/SCARB1/SNMP1.
InterPro; IPR033076; CD36_chordates.
InterPro; IPR002159; CD36_fam.
PANTHER; PTHR11923; PTHR11923; 1.
PANTHER; PTHR11923:SF87; PTHR11923:SF87; 1.
Pfam; PF01130; CD36; 1.
PRINTS; PR01610; CD36ANTIGEN.
PRINTS; PR01609; CD36FAMILY.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
Complete proteome; Direct protein sequencing; Disease mutation;
Disulfide bond; Glycoprotein; Golgi apparatus; Isopeptide bond;
Lipoprotein; Membrane; Palmitate; Polymorphism; Receptor;
Reference proteome; Transmembrane; Transmembrane helix; Transport;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2468669}.
CHAIN 2 472 Platelet glycoprotein 4.
/FTId=PRO_0000144151.
TOPO_DOM 2 7 Cytoplasmic. {ECO:0000255}.
TRANSMEM 8 29 Helical. {ECO:0000255}.
TOPO_DOM 30 439 Extracellular. {ECO:0000255}.
TRANSMEM 440 461 Helical. {ECO:0000255}.
TOPO_DOM 462 472 Cytoplasmic. {ECO:0000255}.
REGION 93 120 Required for interaction with
thrombospondins, THBS1 and THBS2.
{ECO:0000269|PubMed:1371676}.
REGION 460 472 Interaction with PTK2, PXN and LYN.
{ECO:0000269|PubMed:20037584}.
SITE 463 463 Critical for TLR4-TLR6 dimerization and
signaling. {ECO:0000269|PubMed:20037584}.
LIPID 3 3 S-palmitoyl cysteine.
{ECO:0000269|PubMed:8798390}.
LIPID 7 7 S-palmitoyl cysteine.
{ECO:0000269|PubMed:8798390}.
LIPID 464 464 S-palmitoyl cysteine.
{ECO:0000269|PubMed:8798390}.
LIPID 466 466 S-palmitoyl cysteine.
{ECO:0000269|PubMed:8798390}.
CARBOHYD 79 79 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 102 102 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 134 134 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 163 163 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 205 205 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 220 220 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 235 235 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 247 247 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 321 321 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18780401}.
CARBOHYD 417 417 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16263699,
ECO:0000269|PubMed:19159218}.
DISULFID 243 311 {ECO:0000250}.
DISULFID 272 333 {ECO:0000250}.
DISULFID 313 322 {ECO:0000250}.
CROSSLNK 469 469 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000305|PubMed:18353783,
ECO:0000305|PubMed:21610069}.
CROSSLNK 472 472 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000305|PubMed:18353783,
ECO:0000305|PubMed:21610069}.
VAR_SEQ 144 203 Missing (in isoform 4).
{ECO:0000303|Ref.7}.
/FTId=VSP_055976.
VAR_SEQ 234 272 Missing (in isoform 3).
{ECO:0000303|Ref.7}.
/FTId=VSP_055977.
VAR_SEQ 274 288 SIYAVFESDVNLKGI -> ETCVHFTSSFSVCKS (in
isoform 2). {ECO:0000303|Ref.7}.
/FTId=VSP_055978.
VAR_SEQ 289 472 Missing (in isoform 2).
{ECO:0000303|Ref.7}.
/FTId=VSP_055979.
VARIANT 90 90 P -> S (in PG4D; type I; degradation in
the cytoplasm due to defects in
maturation; dbSNP:rs3765187).
{ECO:0000269|PubMed:11950861,
ECO:0000269|PubMed:7533783}.
/FTId=VAR_017913.
VARIANT 123 123 E -> K (in individuals from a malaria
endemic area in West Africa;
dbSNP:rs183461468).
{ECO:0000269|PubMed:11668637}.
/FTId=VAR_017914.
VARIANT 127 127 S -> L (in dbSNP:rs201765331).
{ECO:0000269|PubMed:12506336}.
/FTId=VAR_019049.
VARIANT 154 154 V -> F (in dbSNP:rs5957).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_013918.
VARIANT 174 174 T -> A (in individuals from a malaria
endemic area in West Africa;
dbSNP:rs756525492).
{ECO:0000269|PubMed:11668637}.
/FTId=VAR_017915.
VARIANT 232 232 G -> GN (in individuals from a malaria
endemic area in West Africa).
{ECO:0000269|PubMed:11668637}.
/FTId=VAR_017916.
VARIANT 254 254 F -> L (in PG4D; type I;
dbSNP:rs142186404).
{ECO:0000269|PubMed:11950861}.
/FTId=VAR_017917.
VARIANT 271 271 I -> T (in individuals from a malaria
endemic area in West Africa;
dbSNP:rs370072057).
{ECO:0000269|PubMed:11668637}.
/FTId=VAR_017918.
VARIANT 386 386 R -> W (in dbSNP:rs148910227).
{ECO:0000269|Ref.7}.
/FTId=VAR_071161.
VARIANT 413 413 I -> L (in PG4D; type I;
dbSNP:rs121918035).
{ECO:0000269|PubMed:11950861}.
/FTId=VAR_017919.
VARIANT 470 470 T -> I (in dbSNP:rs200771788).
{ECO:0000269|Ref.7}.
/FTId=VAR_071162.
MUTAGEN 462 472 SYCACRSKTIK->AAAAAAAAAAA: No effect on
cell surface location. Loss of oxLDL-
induced NF-kappa-B activation.
{ECO:0000269|PubMed:20037584}.
MUTAGEN 463 463 Y->A: No effect on cell surface location.
Loss of oxLDL-induced NF-kappa-B
activation. Loss of complex formation
with TLR4 and TLR6.
{ECO:0000269|PubMed:20037584}.
MUTAGEN 464 464 C->S: No effect on cell surface location,
nor on oxLDL-induced NF-kappa-B
activation.
{ECO:0000269|PubMed:20037584}.
MUTAGEN 469 472 KTIK->ATIA: Abolishes ubiquitination
induced by lipids. Enhances fatty acid
uptake. {ECO:0000269|PubMed:18353783,
ECO:0000269|PubMed:21610069}.
CONFLICT 44 44 L -> R (in Ref. 4; AAD13993).
{ECO:0000305}.
CONFLICT 238 238 Y -> D (in Ref. 4; AAD13993).
{ECO:0000305}.
CONFLICT 374 374 E -> Q (in Ref. 3; AAA16068 and 13; AA
sequence). {ECO:0000305}.
HELIX 38 41 {ECO:0000244|PDB:5LGD}.
STRAND 42 45 {ECO:0000244|PDB:5LGD}.
HELIX 49 55 {ECO:0000244|PDB:5LGD}.
STRAND 61 71 {ECO:0000244|PDB:5LGD}.
HELIX 73 79 {ECO:0000244|PDB:5LGD}.
STRAND 83 96 {ECO:0000244|PDB:5LGD}.
STRAND 101 106 {ECO:0000244|PDB:5LGD}.
TURN 107 110 {ECO:0000244|PDB:5LGD}.
STRAND 111 117 {ECO:0000244|PDB:5LGD}.
STRAND 120 122 {ECO:0000244|PDB:5LGD}.
HELIX 124 126 {ECO:0000244|PDB:5LGD}.
STRAND 127 129 {ECO:0000244|PDB:5LGD}.
STRAND 134 138 {ECO:0000244|PDB:5LGD}.
HELIX 140 148 {ECO:0000244|PDB:5LGD}.
HELIX 152 164 {ECO:0000244|PDB:5LGD}.
STRAND 169 174 {ECO:0000244|PDB:5LGD}.
HELIX 175 180 {ECO:0000244|PDB:5LGD}.
HELIX 187 189 {ECO:0000244|PDB:5LGD}.
STRAND 208 215 {ECO:0000244|PDB:5LGD}.
HELIX 221 223 {ECO:0000244|PDB:5LGD}.
STRAND 227 230 {ECO:0000244|PDB:5LGD}.
STRAND 233 235 {ECO:0000244|PDB:5LGD}.
STRAND 237 240 {ECO:0000244|PDB:5LGD}.
HELIX 241 244 {ECO:0000244|PDB:5LGD}.
STRAND 251 253 {ECO:0000244|PDB:5LGD}.
STRAND 263 268 {ECO:0000244|PDB:5LGD}.
TURN 269 272 {ECO:0000244|PDB:5LGD}.
STRAND 273 285 {ECO:0000244|PDB:5LGD}.
STRAND 288 294 {ECO:0000244|PDB:5LGD}.
HELIX 297 300 {ECO:0000244|PDB:5LGD}.
TURN 303 305 {ECO:0000244|PDB:5LGD}.
HELIX 307 312 {ECO:0000244|PDB:5LGD}.
TURN 317 323 {ECO:0000244|PDB:5LGD}.
STRAND 326 329 {ECO:0000244|PDB:5LGD}.
HELIX 331 333 {ECO:0000244|PDB:5LGD}.
TURN 334 336 {ECO:0000244|PDB:5LGD}.
STRAND 339 342 {ECO:0000244|PDB:5LGD}.
HELIX 344 346 {ECO:0000244|PDB:5LGD}.
HELIX 351 354 {ECO:0000244|PDB:5LGD}.
STRAND 357 359 {ECO:0000244|PDB:5LGD}.
HELIX 364 367 {ECO:0000244|PDB:5LGD}.
STRAND 370 373 {ECO:0000244|PDB:5LGD}.
TURN 375 377 {ECO:0000244|PDB:5LGD}.
STRAND 379 393 {ECO:0000244|PDB:5LGD}.
HELIX 400 402 {ECO:0000244|PDB:5LGD}.
STRAND 409 421 {ECO:0000244|PDB:5LGD}.
HELIX 424 433 {ECO:0000244|PDB:5LGD}.
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


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