ID CCKNA_XENLA Reviewed; 123 AA.
AC P50144; B7ZQP7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Cholecystokinin A;
DE AltName: Full=Cholecystokinin type 1;
DE Contains:
DE RecName: Full=Cholecystokinin;
DE Short=CCK;
DE Flags: Precursor;
GN Name=cck-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=7669225; DOI=10.1677/jme.0.0140357;
RA Wechselberger C., Kreil G.;
RT "Structure of two cDNAs encoding cholecystokinin precursors from the brain
RT of Xenopus laevis.";
RL J. Mol. Endocrinol. 14:357-364(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Brain, gastrointestinal tract and lung.
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; Z47557; CAA87638.1; -; mRNA.
DR EMBL; BC169884; AAI69884.1; -; mRNA.
DR EMBL; BC170160; AAI70160.1; -; mRNA.
DR PIR; I51604; I51604.
DR RefSeq; NP_001079303.1; NM_001085834.1.
DR AlphaFoldDB; P50144; -.
DR GeneID; 378611; -.
DR KEGG; xla:378611; -.
DR AGR; Xenbase:XB-GENE-6252398; -.
DR CTD; 378611; -.
DR Xenbase; XB-GENE-6252398; cck.S.
DR OMA; FTTHERH; -.
DR OrthoDB; 5293435at2759; -.
DR Proteomes; UP000186698; Chromosome 6S.
DR Bgee; 378611; Expressed in brain and 6 other cell types or tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005184; F:neuropeptide hormone activity; IEA:InterPro.
DR GO; GO:0007586; P:digestion; IEA:InterPro.
DR InterPro; IPR015499; CCK-like.
DR InterPro; IPR001651; Gastrin/CCK.
DR InterPro; IPR013152; Gastrin/cholecystokinin_CS.
DR PANTHER; PTHR10786; CHOLECYSTOKININ; 1.
DR PANTHER; PTHR10786:SF0; CHOLECYSTOKININ; 1.
DR Pfam; PF00918; Gastrin; 1.
DR SMART; SM00029; 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..20
FT /evidence="ECO:0000255"
FT PROPEP 21..103
FT /evidence="ECO:0000255"
FT /id="PRO_0000010603"
FT PEPTIDE 104..111
FT /note="Cholecystokinin"
FT /id="PRO_0000010604"
FT PROPEP 115..123
FT /evidence="ECO:0000255"
FT /id="PRO_0000010605"
FT MOD_RES 105
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 111
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250"
SQ SEQUENCE 123 AA; 13943 MW; FBDCC9E150A98540 CRC64;
MYSGICICLL LAMLSASSKA HQSEDAVVTE MDQLTLSQLP RYARASSAGQ KKSFQRTDGD
QRSNIGNVLV KYLQQSRKAG PSGRYVVLPN RPIFDQPHRI NDRDYMGWMD FGRRSAEEYE
YSS
//