CCKN_BOVIN
ID CCKN_BOVIN Reviewed; 115 AA.
AC P41520; Q29RG8;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Cholecystokinin;
DE Short=CCK;
DE Contains:
DE RecName: Full=Cholecystokinin-58;
DE Short=CCK58;
DE Contains:
DE RecName: Full=Cholecystokinin-58 desnonopeptide;
DE AltName: Full=(1-49)-CCK58;
DE Contains:
DE RecName: Full=Cholecystokinin-39;
DE Short=CCK39;
DE Contains:
DE RecName: Full=Cholecystokinin-33;
DE Short=CCK33;
DE Contains:
DE RecName: Full=Cholecystokinin-25;
DE Short=CCK25;
DE Contains:
DE RecName: Full=Cholecystokinin-18;
DE Short=CCK18;
DE Contains:
DE RecName: Full=Cholecystokinin-12;
DE Short=CCK12;
DE Contains:
DE RecName: Full=Cholecystokinin-8;
DE Short=CCK8;
DE Contains:
DE RecName: Full=Cholecystokinin-7;
DE Short=CCK7;
DE Contains:
DE RecName: Full=Cholecystokinin-5;
DE Short=CCK5;
DE Flags: Precursor;
GN Name=CCK;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 46-74.
RC TISSUE=Brain;
RX PubMed=2217909; DOI=10.1016/0167-0115(90)90131-f;
RA Eng J., Li H.R., Yalow R.S.;
RT "Purification of bovine cholecystokinin-58 and sequencing of its N-
RT terminus.";
RL Regul. Pept. 30:15-19(1990).
RN [3]
RP PROTEIN SEQUENCE OF 65-103, SULFATION AT TYR-97, AND AMIDATION AT PHE-103.
RC TISSUE=Intestine;
RX PubMed=4011954; DOI=10.1016/0167-0115(85)90028-x;
RA Carlquist M., Mutt V., Joernvall H.;
RT "Characterization of two novel forms of cholecystokinin isolated from
RT bovine upper intestine.";
RL Regul. Pept. 11:27-34(1985).
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. Binding to CCK-A receptors stimulates amylase release from
CC the pancreas, binding to CCK-B receptors stimulates gastric acid
CC secretion. {ECO:0000250|UniProtKB:Q9TS44}.
CC -!- SUBUNIT: Binds to CCK-A receptors in the pancreas and CCK-B receptors
CC in the brain. {ECO:0000250|UniProtKB:Q9TS44}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P09240}.
CC -!- PTM: The precursor is cleaved by proteases to produce a number of
CC active cholecystokinins.
CC -!- PTM: [Cholecystokinin-5]: The precursor is cleaved by ACE, which
CC removes the Gly-Arg-Arg peptide at the C-terminus, leading to mature
CC hormone. {ECO:0000250|UniProtKB:P06307}.
CC -!- SIMILARITY: Belongs to the gastrin/cholecystokinin family.
CC {ECO:0000305}.
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DR EMBL; BC114184; AAI14185.1; -; mRNA.
DR PIR; A60315; A60315.
DR PIR; A60326; A60326.
DR RefSeq; NP_001040068.1; NM_001046603.2.
DR AlphaFoldDB; P41520; -.
DR STRING; 9913.ENSBTAP00000017320; -.
DR PaxDb; P41520; -.
DR Ensembl; ENSBTAT00000017320; ENSBTAP00000017320; ENSBTAG00000013027.
DR Ensembl; ENSBTAT00000068176; ENSBTAP00000062442; ENSBTAG00000013027.
DR GeneID; 617510; -.
DR KEGG; bta:617510; -.
DR CTD; 885; -.
DR VEuPathDB; HostDB:ENSBTAG00000013027; -.
DR VGNC; VGNC:26940; CCK.
DR eggNOG; ENOG502S472; Eukaryota.
DR GeneTree; ENSGT00390000003571; -.
DR InParanoid; P41520; -.
DR OMA; YSGLCIC; -.
DR OrthoDB; 1524113at2759; -.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000013027; Expressed in occipital lobe and 41 other tissues.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0005184; F:neuropeptide hormone activity; ISS:UniProtKB.
DR GO; GO:0051428; F:peptide hormone receptor binding; IEA:Ensembl.
DR GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR GO; GO:0007586; P:digestion; IBA:GO_Central.
DR GO; GO:0042755; P:eating behavior; ISS:UniProtKB.
DR GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR GO; GO:0032094; P:response to food; IDA:AgBase.
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..115
FT /note="Cholecystokinin"
FT /id="PRO_0000260763"
FT PROPEP 21..44
FT /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT /id="PRO_0000260764"
FT PEPTIDE 46..103
FT /note="Cholecystokinin-58"
FT /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT /id="PRO_0000010531"
FT PEPTIDE 46..94
FT /note="Cholecystokinin-58 desnonopeptide"
FT /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT /id="PRO_0000306289"
FT PEPTIDE 65..103
FT /note="Cholecystokinin-39"
FT /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT /id="PRO_0000010532"
FT PEPTIDE 71..103
FT /note="Cholecystokinin-33"
FT /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT /id="PRO_0000010533"
FT PEPTIDE 79..103
FT /note="Cholecystokinin-25"
FT /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT /id="PRO_0000306290"
FT PEPTIDE 86..103
FT /note="Cholecystokinin-18"
FT /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT /id="PRO_0000306291"
FT PEPTIDE 92..103
FT /note="Cholecystokinin-12"
FT /evidence="ECO:0000250|UniProtKB:P01356"
FT /id="PRO_0000010534"
FT PEPTIDE 96..103
FT /note="Cholecystokinin-8"
FT /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT /id="PRO_0000010535"
FT PEPTIDE 97..103
FT /note="Cholecystokinin-7"
FT /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT /id="PRO_0000306292"
FT PEPTIDE 99..103
FT /note="Cholecystokinin-5"
FT /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT /id="PRO_0000306293"
FT PROPEP 107..115
FT /id="PRO_0000260765"
FT REGION 21..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 97
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:4011954"
FT MOD_RES 103
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:4011954"
FT MOD_RES 113
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 115 AA; 12835 MW; D90A4881E6D7120F CRC64;
MNRGVCLCLL MAVLAAGALA QPMPHADPTG PRAQQAEEAP RRQLRAVPRV DDEPRAQLGA
LLARYIQQAR KAPSGRMSVI KNLQSLDPSH RISDRDYMGW MDFGRRSAEE FEYTS
