[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 [MRNA] OF 137-233. TISSUE=Skin; 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).
[3]	PROTEIN SEQUENCE OF CAERULEIN, PYROGLUTAMATE FORMATION AT GLN-73; GLN-88; GLN-152 AND GLN-216, AND SULFATION. 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

M12495; AAA49685.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X01810; CAA25953.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

C23364; SCXL.

NP_001080990.1; -.

3D structure databases

ModBase

P01357.

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; 2.
Pfam graphical view of domain structure.

SMART

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

PS00259; GASTRIN; 4.

Genome annotation databases

GeneID

394315; -.

KEGG

xla:394315; -.

Phylogenomic databases

HOVERGEN

P01357; -.

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; Pyrrolidone carboxylic acid; Repeat; Secreted; Signal; Sulfation.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 26`	`26`	`Potential.`
`PROPEP`	`27 72`	`46`		`PRO_0000010513`
`PEPTIDE`	`73 82`	`10`	`Caerulein.`	`PRO_0000010514`
`PROPEP`	`86 87`	`2`		`PRO_0000010515`
`PEPTIDE`	`88 97`	`10`	`Caerulein.`	`PRO_0000010516`
`PROPEP`	`101 151`	`51`		`PRO_0000010517`
`PEPTIDE`	`152 161`	`10`	`Caerulein.`	`PRO_0000010518`
`PROPEP`	`165 215`	`51`		`PRO_0000010519`
`PEPTIDE`	`216 225`	`10`	`Caerulein.`	`PRO_0000010520`
`PROPEP`	`229 233`	`5`		`PRO_0000010521`
`MOD_RES`	`73 73`		`Pyrrolidone carboxylic acid.`
`MOD_RES`	`76 76`		`Sulfotyrosine.`
`MOD_RES`	`82 82`		`Phenylalanine amide.`
`MOD_RES`	`88 88`		`Pyrrolidone carboxylic acid.`
`MOD_RES`	`91 91`		`Sulfotyrosine.`
`MOD_RES`	`97 97`		`Phenylalanine amide.`
`MOD_RES`	`152 152`		`Pyrrolidone carboxylic acid.`
`MOD_RES`	`155 155`		`Sulfotyrosine.`
`MOD_RES`	`161 161`		`Phenylalanine amide.`
`MOD_RES`	`216 216`		`Pyrrolidone carboxylic acid.`
`MOD_RES`	`219 219`		`Sulfotyrosine.`
`MOD_RES`	`225 225`		`Phenylalanine amide.`

Sequence information

Length: 233 AA [This is the length of the unprocessed precursor]

Molecular weight: 25953 Da [This is the MW of the unprocessed precursor]

CRC64: 8BDE518027EC2FF1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MFKGILLCVL FAVLSANPLS QPEGFADEER DVRGLASLLG KALKATLKIG THFLGGAPQQ 

        70         80         90        100        110        120 
REANDERRFA DGQQDYTGWM DFGRRDGQQD YTGWMDFGRR DDEDDVHERD VRGFGSFLGK 

       130        140        150        160        170        180 
ALKAALKIGA NALGGAPQQR EANDERRFAD GQQDYTGWMD FGRRDDEDDV NERDVRGFGS 

       190        200        210        220        230 
FLGKALKAAL KIGANALGGS PQQREANDER RFADGQQDYT GWMDFGRRNG EDD

P01357 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