CCKN_CARAU
ID CCKN_CARAU Reviewed; 123 AA.
AC O93464;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Cholecystokinin;
DE AltName: Full=CCK8;
DE Contains:
DE RecName: Full=Cholecystokinin-8;
DE Short=CCK8;
DE Contains:
DE RecName: Full=Cholecystokinin-12;
DE Short=CCK12;
DE Contains:
DE RecName: Full=Cholecystokinin-26;
DE Short=CCK26;
DE Contains:
DE RecName: Full=Cholecystokinin-36;
DE Short=CCK36;
DE Contains:
DE RecName: Full=Cholecystokinin-69;
DE Short=CCK69;
DE Flags: Precursor;
GN Name=cck;
OS Carassius auratus (Goldfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Carassius.
OX NCBI_TaxID=7957;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC24727.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain {ECO:0000269|PubMed:9493851};
RX PubMed=9493851; DOI=10.1016/s0196-9781(97)00296-9;
RA Peyon P.E.A., Lin X.W., Himick B.A., Peter R.E.;
RT "Molecular cloning and expression of cDNA encoding brain
RT preprocholecystokinin in goldfish.";
RL Peptides 19:199-210(1998).
RN [2] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=8262360; DOI=10.1006/gcen.1993.1146;
RA Himick B.A., Golosinski A.A., Jonsson A.-C., Peter R.E.;
RT "CCK/gastrin-like immunoreactivity in the goldfish pituitary: regulation of
RT pituitary hormone secretion by CCK-like peptides in vitro.";
RL Gen. Comp. Endocrinol. 92:88-103(1993).
RN [3] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=8092330; DOI=10.1152/ajpregu.1994.267.3.r841;
RA Himick B.A., Peter R.E.;
RT "CCK/gastrin-like immunoreactivity in brain and gut, and CCK suppression of
RT feeding in goldfish.";
RL Am. J. Physiol. 267:R841-R851(1994).
RN [4] {ECO:0000305}
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10640690; DOI=10.1016/s0169-328x(99)00282-x;
RA Peyon P.E.A., Saied H., Lin X.W., Peter R.E.;
RT "Postprandial, seasonal and sexual variations in cholecystokinin gene
RT expression in goldfish brain.";
RL Brain Res. Mol. Brain Res. 74:190-196(1999).
RN [5] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=12124755; DOI=10.1002/cne.10317;
RA Farrell W.J., Boettger B., Ahmadi F., Finger T.E.;
RT "Distribution of cholecystokinin, calcitonin gene-related peptide,
RT neuropeptide Y, and galanin in the primary gustatory nuclei of the
RT goldfish.";
RL J. Comp. Neurol. 450:103-114(2002).
RN [6] {ECO:0000305}
RP INDUCTION.
RX PubMed=14751584; DOI=10.1016/j.brainres.2003.11.011;
RA Volkoff H., Peter R.E.;
RT "Effects of lipopolysaccharide treatment on feeding of goldfish: role of
RT appetite-regulating peptides.";
RL Brain Res. 998:139-147(2004).
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=15256279; DOI=10.1016/j.regpep.2004.04.011;
RA Canosa L.F., Peter R.E.;
RT "Effects of cholecystokinin and bombesin on the expression of
RT preprosomatostatin-encoding genes in goldfish forebrain.";
RL Regul. Pept. 121:99-105(2004).
CC -!- FUNCTION: This peptide hormone induces gall bladder contraction and the
CC release of pancreatic enzymes in the gut (By similarity). Induces the
CC secretion of gonadotropin and growth hormone from the pituitary.
CC Suppresses food intake and decreases the expression of
CC preprosomatostatin genes in the forebrain.
CC {ECO:0000250|UniProtKB:P01356, ECO:0000269|PubMed:15256279,
CC ECO:0000269|PubMed:8092330, ECO:0000269|PubMed:8262360}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:9493851,
CC ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the ovary, kidney, gill,
CC gastrointestinal tract and pituitary. Differentially expressed in the
CC brain in the optic tectum-thalamus, hypothalamus, telencephalon,
CC olfactory bulb and tract, preoptic region and posterior brain region.
CC Expression is strongest in the hypothalamus, where localization is to
CC the posterior ventrolateral region. Expression in the brain is
CC transiently increased 2 hours after feeding. Abundant in the sensory
CC layers of the vagal lobe and along the border of the sensory region of
CC the lobe and the deep fiber laye. Also present in the facial lobe and
CC throughout the glossopharyngeal lobe. {ECO:0000269|PubMed:10640690,
CC ECO:0000269|PubMed:12124755, ECO:0000269|PubMed:8092330,
CC ECO:0000269|PubMed:8262360, ECO:0000269|PubMed:9493851}.
CC -!- DEVELOPMENTAL STAGE: Expression in the brain shows variation throughout
CC the seasonal sexual cycle; in the optic tectum-thalamus of females,
CC expression levels are lower in early gonadal recrudescence (October)
CC compared to other sexual stages. In males, expression is high in the
CC olfactory bulbs in early gonadal recrudescence and low in the posterior
CC brain in late gonadal recrudescence (January). Expression is higher in
CC females than males in the telencephalon-preoptic region and posterior
CC brain during late gonadal recrudescence, and in the olfactory bulbs and
CC optic tectum-thalamus during the sexually mature (April), and post-
CC spawning and sexually regressed (July) stages.
CC {ECO:0000269|PubMed:10640690}.
CC -!- INDUCTION: By lipopolysaccharide (LPS); in hypothalamus.
CC {ECO:0000269|PubMed:14751584}.
CC -!- PTM: The precursor is cleaved by proteases to produce a number of
CC active cholecystokinins. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the gastrin/cholecystokinin family.
CC {ECO:0000250|UniProtKB:P01356}.
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DR EMBL; U70865; AAC24727.1; -; mRNA.
DR AlphaFoldDB; O93464; -.
DR Ensembl; ENSCART00000041420; ENSCARP00000039674; ENSCARG00000017144.
DR Proteomes; UP000515129; Genome assembly.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; ISS:UniProtKB.
DR GO; GO:0007631; P:feeding behavior; IDA:UniProtKB.
DR GO; GO:0030252; P:growth hormone secretion; IDA:UniProtKB.
DR GO; GO:0030072; P:peptide hormone secretion; IDA: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 2: Evidence at transcript level;
KW Amidation; Cleavage on pair of basic residues; Hormone; Reference proteome;
KW Secreted; Signal; Sulfation.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..123
FT /note="Cholecystokinin"
FT /evidence="ECO:0000255"
FT /id="PRO_0000042675"
FT PROPEP 20..103
FT /evidence="ECO:0000255, ECO:0000303|PubMed:9493851"
FT /id="PRO_0000042676"
FT PEPTIDE 43..111
FT /note="Cholecystokinin-69"
FT /evidence="ECO:0000305"
FT /id="PRO_0000042677"
FT PEPTIDE 76..111
FT /note="Cholecystokinin-36"
FT /evidence="ECO:0000305"
FT /id="PRO_0000042678"
FT PEPTIDE 86..111
FT /note="Cholecystokinin-26"
FT /evidence="ECO:0000305"
FT /id="PRO_0000042679"
FT PEPTIDE 100..111
FT /note="Cholecystokinin-12"
FT /evidence="ECO:0000305"
FT /id="PRO_0000042680"
FT PEPTIDE 104..111
FT /note="Cholecystokinin-8"
FT /evidence="ECO:0000305"
FT /id="PRO_0000042681"
FT PROPEP 115..123
FT /evidence="ECO:0000255, ECO:0000303|PubMed:9493851"
FT /id="PRO_0000042682"
FT REGION 43..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 105
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01356"
FT MOD_RES 111
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250"
FT MOD_RES 119
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01356"
FT MOD_RES 121
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01356"
SQ SEQUENCE 123 AA; 13439 MW; 27A850488F9AFAB4 CRC64;
MNAGICVCVL LAALSTSSCL SLPAVSEDGG QSDLGIVMEH TRHTRAAPSS GQLSLLSKAE
DDEEPRSSLT ELLARIISTK GTYRRSPSPK SKSMGNNHRI KDRDYLGWMD FGRRSAEEYE
YSS
