[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Skin; DOI=10.1093/nar/13.6.1817; PubMed=4000945 [NCBI, ExPASy, EBI, Israel, Japan] Wakabayashi T., Kato H., Tachibana S.; "Complete nucleotide sequence of mRNA for caerulein precursor from Xenopus skin: the mRNA contains an unusual repetitive structure."; Nucleic Acids Res. 13:1817-1828(1985).
[2]	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

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.
SIMILARITY: Belongs to the gastrin/cholecystokinin family.

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

X02310; CAA26180.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

P05226.

Ontologies

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; 3.
Pfam graphical view of domain structure.

SMART

SM00029; GASTRIN; 4.
SMART graphical view of domain structure.

PS00259; GASTRIN; 4.

Phylogenomic databases

HOVERGEN

P05226; -.

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; Repeat; Secreted; Signal; Sulfation.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 26`	`26`	`Potential.`
`PROPEP`	`27 73`	`47`		`PRO_0000010504`
`PEPTIDE`	`74 83`	`10`	`Caerulein.`	`PRO_0000010505`
`PROPEP`	`87 137`	`51`		`PRO_0000010506`
`PEPTIDE`	`138 147`	`10`	`Caerulein.`	`PRO_0000010507`
`PROPEP`	`151 152`	`2`		`PRO_0000010508`
`PEPTIDE`	`153 162`	`10`	`Caerulein.`	`PRO_0000010509`
`PROPEP`	`166 216`	`51`		`PRO_0000010510`
`PEPTIDE`	`217 226`	`10`	`Caerulein.`	`PRO_0000010511`
`PROPEP`	`230 234`	`5`		`PRO_0000010512`
`MOD_RES`	`77 77`		`Sulfotyrosine.`
`MOD_RES`	`83 83`		`Phenylalanine amide.`
`MOD_RES`	`141 141`		`Sulfotyrosine.`
`MOD_RES`	`147 147`		`Phenylalanine amide.`
`MOD_RES`	`156 156`		`Sulfotyrosine.`
`MOD_RES`	`162 162`		`Phenylalanine amide.`
`MOD_RES`	`220 220`		`Sulfotyrosine.`
`MOD_RES`	`226 226`		`Phenylalanine amide.`

Sequence information

Length: 234 AA [This is the length of the unprocessed precursor]

Molecular weight: 26055 Da [This is the MW of the unprocessed precursor]

CRC64: 052D82F910541147 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MFKGILLCVL FAVLSANPLS QPEGFADEEE RDVRGLASLL GKALKAALKI GANALGGSPQ 

        70         80         90        100        110        120 
QREANDERRF ADGQQDYTGW MDFGRRDDED DVNERDVRGF GSFLGKALKA GLKIGTHFLG 

       130        140        150        160        170        180 
GAPQQREAND ERRFADGQQD YTGWMDFGRR DGQQDYTGWM DFGRRDDEDD VHERDVRGFG 

       190        200        210        220        230 
SFLGKALKAA LKIGANALGG SPQQREANDE RRFADGQQDY TGWMDFGRRN GEDD

P05226 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 submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools