Reviewed, UniProtKB/Swiss-Prot P05222 (CAER1_XENLA)

Names and origin

Protein names	Recommended name:     Preprocaerulein type-1 Alternative name(s):     Preprocaerulein type I 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	188 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	Secreted.
Tissue specificity	Expressed by the skin glands.
Sequence similarities	Belongs to the gastrin/cholecystokinin family.

Ontologies

Keywords
Cellular component	Secreted
Domain	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 – 170	144	Ref.6		PRO_0000010493
	Peptide	171 – 180	10	Caerulein		PRO_0000010494
	Propeptide	184 – 188	5			PRO_0000010495
Amino acid modifications
	Modified residue	174	1	Sulfotyrosine
	Modified residue	180	1	Phenylalanine amide
Natural variations
	Natural variant	57	1	A → S in clone PXC204.
	Natural variant	85	1	A → G in clone PXC204.
	Natural variant	106 – 107	2	TP → SL in clone PXC204.
	Natural variant	112	1	A → V in clone PXC204.
Experimental info
	Sequence conflict	75	1	Missing Ref.2
	Sequence conflict	147	1	I → SKLEHSF Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P05222-1 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: 716819DAAD46FC0A	FASTA	188	20,505
	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

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]	"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.
[3]	"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." Kuchler K., Kreil G., Sures I. Eur. J. Biochem. 179:281-285(1989) [PubMed: 2465151] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1-49.
[4]	"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 55-188 (CLONE PXC204).
[5]	"Biosynthesis of caerulein in the skin of Xenopus laevis: partial sequences of precursors as deduced from cDNA clones." Hoffmann W., Bach T.C., Seliger H., Kreil G. EMBO J. 2:111-114(1983) [PubMed: 11894896] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 115-188 (CLONE PUF262).
[6]	"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 171-180. Tissue: Skin secretion.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M12304 mRNA. Translation: AAA49686.1. M12454 mRNA. Translation: AAA49691.1. M27984 , M27980, M27981, M27982, M27983 Genomic DNA. Translation: AAA49688.1. K00930 mRNA. Translation: AAA49682.1.
PIR	A23364.
RefSeq	NP_001081262.1.
UniGene	Xl.76006
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	397740.
KEGG	xla:397740.
Phylogenomic databases
HOVERGEN	P05222.
Family and domain databases
InterPro	IPR001651. Gastrin. IPR013152. Gastrin/cholecystokinin_CS. [Graphical view]
Pfam	PF00918. Gastrin. 1 hit. [Graphical view]
PROSITE	PS00259. GASTRIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CAER1_XENLA

Accession

Primary (citable) accession number: P05222
Secondary accession number(s): P87485, Q91722

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	June 16, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Xenopus annotation project