ID   CCKN_STRCA              Reviewed;         130 AA.
AC   Q9PU29;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Cholecystokinin;
DE            Short=CCK;
DE   Contains:
DE     RecName: Full=Cholecystokinin-70;
DE              Short=CCK70;
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   Struthio camelus (Common ostrich).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC   Struthio.
OX   NCBI_TaxID=8801;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAB62255.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 111-118, TISSUE
RP   SPECIFICITY, SULFATION AT TYR-112, AMIDATION AT PHE-118, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain {ECO:0000269|PubMed:11072120};
RX   PubMed=11072120; DOI=10.1016/s0196-9781(00)00276-x;
RA   Jonson L., Schoeman N., Saayman H., Naude R., Jensen H., Johnsen A.H.;
RT   "Identification of ostrich and chicken cholecystokinin cDNA and intestinal
RT   peptides.";
RL   Peptides 21:1337-1344(2000).
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 (By similarity). {ECO:0000250|UniProtKB:P01356}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Highly concentrated in the duodenum. Also localized
CC       in more distal parts of the small intestine.
CC       {ECO:0000269|PubMed:11072120}.
CC   -!- PTM: The precursor is cleaved by proteases to produce a number of
CC       active cholecystokinins.
CC   -!- MASS SPECTROMETRY: [Cholecystokinin-7]: Mass=980.3; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11072120};
CC   -!- MASS SPECTROMETRY: [Cholecystokinin-7]: Mass=1059.9; Method=MALDI;
CC       Note=Tyrosyl sulfated.; Evidence={ECO:0000269|PubMed:11072120};
CC   -!- MASS SPECTROMETRY: [Cholecystokinin-8]: Mass=1095.4; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11072120};
CC   -!- MASS SPECTROMETRY: [Cholecystokinin-8]: Mass=1175.2; Method=MALDI;
CC       Note=Tyrosyl sulfated.; Evidence={ECO:0000269|PubMed:11072120};
CC   -!- SIMILARITY: Belongs to the gastrin/cholecystokinin family.
CC       {ECO:0000250|UniProtKB:P01356}.
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DR   EMBL; AJ251274; CAB62255.1; -; mRNA.
DR   AlphaFoldDB; Q9PU29; -.
DR   GO; GO:0030424; C:axon; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; NAS:UniProtKB.
DR   GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR   GO; GO:0007586; P:digestion; 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; Secreted; Signal; Sulfation.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..130
FT                   /note="Cholecystokinin"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000010580"
FT   PROPEP          21..48
FT                   /evidence="ECO:0000303|PubMed:11072120"
FT                   /id="PRO_0000010581"
FT   PEPTIDE         49..118
FT                   /note="Cholecystokinin-70"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000010582"
FT   PEPTIDE         111..118
FT                   /note="Cholecystokinin-8"
FT                   /id="PRO_0000010583"
FT   PEPTIDE         112..118
FT                   /note="Cholecystokinin-7"
FT                   /id="PRO_0000010584"
FT   PROPEP          122..130
FT                   /evidence="ECO:0000269|PubMed:11072120"
FT                   /id="PRO_0000010585"
FT   REGION          40..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         112
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000303|PubMed:11072120"
FT   MOD_RES         118
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000305|PubMed:11072120"
FT   MOD_RES         126
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P01356"
FT   MOD_RES         128
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P01356"
SQ   SEQUENCE   130 AA;  14273 MW;  ACBDEAEF2B4099F0 CRC64;
     MYSGICICVF LAVLSASSFG QQTAGSHNGN PLAAELEQSL TEHHRHVRAP SSAGPLKPVP
     RLDGSIDQRA NIGALLAKYL QQARKGPTGR ISVMGNRVQS IDPTHRINDR DYMGWMDFGR
     RSAEEYEYSS