P01355 (CCKN_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cholecystokinin
Short name=CCK

Cleaved into the following 5 chains:

1. Cholecystokinin-39
   Short name=CCK39
2. Cholecystokinin-33
   Short name=CCK33
3. Cholecystokinin-22
   Short name=CCK22
4. Cholecystokinin-12
   Short name=CCK12
5. Cholecystokinin-8
   Short name=CCK8

Gene names

Name:

Cck

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	115 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Secreted
Domain	Signal
Molecular function	Hormone
PTM	Amidation Cleavage on pair of basic residues Sulfation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	activation of cysteine-type endopeptidase activity involved in apoptotic process 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 axonogenesis Inferred from sequence or structural similarity. Source: UniProtKB behavioral fear response Inferred from mutant phenotype. Source: RGD eating behavior Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of appetite Inferred from direct assay. Source: RGD neuron migration Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of apoptotic process Inferred from direct assay. Source: RGD positive regulation of cell proliferation 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 component	axon hillock Inferred from direct assay. Source: RGD dendrite Inferred from direct assay. Source: RGD extracellular space Inferred from direct assay Ref.6. 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 function	neuropeptide hormone activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	By similarity
	Propeptide	21 – 45	25			PRO_0000010565
	Chain	46 – 103	58	Cholecystokinin		PRO_0000010566
	Propeptide	47 – 63	17			PRO_0000010567
	Peptide	65 – 103	39	Cholecystokinin-39		PRO_0000010568
	Peptide	71 – 103	33	Cholecystokinin-33		PRO_0000010569
	Peptide	82 – 103	22	Cholecystokinin-22		PRO_0000010570
	Peptide	92 – 103	12	Cholecystokinin-12		PRO_0000010571
	Peptide	96 – 103	8	Cholecystokinin-8		PRO_0000010572
	Propeptide	107 – 115	9			PRO_0000010573
Sites
	Site	106 – 107	2	Cleavage
Amino acid modifications
	Modified residue	97	1	Sulfotyrosine Ref.6
	Modified residue	103	1	Phenylalanine amide
	Modified residue	111	1	Sulfotyrosine Ref.5
	Modified residue	113	1	Sulfotyrosine Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P01355 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 0A713472CAD0F3DF	FASTA	115	12,841
	10 20 30 40 50 60 MKCGVCLCVV MAVLAAGALA QPVVPVEAVD PMEQRAEEAP RRQLRAVLRP DSEPRARLGA 70 80 90 100 110 LLARYIQQVR KAPSGRMSVL KNLQGLDPSH RISDRDYMGW MDFGRRSAED YEYPS

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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X01032 mRNA. Translation: CAA25517.1. K01259 Genomic DNA. Translation: AAA40897.1. M25942 mRNA. Translation: AAA40898.1. M10353, M10352 Genomic DNA. Translation: AAB61086.1.
IPI	IPI00212646.
PIR	GMRTCP. A01624.
RefSeq	NP_036961.1. NM_012829.2.
UniGene	Rn.9781.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P01355.
Proteomic databases
PRIDE	P01355.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000026159; ENSRNOP00000026159; ENSRNOG00000019321.
GeneID	25298.
KEGG	rno:25298.
UCSC	NM_012829. rat.
Organism-specific databases
CTD	885.
RGD	2288. Cck.
Phylogenomic databases
eggNOG	maNOG20952.
GeneTree	ENSGT00390000003571.
HOVERGEN	HBG005806.
InParanoid	P01355.
OMA	LPTHHTR.
OrthoDB	EOG4Z8XXW.
PhylomeDB	P01355.
Gene expression databases
ArrayExpress	P01355.
Genevestigator	P01355.
GermOnline	ENSRNOG00000019321. Rattus norvegicus.
Family and domain databases
InterPro	IPR015499. CCK. IPR001651. Gastrin. IPR013152. Gastrin/cholecystokinin_CS. [Graphical view]
KO	K05226.
PANTHER	PTHR10786. CCK. 1 hit.
Pfam	PF00918. Gastrin. 1 hit. [Graphical view]
SMART	SM00029. GASTRIN. 1 hit. [Graphical view]
PROSITE	PS00259. GASTRIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	606067.
PMAP-CutDB	P01355.

Entry information

Entry name

CCKN_RAT

Accession

Primary (citable) accession number: P01355

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	November 16, 2011
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program