ID   CCKN_LITCT              Reviewed;         130 AA.
AC   P80344;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Cholecystokinin;
DE            Short=CCK;
DE   Contains:
DE     RecName: Full=Cholecystokinin-58;
DE              Short=CCK58;
DE   Contains:
DE     RecName: Full=Cholecystokinin-33;
DE              Short=CCK33;
DE   Contains:
DE     RecName: Full=Cholecystokinin-8;
DE              Short=CCK8;
DE   Contains:
DE     RecName: Full=Cholecystokinin-7;
DE              Short=CCK7;
DE   Flags: Precursor;
GN   Name=CCK;
OS   Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX   NCBI_TaxID=8400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=9075736; DOI=10.1210/endo.138.4.5084;
RA   Rourke I.J., Rehfeld J.F., Moeller M., Johnson A.H.;
RT   "Characterization of the cholecystokinin and gastrin genes from the
RT   bullfrog, Rana catesbeiana: evolutionary conservation of primary and
RT   secondary sites of gene expression.";
RL   Endocrinology 138:1719-1727(1997).
RN   [2]
RP   PROTEIN SEQUENCE OF 50-118, SULFATION AT TYR-112, AND AMIDATION AT PHE-118.
RC   TISSUE=Small intestine;
RX   PubMed=7925386; DOI=10.1111/j.1432-1033.1994.00691.x;
RA   Johnsen A.H.;
RT   "Identification of cholecystokinin from frog and turtle. Divergence of
RT   cholecystokinin and gastrin occurred before the evolution of amphibia.";
RL   Eur. J. Biochem. 224:691-702(1994).
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.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed in brain, lung, testis and throughout the
CC       length of the small intestine. In the brain, expressed predominantly in
CC       the optic tectum and brain stem.
CC   -!- PTM: The precursor is cleaved by proteases to produce a number of
CC       active cholecystokinins.
CC   -!- MISCELLANEOUS: Frog brain contains CCK-octapeptide (CCK8) and CCK7;
CC       whereas the gut contains intact CCK33 and CCK58.
CC   -!- SIMILARITY: Belongs to the gastrin/cholecystokinin family.
CC       {ECO:0000305}.
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DR   EMBL; Y08395; CAA69674.1; -; Genomic_DNA.
DR   EMBL; Y08396; CAA69674.1; JOINED; Genomic_DNA.
DR   EMBL; Y08393; CAA69673.1; -; mRNA.
DR   PIR; S48150; S48150.
DR   AlphaFoldDB; P80344; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
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; Secreted; Signal; Sulfation.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..130
FT                   /note="Cholecystokinin"
FT                   /id="PRO_0000010588"
FT   PROPEP          21..60
FT                   /id="PRO_0000010589"
FT   PEPTIDE         61..118
FT                   /note="Cholecystokinin-58"
FT                   /id="PRO_0000010590"
FT   PEPTIDE         86..118
FT                   /note="Cholecystokinin-33"
FT                   /id="PRO_0000010591"
FT   PEPTIDE         111..118
FT                   /note="Cholecystokinin-8"
FT                   /id="PRO_0000010592"
FT   PEPTIDE         112..118
FT                   /note="Cholecystokinin-7"
FT                   /id="PRO_0000010593"
FT   PROPEP          122..130
FT                   /id="PRO_0000010594"
FT   MOD_RES         112
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000269|PubMed:7925386"
FT   MOD_RES         118
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:7925386"
FT   MOD_RES         126
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         128
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   130 AA;  14449 MW;  B2A265CE4CADB641 CRC64;
     MYIGICICVL LAALSASSTG QQTVGSMNED PGAREIEQQN ILQHPRHIRA SSSAQLKPFQ
     RIDGTSDQKA VIGAMLAKYL QTRKAGSSTG RYAVLPNRPV IDPTHRINDR DYMGWMDFGR
     RSAEEYEYSS