CD36
entrez
948
canonical
uniprot
P16671
canonical
ensembl
ENSG00000135218
resolver
ensp
ENSP00000308165
resolver
ensp
ENSP00000378268
resolver
ensp
ENSP00000392298
resolver
ensp
ENSP00000401863
resolver
ensp
ENSP00000411411
resolver
ensp
ENSP00000415743
resolver
ensp
ENSP00000431296
resolver
ensp
ENSP00000525984
resolver
ensp
ENSP00000525989
resolver
ensp
ENSP00000525993
resolver
ensp
ENSP00000526001
resolver
ensp
ENSP00000526002
resolver
ensp
ENSP00000526004
resolver
ensp
ENSP00000526008
resolver
ensp
ENSP00000526011
resolver
ensp
ENSP00000526013
resolver
ensp
ENSP00000526015
resolver
ensp
ENSP00000626990
resolver
ensp
ENSP00000627022
resolver
ensp
ENSP00000695084
resolver
enst
ENST00000534394
resolver
genesymbol
CD36
resolver
genesymbol_syn
GP3B
resolver
genesymbol_syn
GP4
resolver
hgnc
HGNC:1663
resolver
uniprot
A4D1B1
resolver
uniprot
B7Z6C3
resolver
uniprot
D9IX66
resolver
uniprot
D9IX67
resolver
uniprot
D9IX68
resolver
uniprot
D9IX69
resolver
uniprot
E9PLT1
resolver
uniprot
Q13966
resolver
uniprot
Q16093
resolver
uniprot
Q8TCV7
resolver
uniprot
Q9BPZ8
resolver
uniprot
Q9BQC2
resolver
uniprot
Q9BZM8
resolver
uniprot
Q9BZN3
resolver
uniprot
Q9BZN4
resolver
uniprot
Q9BZN5
resolver
uniprot_entry
A4D1B1_HUMAN
resolver
uniprot_entry
B7Z6C3_HUMAN
resolver
uniprot_entry
CD36_HUMAN
resolver
uniprot_entry
E9PLT1_HUMAN
resolver
uniprot_sec
D9IX66
resolver
uniprot_sec
D9IX67
resolver
uniprot_sec
D9IX68
resolver
uniprot_sec
D9IX69
resolver
uniprot_sec
Q13966
resolver
uniprot_sec
Q16093
resolver
uniprot_sec
Q8TCV7
resolver
uniprot_sec
Q9BPZ8
resolver
uniprot_sec
Q9BQC2
resolver
uniprot_sec
Q9BZM8
resolver
uniprot_sec
Q9BZN3
resolver
uniprot_sec
Q9BZN4
resolver
uniprot_sec
Q9BZN5
resolver
amino_acid_sequence
MGCDRNCGLIAGAVIGAVLAVFGGILMPVGDLLIQKTIKKQVVLEEGTIAFKNWVKTGTEVYRQFWIFDVQNPQEVMMNSSNIQVKQRGPYTYRVRFLAKENVTQDAEDNTVSFLQPNGAIFEPSLSVGTEADNFTVLNLAVAAASHIYQNQFVQMILNSLINKSKSSMFQVRTLRELLWGYRDPFLSLVPYPVTTTVGLFYPYNNTADGVYKVFNGKDNISKVAIIDTYKGKRNLSYWESHCDMINGTDAASFPPFVEKSQVLQFFSSDICRSIYAVFESDVNLKGIPVYRFVLPSKAFASPVENPDNYCFCTEKIISKNCTSYGVLDISKCKEGRPVYISLPHFLYASPDVSEPIDGLNPNEEEHRTYLDIEPITGFTLQFAKRLQVNLLVKPSEKIQVLKNLKRNYIVPILWLNETGTIGDEKANMFRSQVTGKINLLGLIEMILLSVGVVMFVAFMISYCACRSKTIK
uniprot
proteins
disease_involvement
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 variants 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 variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Multifunctional glycoprotein that acts as a 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- and very 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- and very 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:21395585, PubMed:21610069). Mechanistically, palmitoylated CD36 captures fatty acids on the cell surface, the binding of fatty acids activates downstream kinase LYN, which phosphorylates the palmitoyltransferase ZDHHC5 and inactivates it, resulting in the subsequent depalmitoylation of CD36, a step needed to initiate the endocytic process and delivery of fatty acids into the cell (PubMed:32958780). 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 thrombospondins, THBS1 and THBS2, mediating their antiangiogenic effects (By similarity). Involved in inducing apoptosis in podocytes in response to elevated free fatty acids, acting together with THBS1 (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:21395585, 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}.
uniprot
proteins
mass_dalton
53053
uniprot
proteins
mutagenesis
MUTAGEN 462..472; /note="SYCACRSKTIK->AAAAAAAAAAA: No effect on cell surface location. Loss of oxLDL-induced NF-kappa-B activation."; /evidence="ECO:0000269|PubMed:20037584"; MUTAGEN 463; /note="Y->A: No effect on cell surface location. Loss of oxLDL-induced NF-kappa-B activation. Loss of complex formation with TLR4 and TLR6."; /evidence="ECO:0000269|PubMed:20037584"; MUTAGEN 464; /note="C->S: No effect on cell surface location, nor on oxLDL-induced NF-kappa-B activation."; /evidence="ECO:0000269|PubMed:20037584"; MUTAGEN 469..472; /note="KTIK->ATIA: Abolishes ubiquitination induced by lipids. Enhances fatty acid uptake."; /evidence="ECO:0000269|PubMed:18353783, ECO:0000269|PubMed:21610069
uniprot
proteins
post_translational_modification
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: Palmitoylated by ZDHHC5 (PubMed:32958780). Palmitoylation is required for proper localization at the plasma membrane (PubMed:32958780, PubMed:37461827). {ECO:0000269|PubMed:32958780, ECO:0000269|PubMed:37461827}.; 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:18353783, PubMed:21610069). Ubiquitination and degradation are inhibited by insulin which blocks the effect of fatty acids (PubMed:18353783). {ECO:0000269|PubMed:18353783, ECO:0000269|PubMed:21610069}.
uniprot
proteins
protein_family
CD36 family
uniprot
proteins
pubmed
10391209
uniprot
proteins
pubmed
10613822
uniprot
proteins
pubmed
10890433
uniprot
proteins
pubmed
11668637
uniprot
proteins
pubmed
11950861
uniprot
proteins
pubmed
12506336
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
1371676
uniprot
proteins
pubmed
15242332
uniprot
proteins
pubmed
15282206
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16263699
uniprot
proteins
pubmed
16880211
uniprot
proteins
pubmed
18353783
uniprot
proteins
pubmed
18753675
uniprot
proteins
pubmed
18780401
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19471024
uniprot
proteins
pubmed
19864601
uniprot
proteins
pubmed
20037584
uniprot
proteins
pubmed
21395585
uniprot
proteins
pubmed
21610069
uniprot
proteins
pubmed
22240721
uniprot
proteins
pubmed
2468669
uniprot
proteins
pubmed
2473841
uniprot
proteins
pubmed
25822988
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
27667267
uniprot
proteins
pubmed
32958780
uniprot
proteins
pubmed
37461827
uniprot
proteins
pubmed
7503937
uniprot
proteins
pubmed
7505064
uniprot
proteins
pubmed
7518447
uniprot
proteins
pubmed
7533783
uniprot
proteins
pubmed
7693552
uniprot
proteins
pubmed
8798390
uniprot
proteins
sequence_length
472
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16880211, ECO:0000269|PubMed:32958780, ECO:0000269|PubMed:37461827}; 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}.
uniprot
proteins
transmembrane_region
TRANSMEM 8..29; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 440..461; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins