ID   CAER5_XENLA             Reviewed;         187 AA.
AC   P05225;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Preprocaerulein clone PXC202;
DE   Contains:
DE     RecName: Full=Caerulein;
DE   Flags: Precursor; Fragment;
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=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   [2]
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}.
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DR   EMBL; M12453; AAA49689.1; -; mRNA.
DR   AlphaFoldDB; P05225; -.
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; IPR039236; GAST.
DR   InterPro; IPR001651; Gastrin/CCK.
DR   InterPro; IPR013152; Gastrin/cholecystokinin_CS.
DR   PANTHER; PTHR19309; PTHR19309; 2.
DR   Pfam; PF00918; Gastrin; 2.
DR   PROSITE; PS00259; GASTRIN; 4.
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; Sulfation.
FT   PROPEP          <1..9
FT                   /evidence="ECO:0000269|PubMed:5413288"
FT                   /id="PRO_0000010522"
FT   PEPTIDE         10..19
FT                   /note="Caerulein"
FT                   /evidence="ECO:0000269|PubMed:5413288"
FT                   /id="PRO_0000010523"
FT   PROPEP          23..73
FT                   /evidence="ECO:0000269|PubMed:5413288"
FT                   /id="PRO_0000010524"
FT   PEPTIDE         74..83
FT                   /note="Caerulein"
FT                   /evidence="ECO:0000269|PubMed:5413288"
FT                   /id="PRO_0000010525"
FT   PROPEP          87..137
FT                   /evidence="ECO:0000269|PubMed:5413288"
FT                   /id="PRO_0000010526"
FT   PEPTIDE         138..147
FT                   /note="Caerulein"
FT                   /evidence="ECO:0000269|PubMed:5413288"
FT                   /id="PRO_0000010527"
FT   PROPEP          151..152
FT                   /evidence="ECO:0000269|PubMed:5413288"
FT                   /id="PRO_0000010528"
FT   PEPTIDE         153..162
FT                   /note="Caerulein"
FT                   /evidence="ECO:0000269|PubMed:5413288"
FT                   /id="PRO_0000010529"
FT   PROPEP          166..187
FT                   /evidence="ECO:0000269|PubMed:5413288"
FT                   /id="PRO_0000010530"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         13
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         19
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         77
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         83
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         141
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         147
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         156
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         162
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         187
SQ   SEQUENCE   187 AA;  21242 MW;  15738A4F3025E392 CRC64;
     NDERRFADGQ QDYTGWMDFG RRDDEDDVNE RDVRGFGSFL GKALKAALKI GANALGGSPQ
     QREANDERRF ADGQQDYTGW MDFGRRDDED DVNERDVRGF GSFLGKALKA ALKIGANALG
     GSLQQREVND ERRFADGQQD YTGWMDFGRR DGQQDYTGWM DFGRRDDEDD VHERDVRGFG
     SFLGKAL