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UniProtKB/Swiss-Prot entry P50145

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CCKN2_XENLA
Primary accession number P50145
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 1, 1996 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 48)
Name and origin of the protein
Protein name Cholecystokinin type 2 [Precursor]
Synonyms None
Contains Cholecystokinin
     (CCK)
Gene name
Name: cck-B
From
Xenopus laevis (African clawed frog) [TaxID: 8355] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=7669225 [NCBI, ExPASy, EBI, Israel, Japan]
Wechselberger C., Kreil G.;
"Structure of two cDNAs encoding cholecystokinin precursors from the brain of Xenopus laevis.";
J. Mol. Endocrinol. 14:357-364(1995).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Z47558; CAA87639.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR I51605; I51605.
RefSeq NP_001079304.1; -.
UniGene Xl.1147
3D structure databases
ModBase P50145.
Family and domain databases
InterPro IPR015499; CCK.
IPR001651; Gastrin.
IPR013152; Gastrin_CCK_CS.
Graphical view of domain structure.
PANTHER PTHR10786; CCK; 1.
Pfam PF00918; Gastrin; 1.
Pfam graphical view of domain structure.
SMART SM00029; GASTRIN; 1.
SMART graphical view of domain structure.
PROSITE PS00259; GASTRIN; 1.
BLOCKS P50145.
Genome annotation databases
GeneID 378612; -.
KEGG xla:378612; -.
Phylogenomic databases
HOVERGEN P50145; -.
Other
ProtoNet P50145.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amidation; Cleavage on pair of basic residues; Hormone; Secreted; Signal; Sulfation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    20  20     Potential. 
PROPEP   21   108  88     Potential. PRO_0000010606
PEPTIDE   109   116  8     Cholecystokinin. PRO_0000010607
PROPEP   120   128  9     Potential. PRO_0000010608
MOD_RES   110   110        Sulfotyrosine (By similarity). 
MOD_RES   116   116        Phenylalanine amide (By similarity). 
Sequence information
Length: 128 AA [This is the length of the unprocessed precursor] Molecular weight: 14201 Da [This is the MW of the unprocessed precursor] CRC64: EA984DFECADFEDA7 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MCSGVCICLL LAMLSASSKA HQATGSLGED AVGTEMDQLN LSQLPRYARA SSAGQKKSFQ 

        70         80         90        100        110        120 
RTDGDQRSNI GNALVKYLQQ SRKAGPSGRY VVLPNRPIFD QSHRINDRDY MGWMDFGRRS 


AEEYEYSS
P50145 in FASTA format

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