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Platelet glycoprotein 4 (Adipocyte membrane protein) (Fatty acid translocase) (Fatty acid transport protein) (Glycoprotein IIIb) (GPIIIB) (PAS IV) (PAS-4) (Platelet glycoprotein IV) (GPIV) (CD antigen CD36)

 CD36_RAT                Reviewed;         472 AA.
Q07969; Q925W0;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-MAY-2007, sequence version 3.
23-MAY-2018, entry version 132.
RecName: Full=Platelet glycoprotein 4;
AltName: Full=Adipocyte membrane protein;
AltName: Full=Fatty acid translocase;
AltName: Full=Fatty acid transport protein;
AltName: Full=Glycoprotein IIIb;
Short=GPIIIB;
AltName: Full=PAS IV;
AltName: Full=PAS-4;
AltName: Full=Platelet glycoprotein IV;
Short=GPIV;
AltName: CD_antigen=CD36;
Name=Cd36; Synonyms=Fat;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
TISSUE=Adipocyte;
PubMed=7688729;
Abumrad N.A., El-Maghrabi M.R., Amri E.-Z., Lopez E., Grimaldi P.A.;
"Cloning of a rat adipocyte membrane protein implicated in binding or
transport of long-chain fatty acids that is induced during
preadipocyte differentiation. Homology with human CD36.";
J. Biol. Chem. 268:17665-17668(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar;
PubMed=10409247;
Guthmann F., Haupt R., Looman A.C., Spener F., Ruestow B.;
"Fatty acid translocase/CD36 mediates the uptake of palmitate by type
II pneumocytes.";
Am. J. Physiol. 277:L191-L196(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Dark agouti;
Zhang X., Mayrhofer G., Ey P.L.;
"Potential allele of rat CD36 antigen.";
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[4]
PROTEIN SEQUENCE OF 2-31, AND PALMITOYLATION AT CYS-3 AND CYS-7.
TISSUE=Adipocyte;
PubMed=7504047;
Jochen A., Hays J.;
"Purification of the major substrate for palmitoylation in rat
adipocytes: N-terminal homology with CD36 and evidence for cell
surface acylation.";
J. Lipid Res. 34:1783-1792(1993).
[5]
PROTEIN SEQUENCE OF 2-16, AND FUNCTION.
STRAIN=Sprague-Dawley; TISSUE=Adipocyte;
PubMed=8320718; DOI=10.1007/BF00231876;
Harmon C.M., Abumrad N.A.;
"Binding of sulfosuccinimidyl fatty acids to adipocyte membrane
proteins: isolation and amino-terminal sequence of an 88-kD protein
implicated in transport of long-chain fatty acids.";
J. Membr. Biol. 133:43-49(1993).
[6]
FUNCTION.
PubMed=16276419; DOI=10.1172/JCI25299;
Laugerette F., Passilly-Degrace P., Patris B., Niot I., Febbraio M.,
Montmayeur J.P., Besnard P.;
"CD36 involvement in orosensory detection of dietary lipids,
spontaneous fat preference, and digestive secretions.";
J. Clin. Invest. 115:3177-3184(2005).
[7]
FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
UBIQUITINATION.
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).
[8]
FUNCTION.
PubMed=23557700; DOI=10.2337/db12-1689;
Le Foll C., Dunn-Meynell A., Musatov S., Magnan C., Levin B.E.;
"FAT/CD36: a major regulator of neuronal fatty acid sensing and energy
homeostasis in rats and mice.";
Diabetes 62:2709-2716(2013).
-!- 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 (By similarity) (PubMed:8320718).
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:8320718). 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:16276419,
PubMed:21610069). Involved in oral fat perception and preferences
(By similarity) (PubMed:16276419). 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)
(PubMed:16276419). 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) (PubMed:23557700). 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.
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). {ECO:0000250|UniProtKB:P16671,
ECO:0000250|UniProtKB:Q08857, ECO:0000269|PubMed:16276419,
ECO:0000269|PubMed:21610069, ECO:0000269|PubMed:23557700,
ECO:0000269|PubMed:8320718}.
-!- SUBUNIT: Interacts with THBS1 and THBS2; the interactions mediate
the THBS antiangiogenic activity. 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. Upon interaction with
ligands such as diacylated lipopeptides, interacts with the
TLR2:TLR6 heterodimer (By similarity). 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:P16671,
ECO:0000250|UniProtKB:Q08857}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21610069};
Multi-pass membrane protein {ECO:0000255}. Membrane raft
{ECO:0000250|UniProtKB:P16671}. Golgi apparatus
{ECO:0000250|UniProtKB:P16671}. Apical cell membrane
{ECO:0000269|PubMed:21610069}. Note=Upon ligand-binding,
internalized through dynamin-dependent endocytosis.
{ECO:0000250|UniProtKB:P16671}.
-!- TISSUE SPECIFICITY: Expressed at high levels in heart, intestine,
spleen, adipose tissue, skeletal muscle and, at lower levels, in
testes. {ECO:0000269|PubMed:7688729}.
-!- DEVELOPMENTAL STAGE: Induced during preadipocyte differentiation.
{ECO:0000269|PubMed:7688729}.
-!- 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). Ubiquitination and
degradation are inhibited by insulin which blocks the effect of
fatty acids (By similarity). {ECO:0000250|UniProtKB:P16671,
ECO:0000250|UniProtKB:Q08857, ECO:0000269|PubMed:21610069}.
-!- SIMILARITY: Belongs to the CD36 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L19658; AAA02878.1; -; mRNA.
EMBL; AF072411; AAC24876.1; -; mRNA.
EMBL; AF113914; AAF25552.1; -; mRNA.
PIR; A47402; A47402.
UniGene; Rn.102418; -.
UniGene; Rn.203220; -.
UniGene; Rn.231112; -.
SMR; Q07969; -.
STRING; 10116.ENSRNOP00000058398; -.
BindingDB; Q07969; -.
ChEMBL; CHEMBL2163174; -.
iPTMnet; Q07969; -.
PhosphoSitePlus; Q07969; -.
PaxDb; Q07969; -.
PRIDE; Q07969; -.
RGD; 2301; Cd36.
eggNOG; KOG3776; Eukaryota.
eggNOG; ENOG410XS17; LUCA.
HOGENOM; HOG000252951; -.
HOVERGEN; HBG002754; -.
InParanoid; Q07969; -.
PhylomeDB; Q07969; -.
PRO; PR:Q07969; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0045177; C:apical part of cell; IDA:RGD.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0031526; C:brush border membrane; IDA:UniProtKB.
GO; GO:0005901; C:caveola; IDA:RGD.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005622; C:intracellular; IDA:RGD.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0032991; C:protein-containing complex; IDA:RGD.
GO; GO:0042383; C:sarcolemma; IDA:RGD.
GO; GO:0070538; F:oleic acid binding; IDA:RGD.
GO; GO:0070053; F:thrombospondin receptor activity; IDA:BHF-UCL.
GO; GO:0050431; F:transforming growth factor beta binding; IDA:BHF-UCL.
GO; GO:1990000; P:amyloid fibril formation; ISS:UniProtKB.
GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IEP:RGD.
GO; GO:0071726; P:cellular response to diacyl bacterial lipopeptide; ISS:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISS:UniProtKB.
GO; GO:0070508; P:cholesterol import; ISS:UniProtKB.
GO; GO:0048565; P:digestive tract development; IEP:RGD.
GO; GO:0042755; P:eating behavior; IMP:RGD.
GO; GO:0097009; P:energy homeostasis; IMP:UniProtKB.
GO; GO:0006631; P:fatty acid metabolic process; IDA:RGD.
GO; GO:0019395; P:fatty acid oxidation; IMP:RGD.
GO; GO:0015908; P:fatty acid transport; IDA:RGD.
GO; GO:0042593; P:glucose homeostasis; IMP:RGD.
GO; GO:0006955; P:immune response; IEA:InterPro.
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:0044539; P:long-chain fatty acid import; ISS:UniProtKB.
GO; GO:0001676; P:long-chain fatty acid metabolic process; IMP:RGD.
GO; GO:0015909; P:long-chain fatty acid transport; IMP:RGD.
GO; GO:0001893; P:maternal placenta development; IEP:RGD.
GO; GO:0016525; P:negative regulation of angiogenesis; IMP:RGD.
GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; IMP:RGD.
GO; GO:0050715; P:positive regulation of cytokine secretion; IMP:RGD.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
GO; GO:1900227; P:positive regulation of NLRP3 inflammasome complex assembly; ISS:UniProtKB.
