CCKN_RAT
ID CCKN_RAT Reviewed; 115 AA.
AC P01355;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Cholecystokinin;
DE Short=CCK;
DE Contains:
DE RecName: Full=Cholecystokinin-39;
DE Short=CCK39;
DE Contains:
DE RecName: Full=Cholecystokinin-33;
DE Short=CCK33;
DE Contains:
DE RecName: Full=Cholecystokinin-22;
DE Short=CCK22;
DE Contains:
DE RecName: Full=Cholecystokinin-12;
DE Short=CCK12;
DE Contains:
DE RecName: Full=Cholecystokinin-8;
DE Short=CCK8;
DE Flags: Precursor;
GN Name=Cck;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6209267; DOI=10.1093/oxfordjournals.jbchem.a134911;
RA Kuwano R., Araki K., Usui H., Fukui T., Ohtsuka E., Ikehara M.,
RA Takahashi Y.;
RT "Molecular cloning and nucleotide sequence of cDNA coding for rat brain
RT cholecystokinin precursor.";
RL J. Biochem. 96:923-926(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=6199787; DOI=10.1073/pnas.81.3.726;
RA Deschenes R.J., Lorenz L.J., Haun R.S., Roos B.A., Collier K.J.,
RA Dixon J.E.;
RT "Cloning and sequence analysis of a cDNA encoding rat
RT preprocholecystokinin.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:726-730(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3861130; DOI=10.1111/j.1749-6632.1985.tb29906.x;
RA Deschenes R.J., Haun R.S., Sunkel D., Roos B.A., Dixon J.E.;
RT "Modulation of cholecystokinin gene expression.";
RL Ann. N. Y. Acad. Sci. 448:53-60(1985).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2981840; DOI=10.1016/s0021-9258(20)71240-8;
RA Deschenes R.J., Haun R.S., Funckes C.L., Dixon J.E.;
RT "A gene encoding rat cholecystokinin. Isolation, nucleotide sequence, and
RT promoter activity.";
RL J. Biol. Chem. 260:1280-1286(1985).
RN [5]
RP SULFATION AT TYR-111 AND TYR-113.
RA Varro A., Young J., Gregory H., Csech J., Dockray G.J.;
RT "Isolation, structure and properties of the C-terminal fragment of the rat
RT cholecystokinin precursor.";
RL Regul. Pept. 15:195-195(1986).
RN [6]
RP SULFATION AT TYR-97.
RX PubMed=8208365; DOI=10.1016/0143-4179(94)90130-9;
RA Beinfeld M.C.;
RT "Inhibition of pro-cholecystokinin (CCK) sulfation by treatment with sodium
RT chlorate alters its processing and decreases cellular content and secretion
RT of CCK 8.";
RL Neuropeptides 26:195-200(1994).
RN [7]
RP REVIEW.
RX PubMed=12479974; DOI=10.1016/s0024-3205(02)02330-5;
RA Beinfeld M.C.;
RT "Biosynthesis and processing of pro CCK: recent progress and future
RT challenges.";
RL Life Sci. 72:747-757(2003).
CC -!- FUNCTION: This peptide hormone induces gall bladder contraction and the
CC release of pancreatic enzymes in the gut. Its function in the brain is
CC not clear. Binding to CCK-A receptors stimulates amylase release from
CC the pancreas, binding to CCK-B receptors stimulates gastric acid
CC secretion. {ECO:0000303|PubMed:12479974}.
CC -!- SUBUNIT: Binds to CCK-A receptors in the pancreas and CCK-B receptors
CC in the brain. {ECO:0000250|UniProtKB:Q9TS44}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P09240}.
CC -!- TISSUE SPECIFICITY: The shortest form (CCK8) is predominantly found in
CC the brain, whereas the larger ones are found in the intestine.
CC {ECO:0000269|PubMed:6199787}.
CC -!- PTM: The precursor is cleaved by proteases to produce a number of
CC active cholecystokinins.
CC -!- PTM: Sulfation of Tyr-97 is essential for receptor activation.
CC {ECO:0000269|PubMed:8208365, ECO:0000269|Ref.5}.
CC -!- SIMILARITY: Belongs to the gastrin/cholecystokinin family.
CC {ECO:0000305}.
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DR EMBL; X01032; CAA25517.1; -; mRNA.
DR EMBL; K01259; AAA40897.1; -; Genomic_DNA.
DR EMBL; M25942; AAA40898.1; -; mRNA.
DR EMBL; M10353; AAB61086.1; -; Genomic_DNA.
DR EMBL; M10352; AAB61086.1; JOINED; Genomic_DNA.
DR PIR; A01624; GMRTCP.
