ID   CCKNB_XENLA             Reviewed;         128 AA.
AC   P50145;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Cholecystokinin B;
DE   AltName: Full=Cholecystokinin type 2;
DE   Contains:
DE     RecName: Full=Cholecystokinin;
DE              Short=CCK;
DE   Flags: Precursor;
GN   Name=cck-b;
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).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Brain and gastrointestinal tract.
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; Z47558; CAA87639.1; -; mRNA.
DR   PIR; I51605; I51605.
DR   RefSeq; NP_001079304.1; NM_001085835.1.
DR   AlphaFoldDB; P50145; -.
DR   GeneID; 378612; -.
DR   KEGG; xla:378612; -.
DR   CTD; 378612; -.
DR   Xenbase; XB-GENE-865926; cck.L.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 378612; Expressed in brain and 6 other tissues.
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; Reference proteome;
KW   Secreted; Signal; Sulfation.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..108
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000010606"
FT   PEPTIDE         109..116
FT                   /note="Cholecystokinin"
FT                   /id="PRO_0000010607"
FT   PROPEP          120..128
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000010608"
FT   REGION          47..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         110
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         116
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   128 AA;  14201 MW;  EA984DFECADFEDA7 CRC64;
     MCSGVCICLL LAMLSASSKA HQATGSLGED AVGTEMDQLN LSQLPRYARA SSAGQKKSFQ
     RTDGDQRSNI GNALVKYLQQ SRKAGPSGRY VVLPNRPIFD QSHRINDRDY MGWMDFGRRS
     AEEYEYSS