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   25-MAY-2022, entry version 87.
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; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skin;
RX   PubMed=3753978; DOI=10.1016/s0021-9258(17)35700-9;
RA   Richter K., Egger R., Kreil G.;
RT   "Sequence of preprocaerulein cDNAs cloned from skin of Xenopus laevis. A
RT   small family of precursors containing one, three, or four copies of the
RT   final product.";
RL   J. Biol. Chem. 261:3676-3680(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 64-169.
RC   TISSUE=Skin;
RX   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 Xenopus
RT   laevis.";
RL   Gene 31:295-299(1984).
RN   [3]
RP   NUCLEOTIDE SEQUENCE OF 1-28.
RX   PubMed=3678233; DOI=10.1111/j.1432-1033.1987.tb13579.x;
RA   Vlasak R., Wiborg O., Richter K., Burgschwaiger S., Vuust J., Kreil G.;
RT   "Conserved exon-intron organization in two different caerulein precursor
RT   genes of Xenopus laevis. Additional detection of an exon potentially coding
RT   for a new peptide.";
RL   Eur. J. Biochem. 169:53-58(1987).
RN   [4]
RP   PROTEIN SEQUENCE OF CAERULEIN.
RC   TISSUE=Skin secretion;
RX   PubMed=5413288; DOI=10.1111/j.1476-5381.1970.tb10351.x;
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 similar
CC       to the physiological activities of gastrin and related peptides.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC   -!- SIMILARITY: Belongs to the gastrin/cholecystokinin family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) 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   AlphaFoldDB; P05224; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   InterPro; IPR015499; CCK-like.
DR   InterPro; IPR001651; Gastrin/CCK.
DR   InterPro; IPR013152; Gastrin/cholecystokinin_CS.
DR   PANTHER; PTHR10786; PTHR10786; 3.
DR   Pfam; PF00918; Gastrin; 1.
DR   PROSITE; PS00259; GASTRIN; 3.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Reference proteome; Repeat; Secreted; Signal;
KW   Sulfation.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   PROPEP          27..72
FT                   /evidence="ECO:0000269|PubMed:5413288"
FT                   /id="PRO_0000010497"
FT   PEPTIDE         73..82
FT                   /note="Caerulein"
FT                   /evidence="ECO:0000269|PubMed:5413288"
FT                   /id="PRO_0000010498"
FT   PROPEP          86..87
FT                   /evidence="ECO:0000269|PubMed:5413288"
FT                   /id="PRO_0000010499"
FT   PEPTIDE         88..97
FT                   /note="Caerulein"
FT                   /evidence="ECO:0000269|PubMed:5413288"
FT                   /id="PRO_0000010500"
FT   PROPEP          101..151
FT                   /evidence="ECO:0000269|PubMed:5413288"
FT                   /id="PRO_0000010501"
FT   PEPTIDE         152..161
FT                   /note="Caerulein"
FT                   /evidence="ECO:0000269|PubMed:5413288"
FT                   /id="PRO_0000010502"
FT   PROPEP          165..169
FT                   /evidence="ECO:0000269|PubMed:5413288"
FT                   /id="PRO_0000010503"
FT   REGION          135..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         76
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         82
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         91
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         97
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         155
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         161
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000250"
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