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UniProtKB/Swiss-Prot entry P05224


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

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Entry information
Entry name CAER3_XENLA
Primary accession number P05224
Secondary accession number P87486
Integrated into Swiss-Prot on August 13, 1987
Sequence was last modified on August 13, 1987 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 53)
Name and origin of the protein
Protein name Preprocaerulein type-3 [Precursor]
Synonym Preprocaerulein type III
Contains Caerulein
Gene name None
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 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Skin;
PubMed=3753978 [NCBI, ExPASy, EBI, Israel, Japan]
Richter K., Egger R., Kreil G.;
"Sequence of preprocaerulein cDNAs cloned from skin of Xenopus laevis. A small family of precursors containing one, three, or four copies of the final product.";
J. Biol. Chem. 261:3676-3680(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 64-169.
TISSUE=Skin;
DOI=10.1016/0378-1119(84)90225-7; PubMed=6526274 [NCBI, ExPASy, EBI, Israel, Japan]
Wakabayashi T., Kato H., Tachibana S.;
"An unusual repetitive structure of caerulein mRNA from the skin of Xenopus laevis.";
Gene 31:295-299(1984).
[3]
NUCLEOTIDE SEQUENCE OF 1-28.
PubMed=3678233 [NCBI, ExPASy, EBI, Israel, Japan]
Vlasak R., Wiborg O., Richter K., Burgschwaiger S., Vuust J., Kreil G.;
"Conserved exon-intron organization in two different caerulein precursor genes of Xenopus laevis. Additional detection of an exon potentially coding for a new peptide.";
Eur. J. Biochem. 169:53-58(1987).
[4]
PROTEIN SEQUENCE OF CAERULEIN.
TISSUE=Skin secretion;
PubMed=5413288 [NCBI, ExPASy, EBI, Israel, Japan]
Anastasi A., Bertaccini G., Cei J.M., de Daro G., Erspamer V., Impicciatore M., Roseghini M.;
"Presence of caerulein in extracts of the skin of Leptodactylus pentadactylus labyrinthicus and of Xenopus laevis.";
Br. J. Pharmacol. 38:221-228(1970).
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
M64803; AAA49687.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M27986; AAA49687.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M27987; AAA49687.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M27978; AAA49687.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M64800; AAA49687.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M64802; AAA49687.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M12494; AAA49684.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M12455; AAA49690.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR D23364; D23364.
UniGene Xl.76213
3D structure databases
ModBase P05224.
Family and domain databases
InterPro IPR001651; Gastrin.
IPR013152; Gastrin_CCK_CS.
Graphical view of domain structure.
Pfam PF00918; Gastrin; 2.
Pfam graphical view of domain structure.
SMART SM00029; GASTRIN; 3.
SMART graphical view of domain structure.
PROSITE PS00259; GASTRIN; 3.
BLOCKS P05224.
Phylogenomic databases
HOVERGEN P05224; -.
Other
ProtoNet P05224.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amidation; Amphibian defense peptide; Cleavage on pair of basic residues; Direct protein sequencing; Repeat; Secreted; Signal; Sulfation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    26  26     Potential. 
PROPEP   27    72  46      PRO_0000010497
PEPTIDE   73    82  10     Caerulein. PRO_0000010498
PROPEP   86    87  2      PRO_0000010499
PEPTIDE   88    97  10     Caerulein. PRO_0000010500
PROPEP   101   151  51      PRO_0000010501
PEPTIDE   152   161  10     Caerulein. PRO_0000010502
PROPEP   165   169  5      PRO_0000010503
MOD_RES   76    76        Sulfotyrosine. 
MOD_RES   82    82        Phenylalanine amide. 
MOD_RES   91    91        Sulfotyrosine. 
MOD_RES   97    97        Phenylalanine amide. 
MOD_RES   155   155        Sulfotyrosine. 
MOD_RES   161   161        Phenylalanine amide. 
Sequence information
Length: 169 AA [This is the length of the unprocessed precursor] Molecular weight: 18785 Da [This is the MW of the unprocessed precursor] CRC64: 8B8FB99E44018AF7 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MFKGILLCVL FAVLSANPLS QPEGFADEER DVRGLASLLG KALKAGLKIG THFLGGAPQQ 

        70         80         90        100        110        120 
REANDERRFA DGQQDYTGWM DFGRRDGQQD YTGWMDFGRR DDEDDVNERD VRGFGSFLGK 

       130        140        150        160 
ALKAALKIGA NALGGAPQQR EANDERRFAD GQQDYTGWMD FGRRNGEDD 

P05224 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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