CCKN_MACFA
ID CCKN_MACFA Reviewed; 115 AA.
AC P23362; Q4R5N2;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 77.
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; ORFNames=QccE-12659;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2174979; DOI=10.1002/jnr.490270205;
RA Bernal J., Godbout M., Hasel K.W., Travis G.H., Sutcliffe J.G.;
RT "Patterns of cerebral cortex mRNA expression.";
RL J. Neurosci. Res. 27:153-158(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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.
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; M60458; AAA36837.1; -; mRNA.
DR EMBL; AB169511; BAE01593.1; -; mRNA.
DR PIR; A48318; A48318.
DR AlphaFoldDB; P23362; -.
DR STRING; 9541.XP_005546816.1; -.
DR eggNOG; ENOG502S472; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005184; F:neuropeptide hormone activity; ISS:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR GO; GO:0042755; P:eating behavior; 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 3: Inferred from homology;
KW Amidation; Cleavage on pair of basic residues; Hormone; Reference proteome;
KW Secreted; Signal; Sulfation.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..115
FT /note="Cholecystokinin"
FT /id="PRO_0000010544"
FT PROPEP 21..44
FT /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT /id="PRO_0000010545"
FT PEPTIDE 46..103
FT /note="Cholecystokinin-58"
FT /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT /id="PRO_0000010546"
FT PEPTIDE 46..94
FT /note="Cholecystokinin-58 desnonopeptide"
FT /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT /id="PRO_0000306309"
FT PEPTIDE 65..103
FT /note="Cholecystokinin-39"
FT /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT /id="PRO_0000010547"
FT PEPTIDE 71..103
FT /note="Cholecystokinin-33"
FT /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT /id="PRO_0000010548"
FT PEPTIDE 79..103
FT /note="Cholecystokinin-25"
FT /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT /id="PRO_0000306310"
FT PEPTIDE 86..103
FT /note="Cholecystokinin-18"
FT /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT /id="PRO_0000306311"
FT PEPTIDE 92..103
FT /note="Cholecystokinin-12"
FT /evidence="ECO:0000250|UniProtKB:P01356"
FT /id="PRO_0000010549"
FT PEPTIDE 96..103
FT /note="Cholecystokinin-8"
FT /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT /id="PRO_0000010550"
FT PEPTIDE 97..103
FT /note="Cholecystokinin-7"
FT /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT /id="PRO_0000306312"
FT PEPTIDE 99..103
FT /note="Cholecystokinin-5"
FT /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT /id="PRO_0000306313"
FT PROPEP 107..115
FT /id="PRO_0000010551"
FT REGION 21..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 97
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT MOD_RES 103
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250|UniProtKB:P06307"
FT MOD_RES 111
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 113
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 115 AA; 12665 MW; C151B73646E95019 CRC64;
MNSGVSLCVL MAVLAAGALT QPVPPAEPAG SGLQRAEEAP RRQLRAVQRT DGESRAHLGA
LLARYIQQAR KAPSGRMSII KNLQNLDPSH RISDRDYMGW MDFGRRSAEE YEYPS
