CCKN_PIG
ID CCKN_PIG Reviewed; 114 AA.
AC P01356;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-1986, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Cholecystokinin;
DE Short=CCK;
DE Contains:
DE RecName: Full=Cholecystokinin-58;
DE Short=CCK58;
DE Contains:
DE RecName: Full=Cholecystokinin-58 desnonopeptide;
DE AltName: Full=(1-49)-CCK58;
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-25;
DE Short=CCK25;
DE Contains:
DE RecName: Full=Cholecystokinin-18;
DE Short=CCK18;
DE Contains:
DE RecName: Full=Cholecystokinin-12;
DE Short=CCK12;
DE Contains:
DE RecName: Full=Cholecystokinin-8;
DE Short=CCK8;
DE Contains:
DE RecName: Full=Cholecystokinin-7;
DE Short=CCK7;
DE Contains:
DE RecName: Full=Cholecystokinin-5;
DE Short=CCK5;
DE Flags: Precursor;
GN Name=CCK;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=6205394; DOI=10.1073/pnas.81.14.4307;
RA Gubler U., Chua A.O., Hoffman B.J., Collier K.J., Eng J.;
RT "Cloned cDNA to cholecystokinin mRNA predicts an identical
RT preprocholecystokinin in pig brain and gut.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:4307-4310(1984).
RN [2]
RP PROTEIN SEQUENCE OF 70-102.
RA Mutt V., Jorpes J.E.;
RL Submitted (AUG-1970) to the PIR data bank.
RN [3]
RP PROTEIN SEQUENCE OF 91-102, SULFATION AT TYR-96, AND AMIDATION AT PHE-102.
RX PubMed=5410106; DOI=10.1021/ja00704a033;
RA Ondetti M.A., Pluscec J., Sabo E.F., Sheehan J.T., Williams N.;
RT "Synthesis of cholecystokinin-pancreozymin. I. The C-terminal
RT dodecapeptide.";
RL J. Am. Chem. Soc. 92:195-199(1970).
RN [4]
RP SULFATION AT TYR-96; TYR-110 AND TYR-112.
RX PubMed=8443599; DOI=10.1002/pro.5560020210;
RA Rosenquist G.L., Nicholas H.B.;
RT "Analysis of sequence requirements for protein tyrosine sulfation.";
RL Protein Sci. 2:215-222(1993).
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:0000250|UniProtKB:Q9TS44}.
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:0000305|PubMed:5410106}.
CC -!- TISSUE SPECIFICITY: Synthesized in both cerebral cortex and duodenal
CC mucosa. {ECO:0000269|PubMed:6205394}.
CC -!- PTM: The precursor is cleaved by proteases to produce a number of
CC active cholecystokinins. Brain contains CCK-octapeptide (CCK8) and
CC several CCK-desoctapeptides; whereas pig gut contains intact CCK33,
CC CCK39, and CCK58 as well as CCK-octapeptide and the CCK-
CC desoctapeptides. Distribution differences are due to tissue-specific
CC post-translational processing events.
CC -!- PTM: [Cholecystokinin-5]: The precursor is cleaved by ACE, which
CC removes the Gly-Arg-Arg peptide at the C-terminus, leading to mature
CC hormone. {ECO:0000250|UniProtKB:P06307}.
CC -!- SIMILARITY: Belongs to the gastrin/cholecystokinin family.
CC {ECO:0000305}.
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DR EMBL; K01940; AAA31014.1; -; mRNA.
DR PIR; A05084; GMPGCP.
DR RefSeq; NP_999402.1; NM_214237.2.
DR AlphaFoldDB; P01356; -.
DR STRING; 9823.ENSSSCP00000012023; -.
DR BindingDB; P01356; -.
DR PaxDb; P01356; -.
DR Ensembl; ENSSSCT00015062271; ENSSSCP00015024987; ENSSSCG00015046493.
DR Ensembl; ENSSSCT00070019436; ENSSSCP00070016171; ENSSSCG00070010008.
DR GeneID; 397468; -.
DR KEGG; ssc:397468; -.
DR CTD; 885; -.
DR eggNOG; ENOG502S472; Eukaryota.
DR HOGENOM; CLU_169783_0_0_1; -.
DR InParanoid; P01356; -.
DR OrthoDB; 1524113at2759; -.
DR TreeFam; TF333419; -.
DR Reactome; R-SSC-375276; Peptide ligand-binding receptors.
DR Reactome; R-SSC-416476; G alpha (q) signalling events.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 13.
DR Genevisible; P01356; SS.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005184; F:neuropeptide hormone activity; ISS:UniProtKB.
DR GO; GO:0051428; F:peptide hormone receptor binding; IEA:Ensembl.
DR GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR GO; GO:0007586; P:digestion; IBA:GO_Central.
DR GO; GO:0042755; P:eating behavior; ISS:UniProtKB.
DR GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
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; Direct protein sequencing;
KW Hormone; Reference proteome; Secreted; Signal; Sulfation.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..114
FT /note="Cholecystokinin"
FT /id="PRO_0000010558"
FT PEPTIDE 45..102
FT /note="Cholecystokinin-58"
FT /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT /id="PRO_0000010559"
FT PEPTIDE 46..94
FT /note="Cholecystokinin-58 desnonopeptide"
FT /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT /id="PRO_0000306314"
FT PEPTIDE 64..102
FT /note="Cholecystokinin-39"
FT /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT /id="PRO_0000010560"
FT PEPTIDE 70..102
FT /note="Cholecystokinin-33"
FT /evidence="ECO:0000269|Ref.2"
FT /id="PRO_0000010561"
FT PEPTIDE 79..103
FT /note="Cholecystokinin-25"
FT /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT /id="PRO_0000306315"
FT PEPTIDE 86..103
FT /note="Cholecystokinin-18"
FT /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT /id="PRO_0000306316"
FT PEPTIDE 91..102
FT /note="Cholecystokinin-12"
FT /evidence="ECO:0000269|PubMed:5410106"
FT /id="PRO_0000010562"
FT PEPTIDE 95..102
FT /note="Cholecystokinin-8"
FT /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT /id="PRO_0000010563"
FT PEPTIDE 97..103
FT /note="Cholecystokinin-7"
FT /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT /id="PRO_0000306317"
FT PEPTIDE 99..103
FT /note="Cholecystokinin-5"
FT /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT /id="PRO_0000306318"
FT PROPEP 106..114
FT /id="PRO_0000010564"
FT MOD_RES 96
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:5410106,
FT ECO:0000269|PubMed:8443599"
FT MOD_RES 102
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:5410106"
FT MOD_RES 110
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:8443599"
FT MOD_RES 112
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:8443599"
SQ SEQUENCE 114 AA; 12526 MW; 8F8C05DF29B0E6EE CRC64;
MNGGLCLCVL MAVLAAGTLA QPVPPADSAV PGAQEEEAHR RQLRAVQKVD GESRAHLGAL
LARYIQQARK APSGRVSMIK NLQSLDPSHR ISDRDYMGWM DFGRRSAEEY EYTS
