ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P05222


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name CAER1_XENLA
Primary accession number P05222
Secondary accession numbers P87485 Q91722
Integrated into Swiss-Prot on August 13, 1987
Sequence was last modified on August 13, 1987 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 60)
Name and origin of the protein
Protein name Preprocaerulein type-1 [Precursor]
Synonym Preprocaerulein type I
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.
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).
[3]
NUCLEOTIDE SEQUENCE OF 1-49.
PubMed=2465151 [NCBI, ExPASy, EBI, Israel, Japan]
Kuchler K., Kreil G., Sures I.;
"The genes for the frog skin peptides GLa, xenopsin, levitide and caerulein contain a homologous export exon encoding a signal sequence and part of an amphiphilic peptide.";
Eur. J. Biochem. 179:281-285(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 55-188 (CLONE PXC204).
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).
[5]
NUCLEOTIDE SEQUENCE OF 115-188 (CLONE PUF262).
PubMed=11894896 [NCBI, ExPASy, EBI, Israel, Japan]
Hoffmann W., Bach T.C., Seliger H., Kreil G.;
"Biosynthesis of caerulein in the skin of Xenopus laevis: partial sequences of precursors as deduced from cDNA clones.";
EMBO J. 2:111-114(1983).
[6]
PROTEIN SEQUENCE OF 171-180.
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
M12304; AAA49686.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M12454; AAA49691.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M27984; AAA49688.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M27980; AAA49688.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M27981; AAA49688.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M27982; AAA49688.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M27983; AAA49688.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K00930; AAA49682.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A23364; A23364.
RefSeq NP_001081262.1; -.
UniGene Xl.76006
3D structure databases
ModBase P05222.
Ontologies
GO
GO:0006952; Biological process: defense response (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001651; Gastrin.
IPR013152; Gastrin_CCK_CS.
Graphical view of domain structure.
Pfam PF00918; Gastrin; 1.
Pfam graphical view of domain structure.
PROSITE PS00259; GASTRIN; 1.
BLOCKS P05222.
ProtoNet P05222.
Genome annotation databases
GeneID 397740; -.
KEGG xla:397740; -.
Phylogenomic databases
HOVERGEN P05222; -.
Other
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; 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   170  144      PRO_0000010493
PEPTIDE   171   180  10     Caerulein. PRO_0000010494
PROPEP   184   188  5      PRO_0000010495
MOD_RES   174   174        Sulfotyrosine. 
MOD_RES   180   180        Phenylalanine amide. 
VARIANT   57    57  1     A -> S (in clone PXC204). 
VARIANT   85    85  1     A -> G (in clone PXC204). 
VARIANT   106   107  2     TP -> SL (in clone PXC204). 
VARIANT   112   112  1     A -> V (in clone PXC204). 
CONFLICT   75    75        Missing (in Ref. 2). 
CONFLICT   147   147        I -> SKLEHSF (in Ref. 2). 
Sequence information
Length: 188 AA [This is the length of the unprocessed precursor] Molecular weight: 20505 Da [This is the MW of the unprocessed precursor] CRC64: 716819DAAD46FC0A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MFKGILLCVL FAVLSANPLS QPEGFADEER DVRGLASFLG KALKAGLKIG AHLLGGAPQQ 

        70         80         90        100        110        120 
REANDERRFA DDDDDVNERD VRGFASFLGK ALKAALKIGA NMLGGTPQQR EANDERRFAD 

       130        140        150        160        170        180 
DEDDVNERDV RGFGSFLGKA LKAALKIGAN ALGGSPQQRE ANDERRFADG QQDYTGWMDF 


GRRNGEDD 

P05222 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!