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CCKNA_XENLA
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   03-AUG-2022, entry version 75.
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   CTD; 378611; -.
DR   Xenbase; XB-GENE-6252398; cck.S.
DR   OMA; QPHRIND; -.
DR   OrthoDB; 1524113at2759; -.
DR   Proteomes; UP000186698; Chromosome 6S.
DR   Bgee; 378611; 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..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
 
 
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