DR RefSeq; NP_036961.1; NM_012829.2.
DR AlphaFoldDB; P01355; -.
DR STRING; 10116.ENSRNOP00000026159; -.
DR BindingDB; P01355; -.
DR PaxDb; P01355; -.
DR Ensembl; ENSRNOT00000026159; ENSRNOP00000026159; ENSRNOG00000019321.
DR GeneID; 25298; -.
DR KEGG; rno:25298; -.
DR UCSC; RGD:2288; rat.
DR CTD; 885; -.
DR RGD; 2288; Cck.
DR eggNOG; ENOG502S472; Eukaryota.
DR GeneTree; ENSGT00390000003571; -.
DR HOGENOM; CLU_169783_0_0_1; -.
DR InParanoid; P01355; -.
DR OMA; YSGLCIC; -.
DR OrthoDB; 1524113at2759; -.
DR PhylomeDB; P01355; -.
DR TreeFam; TF333419; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR PRO; PR:P01355; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000019321; Expressed in frontal cortex and 17 other tissues.
DR Genevisible; P01355; RN.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0043203; C:axon hillock; IDA:RGD.
DR GO; GO:0043194; C:axon initial segment; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0005576; C:extracellular region; NAS:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR GO; GO:0005179; F:hormone activity; IDA:RGD.
DR GO; GO:0005184; F:neuropeptide hormone activity; IDA:RGD.
DR GO; GO:0051428; F:peptide hormone receptor binding; ISO:RGD.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:RGD.
DR GO; GO:0006915; P:apoptotic process; IDA:RGD.
DR GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR GO; GO:0007586; P:digestion; IBA:GO_Central.
DR GO; GO:0042755; P:eating behavior; IDA:RGD.
DR GO; GO:0007613; P:memory; IMP:RGD.
DR GO; GO:0032099; P:negative regulation of appetite; IDA:RGD.
DR GO; GO:2000986; P:negative regulation of behavioral fear response; IMP:RGD.
DR GO; GO:1903999; P:negative regulation of eating behavior; IDA:RGD.
DR GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:RGD.
DR GO; GO:2000987; P:positive regulation of behavioral fear response; IDA:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:RGD.
DR GO; GO:0014049; P:positive regulation of glutamate secretion; IDA:CACAO.
DR GO; GO:0051901; P:positive regulation of mitochondrial depolarization; IDA:RGD.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:RGD.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IDA:RGD.
DR GO; GO:1904058; P:positive regulation of sensory perception of pain; IDA:RGD.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IDA:RGD.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IDA:RGD.
DR GO; GO:0001836; P:release of cytochrome c from mitochondria; IDA:RGD.
DR GO; GO:0008542; P:visual learning; IMP:RGD.
DR InterPro; IPR015499; CCK-like.
DR InterPro; IPR001651; Gastrin/CCK.
DR InterPro; IPR013152; Gastrin/cholecystokinin_CS.
DR PANTHER; PTHR10786; PTHR10786; 1.
DR Pfam; PF00918; Gastrin; 1.
DR PROSITE; PS00259; GASTRIN; 1.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Hormone; Reference proteome;
KW Secreted; Signal; Sulfation.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..45
FT /id="PRO_0000010565"
FT CHAIN 46..103
FT /note="Cholecystokinin"
FT /id="PRO_0000010566"
FT PROPEP 47..63
FT /id="PRO_0000010567"
FT PEPTIDE 65..103
FT /note="Cholecystokinin-39"
FT /id="PRO_0000010568"
FT PEPTIDE 71..103
FT /note="Cholecystokinin-33"
FT /id="PRO_0000010569"
FT PEPTIDE 82..103
FT /note="Cholecystokinin-22"
FT /id="PRO_0000010570"
FT PEPTIDE 92..103
FT /note="Cholecystokinin-12"
FT /id="PRO_0000010571"
FT PEPTIDE 96..103
FT /note="Cholecystokinin-8"
FT /id="PRO_0000010572"
FT PROPEP 107..115
FT /id="PRO_0000010573"
FT SITE 106..107
FT /note="Cleavage"
FT MOD_RES 97
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:8208365"
FT MOD_RES 103
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250|UniProtKB:P06307"
FT MOD_RES 111
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|Ref.5"
FT MOD_RES 113
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|Ref.5"
SQ SEQUENCE 115 AA; 12841 MW; 0A713472CAD0F3DF CRC64;
MKCGVCLCVV MAVLAAGALA QPVVPVEAVD PMEQRAEEAP RRQLRAVLRP DSEPRARLGA
LLARYIQQVR KAPSGRMSVL KNLQGLDPSH RISDRDYMGW MDFGRRSAED YEYPS
