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Reviewed, UniProtKB/Swiss-Prot P05224 (CAER3_XENLA)

Last modified June 16, 2009. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Preprocaerulein type-3
Alternative name(s):
    Preprocaerulein type III
Cleaved into the following chain:
    1- Recommended name:
            Caerulein
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraMesobatrachiaPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length169 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

The pharmacological activities of caerulein are quite similar to the physiological activities of gastrin and related peptides.

Subcellular location

Secreted.

Tissue specificity

Expressed by the skin glands.

Sequence similarities

Belongs to the gastrin/cholecystokinin family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainRepeat
Signal
   Molecular functionAmphibian defense peptide
   PTMAmidation
Cleavage on pair of basic residues
Sulfation
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processdefense response

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionhormone activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Propeptide27 – 7246
PRO_0000010497
Peptide73 – 8210Caerulein
PRO_0000010498
Propeptide86 – 872
PRO_0000010499
Peptide88 – 9710Caerulein
PRO_0000010500
Propeptide101 – 15151
PRO_0000010501
Peptide152 – 16110Caerulein
PRO_0000010502
Propeptide165 – 1695
PRO_0000010503

Amino acid modifications

Modified residue761Sulfotyrosine
Modified residue821Phenylalanine amide
Modified residue911Sulfotyrosine
Modified residue971Phenylalanine amide
Modified residue1551Sulfotyrosine
Modified residue1611Phenylalanine amide

Sequences

Sequence LengthMass (Da)Tools
P05224-1 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 8B8FB99E44018AF7

FASTA16918,785
        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 

« Hide

References

[1]"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."
Richter K., Egger R., Kreil G.
J. Biol. Chem. 261:3676-3680(1986) [PubMed: 3753978] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Skin.
[2]"An unusual repetitive structure of caerulein mRNA from the skin of Xenopus laevis."
Wakabayashi T., Kato H., Tachibana S.
Gene 31:295-299(1984) [PubMed: 6526274] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 64-169.
Tissue: Skin.
[3]"Conserved exon-intron organization in two different caerulein precursor genes of Xenopus laevis. Additional detection of an exon potentially coding for a new peptide."
Vlasak R., Wiborg O., Richter K., Burgschwaiger S., Vuust J., Kreil G.
Eur. J. Biochem. 169:53-58(1987) [PubMed: 3678233] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1-28.
[4]"Presence of caerulein in extracts of the skin of Leptodactylus pentadactylus labyrinthicus and of Xenopus laevis."
Anastasi A., Bertaccini G., Cei J.M., de Daro G., Erspamer V., Impicciatore M., Roseghini M.
Br. J. Pharmacol. 38:221-228(1970) [PubMed: 5413288] [Abstract]
Cited for: PROTEIN SEQUENCE OF CAERULEIN.
Tissue: Skin secretion.

Cross-references

Sequence databases

M64803 expand/collapse EMBL AC list , M27986, M27987, M27978, M64800, M64802 Genomic DNA. Translation: AAA49687.1.
M12494 mRNA. Translation: AAA49684.1.
M12455 mRNA. Translation: AAA49690.1.
PIRD23364.
UniGeneXl.76213

3D structure databases

ModBaseSearch...

Phylogenomic databases

HOVERGENP05224.

Family and domain databases

InterProIPR001651. Gastrin.
IPR013152. Gastrin/cholecystokinin_CS.
[Graphical view]
PfamPF00918. Gastrin. 2 hits.
[Graphical view]
SMARTSM00029. GASTRIN. 3 hits.
[Graphical view]
PROSITEPS00259. GASTRIN. 3 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCAER3_XENLA
AccessionPrimary (citable) accession number: P05224
Secondary accession number(s): P87486
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: June 16, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectXenopus annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents