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P30551 (CCKAR_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Cholecystokinin receptor type A

Short name=CCK-A receptor
Short name=CCK-AR
Alternative name(s):
Cholecystokinin-1 receptor
Short name=CCK1-R
Gene names
Name:Cckar
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length444 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for cholecystokinin. Mediates pancreatic growth and enzyme secretion, smooth muscle contraction of the gall bladder and stomach. Has a 1000-fold higher affinity for CCK rather than for gastrin. It modulates feeding and dopamine-induced behavior in the central and peripheral nervous system. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Ref.2

Subcellular location

Cell membrane; Multi-pass membrane protein.

Tissue specificity

Pancreas and brain. Also expressed in the gastrointestinal system and vagus nerve. Ref.2

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton reorganization

Inferred from direct assay PubMed 11891013. Source: RGD

cellular response to hormone stimulus

Inferred from expression pattern PubMed 12649564. Source: RGD

elevation of cytosolic calcium ion concentration

Inferred from direct assay PubMed 18776046. Source: RGD

gastric acid secretion

Inferred from direct assay PubMed 9773935. Source: RGD

insulin secretion

Inferred from direct assay PubMed 9773935. Source: RGD

organ regeneration

Inferred from expression pattern PubMed 10403848. Source: RGD

pancreas development

Inferred from expression pattern PubMed 10403848. Source: RGD

pancreatic juice secretion

Inferred from mutant phenotype PubMed 16327284. Source: RGD

positive regulation of somatostatin secretion

Inferred from mutant phenotype PubMed 19959964. Source: RGD

reduction of food intake in response to dietary excess

Inferred from mutant phenotype PubMed 12840200. Source: RGD

regulation of calcium ion transport

Inferred from direct assay PubMed 11207382. Source: RGD

regulation of potassium ion transport

Inferred from direct assay PubMed 12427859. Source: RGD

response to glucocorticoid stimulus

Inferred from expression pattern PubMed 7977738. Source: RGD

response to heat

Inferred from mutant phenotype PubMed 16891771. Source: RGD

response to lipopolysaccharide

Inferred from expression pattern PubMed 17622698. Source: RGD

response to nutrient

Inferred from expression pattern PubMed 15127944. Source: RGD

response to radiation

Inferred from expression pattern PubMed 16472889. Source: RGD

response to starvation

Inferred from mutant phenotype PubMed 12954406. Source: RGD

temperature homeostasis

Inferred from mutant phenotype PubMed 15178543. Source: RGD

   Cellular_componentendoplasmic reticulum

Inferred from direct assay PubMed 9169450. Source: RGD

endosome

Inferred from direct assay PubMed 9169450. Source: RGD

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

lysosome

Inferred from direct assay PubMed 9169450. Source: RGD

plasma membrane

Inferred from direct assay PubMed 10535877. Source: RGD

terminal bouton

Inferred from direct assay PubMed 3408996. Source: RGD

   Molecular_functioncholecystokinin receptor activity

Inferred from direct assay PubMed 18776046. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 444444Cholecystokinin receptor type A
PRO_0000069226

Regions

Topological domain1 – 5656Extracellular Potential
Transmembrane57 – 8226Helical; Name=1; Potential
Topological domain83 – 9210Cytoplasmic Potential
Transmembrane93 – 11927Helical; Name=2; Potential
Topological domain120 – 13011Extracellular Potential
Transmembrane131 – 15222Helical; Name=3; Potential
Topological domain153 – 17220Cytoplasmic Potential
Transmembrane173 – 19321Helical; Name=4; Potential
Topological domain194 – 22532Extracellular Potential
Transmembrane226 – 24924Helical; Name=5; Potential
Topological domain250 – 32980Cytoplasmic Potential
Transmembrane330 – 35021Helical; Name=6; Potential
Topological domain351 – 36515Extracellular Potential
Transmembrane366 – 38924Helical; Name=7; Potential
Topological domain390 – 44455Cytoplasmic Potential

Amino acid modifications

Lipidation4031S-palmitoyl cysteine By similarity
Glycosylation251N-linked (GlcNAc...) Potential
Glycosylation391N-linked (GlcNAc...) Potential
Glycosylation2051N-linked (GlcNAc...) Potential
Disulfide bond33 ↔ 44 Ref.3
Disulfide bond129 ↔ 211 By similarity

