ID   CCKN_TRASC              Reviewed;         130 AA.
AC   P80345; O93608;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   24-OCT-2003, 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-40;
DE              Short=CCK40;
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;
OS   Trachemys scripta (Red-eared slider turtle) (Pseudemys scripta).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Testudinoidea; Emydidae; Trachemys.
OX   NCBI_TaxID=34903;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=10561540; DOI=10.1016/s0167-4838(99)00197-1;
RA   Joenson L., Bundgaard J.R., Johnsen A.H., Rourke I.J.;
RT   "Identification and expression of gastrin and cholecystokinin mRNAs from
RT   the turtle, Pseudemys scripta: evidence of tissue-specific tyrosyl
RT   sulfation.";
RL   Biochim. Biophys. Acta 1435:84-93(1999).
RN   [2]
RP   PROTEIN SEQUENCE OF 49-118, SULFATION AT TYR-112, AND AMIDATION AT PHE-118.
RC   TISSUE=Brain, and 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, duodenum and small intestine.
CC       {ECO:0000269|PubMed:10561540}.
CC   -!- PTM: The precursor is cleaved by proteases to produce a number of
CC       active cholecystokinins. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Turtle brain contains CCK-octapeptide (CCK8) and CCK7,
CC       whereas the gut contains intact CCK33, CCK40 and CCK58.
CC   -!- SIMILARITY: Belongs to the gastrin/cholecystokinin family.
CC       {ECO:0000305}.
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DR   EMBL; AJ010742; CAA09334.1; -; mRNA.
DR   PIR; S48170; S48170.
DR   AlphaFoldDB; P80345; -.
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_0000010595"
FT   PROPEP          21..60
FT                   /id="PRO_0000010596"
FT   PEPTIDE         61..118
FT                   /note="Cholecystokinin-58"
FT                   /id="PRO_0000010597"
FT   PEPTIDE         79..118
FT                   /note="Cholecystokinin-40"
FT                   /id="PRO_0000010598"
FT   PEPTIDE         86..118
FT                   /note="Cholecystokinin-33"
FT                   /id="PRO_0000010599"
FT   PEPTIDE         111..118
FT                   /note="Cholecystokinin-8"
FT                   /id="PRO_0000010600"
FT   PEPTIDE         112..118
FT                   /note="Cholecystokinin-7"
FT                   /id="PRO_0000010601"
FT   PROPEP          122..130
FT                   /id="PRO_0000010602"
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;  14603 MW;  AB2F5252A917808A CRC64;
     MYSGICIYMF LAMLSTSSSG QQATGSHNEN PVATELEQSL TEHHRHVRVP SSAGQLKPIQ
     RLDGNVDQKA NIGALLAKYL QQARKGPTGR ISMMGNRVQN IDPTHRINDR DYMGWMDFGR
     RSAEEYEYSS