GO; GO:0050766; P:positive regulation of phagocytosis; IMP:RGD.
GO; GO:0090208; P:positive regulation of triglyceride metabolic process; IDA:RGD.
GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
GO; GO:0014823; P:response to activity; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0070542; P:response to fatty acid; IDA:UniProtKB.
GO; GO:0060416; P:response to growth hormone; IEP:RGD.
GO; GO:0070543; P:response to linoleic acid; ISS:UniProtKB.
GO; GO:0033993; P:response to lipid; IMP:UniProtKB.
GO; GO:0009612; P:response to mechanical stimulus; IMP:RGD.
GO; GO:0007584; P:response to nutrient; IEP:RGD.
GO; GO:0050909; P:sensory perception of taste; ISS:UniProtKB.
GO; GO:0006641; P:triglyceride metabolic process; IMP:RGD.
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:SF12; PTHR11923:SF12; 1.
Pfam; PF01130; CD36; 1.
PRINTS; PR01610; CD36ANTIGEN.
PRINTS; PR01609; CD36FAMILY.
1: Evidence at protein level;
Cell adhesion; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Golgi apparatus; Isopeptide bond; Lipoprotein; Membrane; Palmitate;
Receptor; Reference proteome; Transmembrane; Transmembrane helix;
Transport; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:7504047,
ECO:0000269|PubMed:8320718}.
CHAIN 2 472 Platelet glycoprotein 4.
/FTId=PRO_0000144154.
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:0000250}.
REGION 460 472 Interaction with PTK2, PXN and LYN.
{ECO:0000250|UniProtKB:P16671}.
SITE 463 463 Critical for TLR4-TLR6 dimerization and
signaling.
{ECO:0000250|UniProtKB:P16671}.
LIPID 3 3 S-palmitoyl cysteine.
{ECO:0000305|PubMed:7504047}.
LIPID 7 7 S-palmitoyl cysteine.
{ECO:0000305|PubMed:7504047}.
LIPID 464 464 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 466 466 S-palmitoyl cysteine. {ECO:0000250}.
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 205 205 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
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:0000255}.
CARBOHYD 417 417 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
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:0000250|UniProtKB:P16671}.
CROSSLNK 472 472 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P16671}.
CONFLICT 67 67 I -> V (in Ref. 1; AAA02878).
{ECO:0000305}.
CONFLICT 86 86 K -> I (in Ref. 1; AAA02878).
{ECO:0000305}.
CONFLICT 215 215 F -> S (in Ref. 1; AAA02878).
{ECO:0000305}.
CONFLICT 257 258 FV -> LG (in Ref. 1; AAA02878).
{ECO:0000305}.
CONFLICT 262 262 Q -> R (in Ref. 1; AAA02878).
{ECO:0000305}.
CONFLICT 341 341 I -> N (in Ref. 1; AAA02878).
{ECO:0000305}.
CONFLICT 363 363 N -> T (in Ref. 1; AAA02878).
{ECO:0000305}.
CONFLICT 384 384 A -> S (in Ref. 1; AAA02878).
{ECO:0000305}.
SEQUENCE 472 AA; 52731 MW; 69F9513B1B85CBF0 CRC64;
MGCDRNCGLI TGAVIGAVLA VFGGILMPVG DLLIEKTIKR EVVLEEGTIA FKNWVKTGTT
VYRQFWIFDV QNPEEVAKNS SKIKVKQRGP YTYRVRYLAK ENITQDPKDS TVSFVQPNGA
IFEPSLSVGT ENDNFTVLNL AVAAAPHIYT NSFVQGVLNS LIKKSKSSMF QTRSLKELLW
GYKDPFLSLV PYPISTTVGV FYPYNNTVDG VYKVFNGKDN ISKVAIIDTY KGKRNLSYWE
SYCDMINGTD AASFPPFVEK SQTLRFFSSD ICRSIYAVFE SEVNLKGIPV YRFVLPANAF
ASPLQNPDNH CFCTEKVISN NCTSYGVLDI GKCKEGKPVY ISLPHFLHAS PDVSEPIEGL
NPNEDEHRTY LDVEPITGFT LQFAKRLQVN ILVKPARKIE ALKNLKRPYI VPILWLNETG
TIGDEKAEMF RNQVTGKIKL LGLVEMVLLG VGVVMFVAFM ISYCACRSKN GK


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