ID   CCKN_PAROL              Reviewed;         135 AA.
AC   O57312;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Cholecystokinin;
DE            Short=CCK;
DE   Contains:
DE     RecName: Full=Cholecystokinin-8;
DE              Short=CCK8;
DE   Flags: Precursor;
GN   Name=cck;
OS   Paralichthys olivaceus (Bastard halibut) (Hippoglossus olivaceus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Paralichthyidae;
OC   Paralichthys.
OX   NCBI_TaxID=8255;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=11042006; DOI=10.1006/gcen.2000.7512;
RA   Kurokawa T., Suzuki T., Andoh T.;
RT   "Development of cholecystokinin and pancreatic polypeptide endocrine
RT   systems during the larval stage of Japanese flounder, Paralichthys
RT   olivaceus.";
RL   Gen. Comp. Endocrinol. 120:8-16(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}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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:0000305}.
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DR   EMBL; AB009281; BAA23734.1; -; mRNA.
DR   RefSeq; XP_019946102.1; XM_020090543.1.
DR   AlphaFoldDB; O57312; -.
DR   GeneID; 109631669; -.
DR   KEGG; pov:109631669; -.
DR   CTD; 100000095; -.
DR   OrthoDB; 1524113at2759; -.
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   2: Evidence at transcript level;
KW   Amidation; Cleavage on pair of basic residues; Hormone; Secreted; Signal;
KW   Sulfation.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..135
FT                   /note="Cholecystokinin"
FT                   /id="PRO_0000010586"
FT   PEPTIDE         116..123
FT                   /note="Cholecystokinin-8"
FT                   /id="PRO_0000010587"
FT   REGION          26..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         117
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         123
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         131
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         133
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   135 AA;  14773 MW;  F092E2FCC036534D CRC64;
     MTAGLCVCVL LAVLCTSCLG HPISSQHLDE GQRSISTPSE ALLEADTHSL GEPHLRQSRS
     APQLKSLPVA EEDGDSRANL SELLARLISS RKGSVRRNST AYSKGLSPNH RIADRDYLGW
     MDFGRRSAEE YEYSS