Reviewed,
UniProtKB/Swiss-Prot P05224 (CAER3_XENLA)
Last modified
June 16, 2009.
Version 58.
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 names | Recommended name: Preprocaerulein type-3 Alternative name(s): Preprocaerulein type III Cleaved into the following chain: 1- Recommended name: Caerulein |
| Organism | Xenopus laevis (African clawed frog) |
| Taxonomic identifier | 8355 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus |
Protein attributes
| Sequence length | 169 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence 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 | |
| Tissue specificity | Expressed by the skin glands. |
| Sequence similarities | Belongs to the gastrin/cholecystokinin family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Domain | Repeat Signal |
| Molecular function | Amphibian defense peptide |
| PTM | Amidation Cleavage on pair of basic residues Sulfation |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | defense response Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | hormone activity Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 26 | 26 | Potential | ||||||
| Propeptide | 27 – 72 | 46 | PRO_0000010497 | ||||||
| Peptide | 73 – 82 | 10 | Caerulein | PRO_0000010498 | |||||
| Propeptide | 86 – 87 | 2 | PRO_0000010499 | ||||||
| Peptide | 88 – 97 | 10 | Caerulein | PRO_0000010500 | |||||
| Propeptide | 101 – 151 | 51 | PRO_0000010501 | ||||||
| Peptide | 152 – 161 | 10 | Caerulein | PRO_0000010502 | |||||
| Propeptide | 165 – 169 | 5 | PRO_0000010503 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 76 | 1 | Sulfotyrosine | ||||||
| Modified residue | 82 | 1 | Phenylalanine amide | ||||||
| Modified residue | 91 | 1 | Sulfotyrosine | ||||||
| Modified residue | 97 | 1 | Phenylalanine amide | ||||||
| Modified residue | 155 | 1 | Sulfotyrosine | ||||||
| Modified residue | 161 | 1 | Phenylalanine amide | ||||||
Sequences
| ||||||||||||||||||
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 M64802 Genomic DNA. Translation: AAA49687.1. M12494 mRNA. Translation: AAA49684.1. M12455 mRNA. Translation: AAA49690.1. | |
| PIR | D23364. |
| UniGene | Xl.76213 |
3D structure databases | |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | P05224. |
Family and domain databases | |
| InterPro | IPR001651. Gastrin. IPR013152. Gastrin/cholecystokinin_CS. [Graphical view] |
| Pfam | PF00918. Gastrin. 2 hits. [Graphical view] |
| SMART | SM00029. GASTRIN. 3 hits. [Graphical view] |
| PROSITE | PS00259. GASTRIN. 3 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CAER3_XENLA | ||||||||
| Accession | Primary (citable) accession number: P05224 Secondary accession number(s): P87486 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Xenopus annotation project | ||||||||

Clusters with


