CCKN_CHICK
ID CCKN_CHICK Reviewed; 130 AA.
AC Q9PU41;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 96.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAB62203.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=White Plymouthrock {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).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 111-118, SULFATION AT TYR-112, AND AMIDATION AT
RP PHE-118.
RC TISSUE=Brain {ECO:0000269|PubMed:3620999};
RX PubMed=3620999; DOI=10.1016/0361-9230(87)90211-5;
RA Fan Z.-W., Eng J., Miedel M., Hulmes J.D., Pan Y.-C., Yalow R.S.;
RT "Cholecystokinin octapeptides purified from chinchilla and chicken
RT brains.";
RL Brain Res. Bull. 18:757-760(1987).
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=8355559; DOI=10.1016/0024-3205(93)90139-t;
RA Martinez V., Jimenez M., Gonalons E., Vergara P.;
RT "Effects of cholecystokinin and gastrin on gastroduodenal motility and
RT coordination in chickens.";
RL Life Sci. 52:191-198(1993).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=8637413; DOI=10.1016/0024-3205(96)00152-x;
RA Rodriguez-Sinovas A., Fernandez E., Gonalons E.;
RT "Central and NO mediated mechanisms are involved in the inhibitory effects
RT of CCK on the chicken cecorectal area.";
RL Life Sci. 58:1869-1882(1996).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=9039026; DOI=10.1152/ajpregu.1997.272.1.r334;
RA Rodriguez-Sinovas A., Fernandez E., Manteca X., Fernandez A.G.,
RA Gonalons E.;
RT "CCK is involved in both peripheral and central mechanisms controlling food
RT intake in chickens.";
RL Am. J. Physiol. 272:R334-R340(1997).
RN [6] {ECO:0000305}
RP INDUCTION, AND FUNCTION.
RX PubMed=10069039;
RX DOI=10.1002/(sici)1097-010x(19990301/01)283:4/5<448::aid-jez14>3.0.co;2-z;
RA Furuse M.;
RT "Release and endogenous actions of the gastrin/cholecystokinin (CCK) family
RT in the chicken.";
RL J. Exp. Zool. 283:448-454(1999).
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). It also decreases food intake and regulates
CC gastrointestinal physiological processes.
CC {ECO:0000250|UniProtKB:P01356, ECO:0000269|PubMed:10069039,
CC ECO:0000269|PubMed:8355559, ECO:0000269|PubMed:8637413,
CC ECO:0000269|PubMed:9039026}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: In the small intestine, the major production site
CC is around the vitelline diverticulum. {ECO:0000269|PubMed:11072120}.
CC -!- INDUCTION: By dietary protein, amino acids and medium-chain
CC triacylglycerol. {ECO:0000269|PubMed:10069039}.
CC -!- PTM: The precursor is cleaved by proteases to produce a number of
CC active cholecystokinins.
CC -!- SIMILARITY: Belongs to the gastrin/cholecystokinin family.
CC {ECO:0000250|UniProtKB:P01356}.
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DR EMBL; AJ251273; CAB62203.1; -; mRNA.
DR RefSeq; NP_001001741.1; NM_001001741.1.
DR RefSeq; XP_015136818.1; XM_015281332.1.
DR AlphaFoldDB; Q9PU41; -.
DR STRING; 9031.ENSGALP00000019451; -.
DR PaxDb; Q9PU41; -.
DR GeneID; 414884; -.
DR KEGG; gga:414884; -.
DR CTD; 885; -.
DR VEuPathDB; HostDB:geneid_414884; -.
DR eggNOG; ENOG502S472; Eukaryota.
DR InParanoid; Q9PU41; -.
DR OrthoDB; 1524113at2759; -.
DR PhylomeDB; Q9PU41; -.
DR PRO; PR:Q9PU41; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005179; F:hormone activity; NAS:UniProtKB.
DR GO; GO:0005184; F:neuropeptide hormone activity; IBA:GO_Central.
DR GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR GO; GO:0007586; P:digestion; IDA: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..130
FT /note="Cholecystokinin"
FT /evidence="ECO:0000255"
FT /id="PRO_0000010574"
FT PROPEP 21..48
FT /evidence="ECO:0000303|PubMed:11072120"
FT /id="PRO_0000010575"
FT PEPTIDE 49..118
FT /note="Cholecystokinin-70"
FT /evidence="ECO:0000305"
FT /id="PRO_0000010576"
FT PEPTIDE 111..118
FT /note="Cholecystokinin-8"
FT /id="PRO_0000010577"
FT PEPTIDE 112..118
FT /note="Cholecystokinin-7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000010578"
FT PROPEP 122..130
FT /evidence="ECO:0000303|PubMed:11072120"
FT /id="PRO_0000010579"
FT REGION 21..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 112
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:3620999"
FT MOD_RES 118
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:3620999"
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; 14091 MW; 05CEBE4BB10527C4 CRC64;
MYGGICICVL LAALSVSSLG QQPAGSHDGS PVAAELQQSL TEPHRHSRAP SSAGPLKPAP
RLDGSFEQRA TIGALLAKYL QQARKGSTGR FSVLGNRVQS IDPTHRINDR DYMGWMDFGR
RSAEEYEYSS
