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Q07969 (CD36_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Platelet glycoprotein 4
Alternative name(s):
Adipocyte membrane protein
Fatty acid translocase
Fatty acid transport protein
Glycoprotein IIIb
Short name=GPIIIB
PAS IV
PAS-4
Platelet glycoprotein IV
Short name=GPIV
CD_antigen=CD36
Gene names
Name:Cd36
Synonyms:Fat
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length472 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Seems to have numerous potential physiological functions. Binds to collagen, thrombospondin, anionic phospholipids and oxidized LDL. May function as a cell adhesion molecule. Directly mediates cytoadherence of Plasmodium falciparum parasitized erythrocytes. Receptor for thombospondins, THBS1 AND THBS2, mediating their antiangiogenic effects By similarity. Binds long chain fatty acids and may function in the transport and/or as a regulator of fatty acid transport. Ref.5

Subunit structure

Interacts with THBS1 and THBS2; the interactions mediate the THBS antiangiogenic activity By similarity.

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Predominant in heart, intestine, spleen, fat, skeletal muscle, lower in testes.

Developmental stage

Induced during preadipocyte differentiation.

Sequence similarities

Belongs to the CD36 family.

Ontologies

Keywords
   Biological processCell adhesion
Transport
   Cellular componentMembrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to insulin stimulus

Inferred from expression pattern PubMed 19273501. Source: RGD

digestive tract development

Inferred from expression pattern PubMed 11595646. Source: RGD

fatty acid metabolic process

Inferred from direct assay PubMed 11729182. Source: RGD

fatty acid oxidation

Inferred from mutant phenotype PubMed 15161924PubMed 15331529. Source: RGD

fatty acid transport

Inferred from direct assay PubMed 14748718. Source: RGD

long-chain fatty acid metabolic process

Inferred from mutant phenotype PubMed 15161924. Source: RGD

long-chain fatty acid transport

Inferred from mutant phenotype PubMed 15848183PubMed 9315741. Source: RGD

negative regulation of angiogenesis

Inferred from mutant phenotype PubMed 18772338. Source: RGD

negative regulation of systemic arterial blood pressure

Inferred from mutant phenotype PubMed 22128087. Source: RGD

positive regulation of cytokine secretion

Inferred from mutant phenotype PubMed 20075072. Source: RGD

response to activity

Inferred from expression pattern PubMed 17374701. Source: RGD

response to drug

Inferred from expression pattern PubMed 15492479PubMed 17374701. Source: RGD

response to estradiol

Inferred from expression pattern PubMed 17640331. Source: RGD

response to growth hormone

Inferred from expression pattern PubMed 17640331. Source: RGD

response to mechanical stimulus

Inferred from mutant phenotype PubMed 18772338. Source: RGD

response to nutrient

Inferred from expression pattern PubMed 17640331. Source: RGD

signal transduction

Inferred from direct assay PubMed 10487979. Source: GOC

triglyceride metabolic process

Inferred from mutant phenotype PubMed 15331529. Source: RGD

   Cellular_componentapical part of cell

Inferred from direct assay PubMed 9315741. Source: RGD

caveola

Inferred from direct assay PubMed 12637562. Source: RGD

cell surface

Inferred from direct assay PubMed 10487979. Source: BHF-UCL

endoplasmic reticulum

Inferred from direct assay PubMed 20237389. Source: RGD

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular

Inferred from direct assay PubMed 15848183. Source: RGD

intracellular membrane-bounded organelle

Inferred from direct assay PubMed 12829625. Source: RGD

mitochondrion

Inferred from direct assay PubMed 15161924. Source: RGD

plasma membrane

Inferred from direct assay PubMed 11729182PubMed 15161924PubMed 15848183. Source: RGD

protein complex

Inferred from direct assay PubMed 20237389. Source: RGD

sarcolemma

Inferred from direct assay PubMed 12829625. Source: RGD

   Molecular_functionoleic acid binding

Inferred from direct assay Ref.5. Source: RGD

thrombospondin receptor activity

Inferred from direct assay PubMed 10487979. Source: BHF-UCL

transforming growth factor beta binding

Inferred from direct assay PubMed 10487979. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4 Ref.5
Chain2 – 472471Platelet glycoprotein 4
PRO_0000144154

Regions

Topological domain2 – 76Cytoplasmic Potential
Transmembrane8 – 2922Helical; Potential
Topological domain30 – 439410Extracellular Potential
Transmembrane440 – 46122Helical; Potential
Topological domain462 – 47211Cytoplasmic Potential
Region93 – 12028Required for interaction with thrombospondins, THBS1 and THBS2 By similarity

Amino acid modifications

Lipidation31S-palmitoyl cysteine Probable
Lipidation71S-palmitoyl cysteine Probable
Lipidation4641S-palmitoyl cysteine By similarity
Lipidation4661S-palmitoyl cysteine By similarity
Glycosylation791N-linked (GlcNAc...) Potential
Glycosylation1021N-linked (GlcNAc...) Potential
Glycosylation1341N-linked (GlcNAc...) Potential
Glycosylation2051N-linked (GlcNAc...) Potential
Glycosylation2201N-linked (GlcNAc...) Potential
Glycosylation2351N-linked (GlcNAc...) Potential
Glycosylation2471N-linked (GlcNAc...) Potential
Glycosylation3211N-linked (GlcNAc...) Potential
Glycosylation4171N-linked (GlcNAc...) Potential
Disulfide bond243 ↔ 311 By similarity
Disulfide bond272 ↔ 333 By similarity
Disulfide bond313 ↔ 322 By similarity

Experimental info

Sequence conflict671I → V in AAA02878. Ref.1
Sequence conflict861K → I in AAA02878. Ref.1
Sequence conflict2151F → S in AAA02878. Ref.1
Sequence conflict257 – 2582FV → LG in AAA02878. Ref.1
Sequence conflict2621Q → R in AAA02878. Ref.1
Sequence conflict3411I → N in AAA02878. Ref.1
Sequence conflict3631N → T in AAA02878. Ref.1
Sequence conflict3841A → S in AAA02878. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q07969 [UniParc].

Last modified May 1, 2007. Version 3.
Checksum: 69F9513B1B85CBF0

FASTA47252,731
        10         20         30         40         50         60 
MGCDRNCGLI TGAVIGAVLA VFGGILMPVG DLLIEKTIKR EVVLEEGTIA FKNWVKTGTT 

        70         80         90        100        110        120 
VYRQFWIFDV QNPEEVAKNS SKIKVKQRGP YTYRVRYLAK ENITQDPKDS TVSFVQPNGA 

       130        140        150        160        170        180 
IFEPSLSVGT ENDNFTVLNL AVAAAPHIYT NSFVQGVLNS LIKKSKSSMF QTRSLKELLW 

       190        200        210        220        230        240 
GYKDPFLSLV PYPISTTVGV FYPYNNTVDG VYKVFNGKDN ISKVAIIDTY KGKRNLSYWE 

       250        260        270        280        290        300 
SYCDMINGTD AASFPPFVEK SQTLRFFSSD ICRSIYAVFE SEVNLKGIPV YRFVLPANAF 

       310        320        330        340        350        360 
ASPLQNPDNH CFCTEKVISN NCTSYGVLDI GKCKEGKPVY ISLPHFLHAS PDVSEPIEGL 

       370        380        390        400        410        420 
NPNEDEHRTY LDVEPITGFT LQFAKRLQVN ILVKPARKIE ALKNLKRPYI VPILWLNETG 

       430        440        450        460        470 
TIGDEKAEMF RNQVTGKIKL LGLVEMVLLG VGVVMFVAFM ISYCACRSKN GK 

« Hide

References

[1]"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."
Abumrad N.A., El-Maghrabi M.R., Amri E.-Z., Lopez E., Grimaldi P.A.
J. Biol. Chem. 268:17665-17668(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Adipocyte.
[2]"Fatty acid translocase/CD36 mediates the uptake of palmitate by type II pneumocytes."
Guthmann F., Haupt R., Looman A.C., Spener F., Ruestow B.
Am. J. Physiol. 277:L191-L196(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
[3]"Potential allele of rat CD36 antigen."
Zhang X., Mayrhofer G., Ey P.L.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Dark agouti.
[4]"Purification of the major substrate for palmitoylation in rat adipocytes: N-terminal homology with CD36 and evidence for cell surface acylation."
Jochen A., Hays J.
J. Lipid Res. 34:1783-1792(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-31, PALMITOYLATION AT CYS-3 AND CYS-7.
Tissue: Adipocyte.
[5]"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."
Harmon C.M., Abumrad N.A.
J. Membr. Biol. 133:43-49(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-16, FUNCTION.
Strain: Sprague-Dawley.
Tissue: Adipocyte.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L19658 mRNA. Translation: AAA02878.1.
AF072411 mRNA. Translation: AAC24876.1.
AF113914 mRNA. Translation: AAF25552.1.
PIRA47402.
UniGeneRn.102418.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4997133.

Chemistry

ChEMBLCHEMBL2163174.

Proteomic databases

PaxDbQ07969.
PRIDEQ07969.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

RGD2301. Cd36.

Phylogenomic databases

eggNOGNOG257244.
HOGENOMHOG000252951.
HOVERGENHBG002754.
InParanoidQ07969.
PhylomeDBQ07969.

Gene expression databases

GenevestigatorQ07969.

Family and domain databases

InterProIPR002159. CD36.
IPR005428. CD36_antigen.
[Graphical view]
PANTHERPTHR11923. PTHR11923. 1 hit.
PfamPF01130. CD36. 1 hit.
[Graphical view]
PRINTSPR01610. CD36ANTIGEN.
PR01609. CD36FAMILY.
ProtoNetSearch...

Entry information

Entry nameCD36_RAT
AccessionPrimary (citable) accession number: Q07969
Secondary accession number(s): Q925W0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: May 1, 2007
Last modified: April 16, 2014
This is version 104 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families