Reviewed, UniProtKB/Swiss-Prot P01357 (CAER4_XENLA)

Names and origin

Protein names	Recommended name:     Preprocaerulein type-4 Alternative name(s):     Preprocaerulein type IV 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	233 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	Repeat Signal
Molecular function	Amphibian defense peptide
PTM	Amidation Cleavage on pair of basic residues Pyrrolidone carboxylic acid 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_0000010513
	Peptide	73 – 82	10	Caerulein		PRO_0000010514
	Propeptide	86 – 87	2			PRO_0000010515
	Peptide	88 – 97	10	Caerulein		PRO_0000010516
	Propeptide	101 – 151	51			PRO_0000010517
	Peptide	152 – 161	10	Caerulein		PRO_0000010518
	Propeptide	165 – 215	51			PRO_0000010519
	Peptide	216 – 225	10	Caerulein		PRO_0000010520
	Propeptide	229 – 233	5			PRO_0000010521
Amino acid modifications
	Modified residue	73	1	Pyrrolidone carboxylic acid
	Modified residue	76	1	Sulfotyrosine
	Modified residue	82	1	Phenylalanine amide
	Modified residue	88	1	Pyrrolidone carboxylic acid
	Modified residue	91	1	Sulfotyrosine
	Modified residue	97	1	Phenylalanine amide
	Modified residue	152	1	Pyrrolidone carboxylic acid
	Modified residue	155	1	Sulfotyrosine
	Modified residue	161	1	Phenylalanine amide
	Modified residue	216	1	Pyrrolidone carboxylic acid
	Modified residue	219	1	Sulfotyrosine
	Modified residue	225	1	Phenylalanine amide

Sequences

	Sequence		Length	Mass (Da)
	P01357-1 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: 8BDE518027EC2FF1	FASTA	233	25,953
	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

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]	"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 [MRNA] OF 137-233. Tissue: Skin.
[3]	"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, PYROGLUTAMATE FORMATION AT GLN-73; GLN-88; GLN-152 AND GLN-216, SULFATION. Tissue: Skin secretion.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M12495 mRNA. Translation: AAA49685.1. X01810 mRNA. Translation: CAA25953.1.
PIR	SCXL. C23364.
RefSeq	NP_001080990.1.
UniGene	Xl.76213
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	394315.
KEGG	xla:394315.
Phylogenomic databases
HOVERGEN	P01357.
Family and domain databases
InterPro	IPR001651. Gastrin. IPR013152. Gastrin/cholecystokinin_CS. [Graphical view]
Pfam	PF00918. Gastrin. 2 hits. [Graphical view]
SMART	SM00029. GASTRIN. 4 hits. [Graphical view]
PROSITE	PS00259. GASTRIN. 4 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CAER4_XENLA

Accession

Primary (citable) accession number: P01357

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
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