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Reviewed, UniProtKB/Swiss-Prot P01355 (CCKN_RAT)

Last modified May 26, 2009. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cholecystokinin
      Short name=CCK
Cleaved into the following 5 chains:
    1- Recommended name:
            Cholecystokinin-39
                Short name=CCK39
    2- Recommended name:
            Cholecystokinin-33
                Short name=CCK33
    3- Recommended name:
            Cholecystokinin-22
                Short name=CCK22
    4- Recommended name:
            Cholecystokinin-12
                Short name=CCK12
    5- Recommended name:
            Cholecystokinin-8
                Short name=CCK8
Gene names
Name: Cck
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length115 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

This peptide hormone induces gall bladder contraction and the release of pancreatic enzymes in the gut. Its function in the brain is not clear. Binding to CCK-A receptors stimulates amylase release from the pancreas, binding to CCK-B receptors stimulates gastric acid secretion.

Subunit structure

Binds to CCK-A receptors in the pancreas and CCK-B receptors in the brain By similarity.

Subcellular location

Secreted.

Tissue specificity

The shortest form (CCK8) is predominantly found in the brain, whereas the larger ones are found in the intestine.

Post-translational modification

The precursor is cleaved by proteases to produce a number of active cholecystokinins.

Sulfation of Tyr-97 is essential for receptor activation.

Sequence similarities

Belongs to the gastrin/cholecystokinin family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionHormone
   PTMAmidation
Cleavage on pair of basic residues
Sulfation
Gene Ontology (GO)
   Biological processactivation of caspase activity

Inferred from direct assay. Source: RGD

activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway

Inferred from direct assay. Source: RGD

behavioral fear response

Inferred from mutant phenotype. Source: RGD

eating behavior

Inferred from direct assay. Source: RGD

negative regulation of appetite

Inferred from direct assay. Source: RGD

positive regulation of apoptosis

Inferred from direct assay. Source: RGD

positive regulation of mitochondrial depolarization

Inferred from direct assay. Source: RGD

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from direct assay. Source: RGD

positive regulation of protein oligomerization

Inferred from direct assay. Source: RGD

regulation of sensory perception of pain

Inferred from direct assay. Source: RGD

release of cytochrome c from mitochondria

Inferred from direct assay. Source: RGD

   Cellular componentaxon hillock

Inferred from direct assay. Source: RGD

dendrite

Inferred from direct assay. Source: RGD

extracellular space Ref.6

Inferred from direct assay. Source: RGD

initial segment

Inferred from direct assay. Source: RGD

perikaryon

Inferred from direct assay. Source: RGD

terminal button

Inferred from direct assay. Source: RGD

   Molecular functionneuropeptide hormone activity

Inferred from direct assay. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 By similarity
Propeptide21 – 4525
PRO_0000010565
Chain46 – 10358Cholecystokinin
PRO_0000010566
Propeptide47 – 6317
PRO_0000010567
Peptide65 – 10339Cholecystokinin-39
PRO_0000010568
Peptide71 – 10333Cholecystokinin-33
PRO_0000010569
Peptide82 – 10322Cholecystokinin-22
PRO_0000010570
Peptide92 – 10312Cholecystokinin-12
PRO_0000010571
Peptide96 – 1038Cholecystokinin-8
PRO_0000010572
Propeptide107 – 1159
PRO_0000010573

Sites

Site106 – 1072Cleavage

Amino acid modifications

Modified residue971Sulfotyrosine
Modified residue1031Phenylalanine amide
Modified residue1111Sulfotyrosine
Modified residue1131Sulfotyrosine

Sequences

Sequence LengthMass (Da)Tools
P01355-1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 0A713472CAD0F3DF

FASTA11512,841
        10         20         30         40         50         60 
MKCGVCLCVV MAVLAAGALA QPVVPVEAVD PMEQRAEEAP RRQLRAVLRP DSEPRARLGA 

        70         80         90        100        110 
LLARYIQQVR KAPSGRMSVL KNLQGLDPSH RISDRDYMGW MDFGRRSAED YEYPS 

« Hide

References

[1]"Molecular cloning and nucleotide sequence of cDNA coding for rat brain cholecystokinin precursor."
Kuwano R., Araki K., Usui H., Fukui T., Ohtsuka E., Ikehara M., Takahashi Y.
J. Biochem. 96:923-926(1984) [PubMed: 6209267] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning and sequence analysis of a cDNA encoding rat preprocholecystokinin."
Deschenes R.J., Lorenz L.J., Haun R.S., Roos B.A., Collier K.J., Dixon J.E.
Proc. Natl. Acad. Sci. U.S.A. 81:726-730(1984) [PubMed: 6199787] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Modulation of cholecystokinin gene expression."
Deschenes R.J., Haun R.S., Sunkel D., Roos B.A., Dixon J.E.
Ann. N. Y. Acad. Sci. 448:53-60(1985) [PubMed: 3861130] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"A gene encoding rat cholecystokinin. Isolation, nucleotide sequence, and promoter activity."
Deschenes R.J., Haun R.S., Funckes C.L., Dixon J.E.
J. Biol. Chem. 260:1280-1286(1985) [PubMed: 2981840] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Isolation, structure and properties of the C-terminal fragment of the rat cholecystokinin precursor."
Varro A., Young J., Gregory H., Csech J., Dockray G.J.
Regul. Pept. 15:195-195(1986)
Cited for: SULFATION AT TYR-111 AND TYR-113.
[6]"Inhibition of pro-cholecystokinin (CCK) sulfation by treatment with sodium chlorate alters its processing and decreases cellular content and secretion of CCK 8."
Beinfeld M.C.
Neuropeptides 26:195-200(1994) [PubMed: 8208365] [Abstract]
Cited for: SULFATION AT TYR-97.
[7]"Biosynthesis and processing of pro CCK: recent progress and future challenges."
Beinfeld M.C.
Life Sci. 72:747-757(2003) [PubMed: 12479974] [Abstract]
Cited for: REVIEW.

Cross-references

Sequence databases

X01032 mRNA. Translation: CAA25517.1.
K01259 Genomic DNA. Translation: AAA40897.1.
M25942 mRNA. Translation: AAA40898.1.
M10353, M10352 Genomic DNA. Translation: AAB61086.1.
IPIIPI00212646.
PIRGMRTCP. A01624.
RefSeqNP_036961.1.
UniGeneRn.9781

3D structure databases

ModBaseSearch...

Genome annotation databases

EnsemblENSRNOG00000019321. Rattus norvegicus. [Contig view]
GeneID25298.
KEGGrno:25298.

Organism-specific databases

RGD2288. Cck.

Phylogenomic databases

HOVERGENP01355.
OMAP01355. PSHRISD.

Gene expression databases

ArrayExpressP01355.
GermOnlineENSRNOG00000019321. Rattus norvegicus.

Family and domain databases

InterProIPR015499. CCK.
IPR001651. Gastrin.
IPR013152. Gastrin/cholecystokinin_CS.
[Graphical view]
PANTHERPTHR10786. CCK. 1 hit.
PfamPF00918. Gastrin. 1 hit.
[Graphical view]
SMARTSM00029. GASTRIN. 1 hit.
[Graphical view]
PROSITEPS00259. GASTRIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio606067.
PMAP-CutDBP01355.

Entry information

Entry nameCCKN_RAT
AccessionPrimary (citable) accession number: P01355
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 26, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents