CCKN_CANLF
ID CCKN_CANLF Reviewed; 58 AA.
AC Q9TS44;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Cholecystokinins;
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 {ECO:0000250|UniProtKB:P01356};
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE.
RC STRAIN=Mongrel {ECO:0000269|PubMed:2430967};
RC TISSUE=Intestinal mucosa {ECO:0000269|PubMed:2430967};
RX PubMed=2430967; DOI=10.1016/s0021-9258(18)66578-0;
RA Reeve J.R. Jr., Eysselein V.E., Walsh J.H., Ben-Avram C.M., Shively J.E.;
RT "New molecular forms of cholecystokinin. Microsequence analysis of forms
RT previously characterized by chromatographic methods.";
RL J. Biol. Chem. 261:16392-16397(1986).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 1-38, AND FUNCTION.
RC TISSUE=Intestinal mucosa {ECO:0000269|PubMed:7134033};
RX PubMed=7134033; DOI=10.1016/0196-9781(82)90171-1;
RA Eysselein V.E., Reeve J.R. Jr., Shively J.E., Hawke D., Walsh J.H.;
RT "Partial structure of a large canine cholecystokinin (CCK58): amino acid
RT sequence.";
RL Peptides 3:687-691(1982).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 1-29, SYNTHESIS, FUNCTION, MASS SPECTROMETRY, AND
RP SULFATION AT TYR-52.
RX PubMed=12686463; DOI=10.1016/s0167-0115(02)00301-4;
RA Reeve J.R. Jr., Keire D.A., Coskun T., Green G.M., Evans C., Ho F.-J.,
RA Lee T.D., Davis M.T., Shively J.E., Solomon T.E.;
RT "Synthesis of biologically active canine CCK-58.";
RL Regul. Pept. 113:71-77(2003).
RN [4] {ECO:0000305}
RP PROTEIN SEQUENCE OF 1-25 AND 32-58, FUNCTION, AMIDATION AT PHE-58, AND
RP SULFATION AT TYR-52.
RC TISSUE=Intestinal mucosa {ECO:0000269|PubMed:15064233};
RX PubMed=15064233; DOI=10.1152/ajpgi.00520.2003;
RA Reeve J.R. Jr., Liddle R.A., McVey D.C., Vigna S.R., Solomon T.E.,
RA Keire D.A., Rosenquist G., Shively J.E., Lee T.D., Chew P., Green G.M.,
RA Coskun T.;
RT "Identification of nonsulfated cholecystokinin-58 in canine intestinal
RT extracts and its biological properties.";
RL Am. J. Physiol. 287:G326-G333(2004).
RN [5] {ECO:0000305}
RP PROTEIN SEQUENCE OF 1-22.
RC STRAIN=Mongrel {ECO:0000269|PubMed:6093106};
RC TISSUE=Brain {ECO:0000269|PubMed:6093106};
RX PubMed=6093106; DOI=10.1073/pnas.81.21.6565;
RA Eysselein V.E., Reeve J.R. Jr., Shively J.E., Miller C., Walsh J.H.;
RT "Isolation of a large cholecystokinin precursor from canine brain.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:6565-6568(1984).
RN [6] {ECO:0000305, ECO:0000312|PIR:A39462}
RP PROTEIN SEQUENCE OF 1-12, FUNCTION, AND MASS SPECTROMETRY.
RC STRAIN=Mongrel {ECO:0000269|PubMed:1713209};
RC TISSUE=Intestinal mucosa {ECO:0000269|PubMed:1713209};
RX PubMed=1713209; DOI=10.1016/s0021-9258(18)92767-5;
RA Reeve J.R. Jr., Eysselein V.E., Eberlein G.A., Chew P., Ho F.-J.,
RA Huebner V.D., Shively J.E., Lee T.D., Liddle R.A.;
RT "Characterization of canine intestinal cholecystokinin-58 lacking its
RT carboxyl-terminal nonapeptide. Evidence for similar post-translational
RT processing in brain and gut.";
RL J. Biol. Chem. 266:13770-13776(1991).
RN [7] {ECO:0000305}
RP FUNCTION, SYNTHESIS OF 51-58, AND MASS SPECTROMETRY.
RX PubMed=8967499; DOI=10.1152/ajpgi.1996.270.5.g860;
RA Reeve J.R. Jr., Eysselein V.E., Rosenquist G., Zeeh J., Regner U.,
RA Ho F.-J., Chew P., Davis M.T., Lee T.D., Shively J.E., Brazer S.R.,
RA Liddle R.A.;
RT "Evidence that CCK-58 has structure that influences its biological
RT activity.";
RL Am. J. Physiol. 270:G860-G868(1996).
RN [8] {ECO:0000305}
RP SUBUNIT, AND MASS SPECTROMETRY.
RX PubMed=12370550; DOI=10.1097/00006676-200210000-00021;
RA Reeve J.R. Jr., McVey D.C., Bunnett N.W., Solomon T.E., Keire D.A.,
RA Ho F.-J., Davis M.T., Lee T.D., Shively J.E., Vigna S.R.;
RT "Differences in receptor binding and stability to enzymatic digestion
RT between CCK-8 and CCK-58.";
RL Pancreas 25:E50-E55(2002).
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. cholecystokinin 58 and cholecystokinin 8, but not
CC cholecystokinin 58 desnonopeptide, stimulate amylase release from the
CC pancreas. cholecystokinin 58, but not cholecystokinin 8, increases
CC bile-pancreatic volume. {ECO:0000269|PubMed:12686463,
CC ECO:0000269|PubMed:15064233, ECO:0000269|PubMed:1713209,
CC ECO:0000269|PubMed:7134033, ECO:0000269|PubMed:8967499, ECO:0000305}.
CC -!- SUBUNIT: Binds to CCK-A receptors in the pancreas and CCK-B receptors
CC in the brain. cholecystokinin 8 binds CCK-A receptors more potently
CC than cholecystokinin 58, cholecystokinin 8 and cholecystokinin 58 bind
CC CCK-B receptors with equal affinity. {ECO:0000269|PubMed:12370550}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- PTM: The precursor is cleaved by proteases to produce a number of
CC active cholecystokinins. {ECO:0000269|PubMed:2430967}.
CC -!- PTM: [Cholecystokinin-58]: Cholecystokinin 58 occurs in both sulfated
CC (CCK58(s)) and nonsulfated (CCK58(ns)) forms, which differ in their
CC receptor-binding activities. CCK58(s) binds to the CCK-A receptor with
CC high affinity, CCK58(ns) binds poorly to the CCK-A receptor. CCK58(s)
CC and CCK58(ns) both bind the CCK-B receptor.
CC {ECO:0000269|PubMed:12686463, ECO:0000269|PubMed:15064233}.
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 -!- MASS SPECTROMETRY: [Cholecystokinin-58]: Mass=6688;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:12370550};
CC -!- MASS SPECTROMETRY: [Cholecystokinin-58]: Mass=6690;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:12686463};
CC -!- MASS SPECTROMETRY: [Cholecystokinin-58]: Mass=6680; Method=FAB;
CC Evidence={ECO:0000269|PubMed:8967499};
CC -!- MASS SPECTROMETRY: [Cholecystokinin-58 desnonopeptide]: Mass=5407.6;
CC Method=FAB; Evidence={ECO:0000269|PubMed:1713209};
CC -!- SIMILARITY: Belongs to the gastrin/cholecystokinin family.
CC {ECO:0000255}.
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DR PIR; A39462; A39462.
DR AlphaFoldDB; Q9TS44; -.
DR SMR; Q9TS44; -.
DR STRING; 9612.ENSCAFP00000007846; -.
DR PaxDb; Q9TS44; -.
DR eggNOG; ENOG502S472; Eukaryota.
DR InParanoid; Q9TS44; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; ISS:AgBase.
DR GO; GO:0005184; F:neuropeptide hormone activity; IBA:GO_Central.
DR GO; GO:0007586; P:digestion; IBA:GO_Central.
DR GO; GO:0032094; P:response to food; ISS: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; Sulfation.
FT PEPTIDE 1..58
FT /note="Cholecystokinin-58"
FT /evidence="ECO:0000269|PubMed:2430967"
FT /id="PRO_0000306294"
FT PEPTIDE 1..49
FT /note="Cholecystokinin-58 desnonopeptide"
FT /evidence="ECO:0000269|PubMed:2430967"
FT /id="PRO_0000306295"
FT PEPTIDE 20..58
FT /note="Cholecystokinin-39"
FT /evidence="ECO:0000269|PubMed:2430967"
FT /id="PRO_0000306296"
FT PEPTIDE 26..58
FT /note="Cholecystokinin-33"
FT /evidence="ECO:0000269|PubMed:2430967"
FT /id="PRO_0000306297"
FT PEPTIDE 34..58
FT /note="Cholecystokinin-25"
FT /evidence="ECO:0000269|PubMed:2430967"
FT /id="PRO_0000306298"
FT PEPTIDE 41..58
FT /note="Cholecystokinin-18"
FT /evidence="ECO:0000269|PubMed:2430967"
FT /id="PRO_0000306299"
FT PEPTIDE 47..58
FT /note="Cholecystokinin-12"
FT /evidence="ECO:0000250|UniProtKB:P01356"
FT /id="PRO_0000306300"
FT PEPTIDE 51..58
FT /note="Cholecystokinin-8"
FT /evidence="ECO:0000269|PubMed:8967499"
FT /id="PRO_0000306301"
FT PEPTIDE 52..58
FT /note="Cholecystokinin-7"
FT /evidence="ECO:0000269|PubMed:2430967"
FT /id="PRO_0000306302"
FT PEPTIDE 54..58
FT /note="Cholecystokinin-5"
FT /evidence="ECO:0000269|PubMed:2430967"
FT /id="PRO_0000306303"
FT MOD_RES 52
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:12686463,
FT ECO:0000269|PubMed:15064233"
FT MOD_RES 58
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:15064233"
FT CONFLICT 2
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 6
FT /note="D -> NS (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 58 AA; 6610 MW; 70E0A78FBB09D444 CRC64;
AVQKVDGEPR AHLGALLARY IQQARKAPSG RMSVIKNLQN LDPSHRISDR DYMGWMDF
