ID   CAER3_XENLA             Reviewed;         169 AA.
AC   P05224; P87486;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   04-NOV-2008, entry version 54.
DE   RecName: Full=Preprocaerulein type-3;
DE   AltName: Full=Preprocaerulein type III;
DE   Contains:
DE     RecName: Full=Caerulein;
DE   Flags: Precursor;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae;
OC   Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skin;
RX   MEDLINE=86140161; PubMed=3753978;
RA   Richter K., Egger R., Kreil G.;
RT   "Sequence of preprocaerulein cDNAs cloned from skin of Xenopus laevis.
RT   A small family of precursors containing one, three, or four copies of
RT   the final product.";
RL   J. Biol. Chem. 261:3676-3680(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 64-169.
RC   TISSUE=Skin;
RX   MEDLINE=85128451; PubMed=6526274; DOI=10.1016/0378-1119(84)90225-7;
RA   Wakabayashi T., Kato H., Tachibana S.;
RT   "An unusual repetitive structure of caerulein mRNA from the skin of
RT   Xenopus laevis.";
RL   Gene 31:295-299(1984).
RN   [3]
RP   NUCLEOTIDE SEQUENCE OF 1-28.
RX   MEDLINE=88055051; PubMed=3678233;
RA   Vlasak R., Wiborg O., Richter K., Burgschwaiger S., Vuust J.,
RA   Kreil G.;
RT   "Conserved exon-intron organization in two different caerulein
RT   precursor genes of Xenopus laevis. Additional detection of an exon
RT   potentially coding for a new peptide.";
RL   Eur. J. Biochem. 169:53-58(1987).
RN   [4]
RP   PROTEIN SEQUENCE OF CAERULEIN.
RC   TISSUE=Skin secretion;
RX   MEDLINE=70106037; PubMed=5413288;
RA   Anastasi A., Bertaccini G., Cei J.M., de Daro G., Erspamer V.,
RA   Impicciatore M., Roseghini M.;
RT   "Presence of caerulein in extracts of the skin of Leptodactylus
RT   pentadactylus labyrinthicus and of Xenopus laevis.";
RL   Br. J. Pharmacol. 38:221-228(1970).
CC   -!- FUNCTION: The pharmacological activities of caerulein are quite
CC       similar to the physiological activities of gastrin and related
CC       peptides.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC   -!- SIMILARITY: Belongs to the gastrin/cholecystokinin family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M64803; AAA49687.1; -; Genomic_DNA.
DR   EMBL; M27986; AAA49687.1; JOINED; Genomic_DNA.
DR   EMBL; M27987; AAA49687.1; JOINED; Genomic_DNA.
DR   EMBL; M27978; AAA49687.1; JOINED; Genomic_DNA.
DR   EMBL; M64800; AAA49687.1; JOINED; Genomic_DNA.
DR   EMBL; M64802; AAA49687.1; JOINED; Genomic_DNA.
DR   EMBL; M12494; AAA49684.1; -; mRNA.
DR   EMBL; M12455; AAA49690.1; -; mRNA.
DR   PIR; D23364; D23364.
DR   UniGene; Xl.76213; -.
DR   HOVERGEN; P05224; -.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   InterPro; IPR001651; Gastrin.
DR   InterPro; IPR013152; Gastrin_CCK_CS.
DR   Pfam; PF00918; Gastrin; 2.
DR   SMART; SM00029; GASTRIN; 3.
DR   PROSITE; PS00259; GASTRIN; 3.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide;
KW   Cleavage on pair of basic residues; Direct protein sequencing; Repeat;
KW   Secreted; Signal; Sulfation.
FT   SIGNAL        1     26       Potential.
FT   PROPEP       27     72
FT                                /FTId=PRO_0000010497.
FT   PEPTIDE      73     82       Caerulein.
FT                                /FTId=PRO_0000010498.
FT   PROPEP       86     87
FT                                /FTId=PRO_0000010499.
FT   PEPTIDE      88     97       Caerulein.
FT                                /FTId=PRO_0000010500.
FT   PROPEP      101    151
FT                                /FTId=PRO_0000010501.
FT   PEPTIDE     152    161       Caerulein.
FT                                /FTId=PRO_0000010502.
FT   PROPEP      165    169
FT                                /FTId=PRO_0000010503.
FT   MOD_RES      76     76       Sulfotyrosine.
FT   MOD_RES      82     82       Phenylalanine amide.
FT   MOD_RES      91     91       Sulfotyrosine.
FT   MOD_RES      97     97       Phenylalanine amide.
FT   MOD_RES     155    155       Sulfotyrosine.
FT   MOD_RES     161    161       Phenylalanine amide.
SQ   SEQUENCE   169 AA;  18785 MW;  8B8FB99E44018AF7 CRC64;
     MFKGILLCVL FAVLSANPLS QPEGFADEER DVRGLASLLG KALKAGLKIG THFLGGAPQQ
     REANDERRFA DGQQDYTGWM DFGRRDGQQD YTGWMDFGRR DDEDDVNERD VRGFGSFLGK
     ALKAALKIGA NALGGAPQQR EANDERRFAD GQQDYTGWMD FGRRNGEDD
//