Sequences

Sequence LengthMass (Da)Tools
P30551 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: B435BE7505C2FB11

FASTA44449,657
        10         20         30         40         50         60 
MSHSPARQHL VESSRMDVVD SLLMNGSNIT PPCELGLENE TLFCLDQPQP SKEWQSALQI 

        70         80         90        100        110        120 
LLYSIIFLLS VLGNTLVITV LIRNKRMRTV TNIFLLSLAV SDLMLCLFCM PFNLIPNLLK 

       130        140        150        160        170        180 
DFIFGSAVCK TTTYFMGTSV SVSTFNLVAI SLERYGAICR PLQSRVWQTK SHALKVIAAT 

       190        200        210        220        230        240 
WCLSFTIMTP YPIYSNLVPF TKNNNQTANM CRFLLPSDAM QQSWQTFLLL ILFLLPGIVM 

       250        260        270        280        290        300 
VVAYGLISLE LYQGIKFDAS QKKSAKEKKP STGSSTRYED SDGCYLQKSR PPRKLELQQL 

       310        320        330        340        350        360 
SSGSGGSRLN RIRSSSSAAN LIAKKRVIRM LIVIVVLFFL CWMPIFSANA WRAYDTVSAE 

       370        380        390        400        410        420 
KHLSGTPISF ILLLSYTSSC VNPIIYCFMN KRFRLGFMAT FPCCPNPGPP GVRGEVGEEE 

       430        440 
DGRTIRALLS RYSYSHMSTS APPP 

« Hide

References

[1]"Purification, molecular cloning, and functional expression of the cholecystokinin receptor from rat pancreas."
Wank S.A., Harkins R., Jensen R.T., Shapira H., de Weerth A., Slattery T.
Proc. Natl. Acad. Sci. U.S.A. 89:3125-3129(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 111-158; 270-314 AND 392-402.
Tissue: Pancreas.
[2]"Gene structure of rat cholecystokinin type-A receptor."
Takata Y., Takiguchi S., Funakoshi A., Kono A.
Biochem. Biophys. Res. Commun. 213:958-966(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, FUNCTION.
[3]"Disulfide bond structure and accessibility of cysteines in the ectodomain of the cholecystokinin receptor: specific mono-reactive receptor constructs examine charge-sensitivity of loop regions."
Ding X.Q., Dolu V., Hadac E.M., Schuetz M., Miller L.J.
Recept. Channels 9:83-91(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS.
[4]"The seventh transmembrane domain of gastrin/CCK receptors contributes to non-peptide antagonist binding."
Mantamadiotis T., Baldwin G.S.
Biochem. Biophys. Res. Commun. 201:1382-1389(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: ANTAGONIST BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M88096 mRNA. Translation: AAA40899.1.
D50608 Genomic DNA. Translation: BAA09170.1.
IPIIPI00210085.
PIRA42685.
RefSeqNP_036820.1. NM_012688.3.
UniGeneRn.10184.

3D structure databases

ProteinModelPortalP30551.
SMRP30551. Positions 16-62, 345-373.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000063137.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP30551.

Proteomic databases

PRIDEP30551.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID24889.
KEGGrno:24889.

Organism-specific databases

CTD886.
RGD2289. Cckar.

Phylogenomic databases

eggNOGNOG238659.
HOGENOMHOG000198281.
HOVERGENHBG036927.
KOK04194.
OrthoDBEOG43N7D1.

Gene expression databases

ArrayExpressP30551.
GenevestigatorP30551.

Family and domain databases

Gene3D4.10.670.10. 1 hit.
InterProIPR009126. Cholcskin_rcpt.
IPR000596. Cholcy_rcpt_A.
IPR015276. CholecystokininA_recpt_N.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PfamPF00001. 7tm_1. 1 hit.
PF09193. CholecysA-Rec_N. 1 hit.
[Graphical view]
PRINTSPR01822. CCYSTOKININR.
PR00524. CCYSTOKNINAR.
PR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP30551.
ChEMBLCHEMBL2871.
NextBio604752.
PMAP-CutDBP30551.

Entry information

Entry nameCCKAR_RAT
AccessionPrimary (citable) accession number: P30551
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: April 3, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries

SIMILARITY comments

Index of protein domains and families