[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Skin; DOI=10.1016/0378-1119(84)90225-7; PubMed=6526274 [NCBI, ExPASy, EBI, Israel, Japan] Wakabayashi T., Kato H., Tachibana S.; "An unusual repetitive structure of caerulein mRNA from the skin of Xenopus laevis."; Gene 31:295-299(1984).
[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

M12453; AAA49689.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

P05225.

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.

Phylogenomic databases

HOVERGEN

P05225; -.

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; Sulfation.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`PROPEP`	`<1 9`	`>9`		`PRO_0000010522`
`PEPTIDE`	`10 19`	`10`	`Caerulein.`	`PRO_0000010523`
`PROPEP`	`23 73`	`51`		`PRO_0000010524`
`PEPTIDE`	`74 83`	`10`	`Caerulein.`	`PRO_0000010525`
`PROPEP`	`87 137`	`51`		`PRO_0000010526`
`PEPTIDE`	`138 147`	`10`	`Caerulein.`	`PRO_0000010527`
`PROPEP`	`151 152`	`2`		`PRO_0000010528`
`PEPTIDE`	`153 162`	`10`	`Caerulein.`	`PRO_0000010529`
`PROPEP`	`166 187`	`22`		`PRO_0000010530`
`MOD_RES`	`13 13`		`Sulfotyrosine.`
`MOD_RES`	`19 19`		`Phenylalanine amide.`
`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.`
`NON_TER`	`1 1`
`NON_TER`	`187 187`

Sequence information

Length: 187 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 21242 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 15738A4F3025E392 [This is a checksum on the sequence]

        10         20         30         40         50         60 
NDERRFADGQ QDYTGWMDFG RRDDEDDVNE RDVRGFGSFL GKALKAALKI GANALGGSPQ 

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

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


SFLGKAL

P05225 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