ID   CAER4_XENBO             Reviewed;         234 AA.
AC   P05226;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Preprocaerulein type-4;
DE   AltName: Full=Preprocaerulein type IV;
DE   Contains:
DE     RecName: Full=Caerulein;
DE   Flags: Precursor;
OS   Xenopus borealis (Kenyan clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skin;
RX   PubMed=4000945; DOI=10.1093/nar/13.6.1817;
RA   Wakabayashi T., Kato H., Tachibana S.;
RT   "Complete nucleotide sequence of mRNA for caerulein precursor from Xenopus
RT   skin: the mRNA contains an unusual repetitive structure.";
RL   Nucleic Acids Res. 13:1817-1828(1985).
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; X02310; CAA26180.1; -; mRNA.
DR   AlphaFoldDB; P05226; -.
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; 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; Repeat; Secreted; Signal; Sulfation.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   PROPEP          27..73
FT                   /evidence="ECO:0000269|PubMed:5413288"
FT                   /id="PRO_0000010504"
FT   PEPTIDE         74..83
FT                   /note="Caerulein"
FT                   /evidence="ECO:0000269|PubMed:5413288"
FT                   /id="PRO_0000010505"
FT   PROPEP          87..137
FT                   /evidence="ECO:0000269|PubMed:5413288"
FT                   /id="PRO_0000010506"
FT   PEPTIDE         138..147
FT                   /note="Caerulein"
FT                   /evidence="ECO:0000269|PubMed:5413288"
FT                   /id="PRO_0000010507"
FT   PROPEP          151..152
FT                   /evidence="ECO:0000269|PubMed:5413288"
FT                   /id="PRO_0000010508"
FT   PEPTIDE         153..162
FT                   /note="Caerulein"
FT                   /evidence="ECO:0000269|PubMed:5413288"
FT                   /id="PRO_0000010509"
FT   PROPEP          166..216
FT                   /evidence="ECO:0000269|PubMed:5413288"
FT                   /id="PRO_0000010510"
FT   PEPTIDE         217..226
FT                   /note="Caerulein"
FT                   /evidence="ECO:0000269|PubMed:5413288"
FT                   /id="PRO_0000010511"
FT   PROPEP          230..234
FT                   /evidence="ECO:0000269|PubMed:5413288"
FT                   /id="PRO_0000010512"
FT   REGION          198..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   MOD_RES         220
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         226
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   234 AA;  26055 MW;  052D82F910541147 CRC64;
     MFKGILLCVL FAVLSANPLS QPEGFADEEE RDVRGLASLL GKALKAALKI GANALGGSPQ
     QREANDERRF ADGQQDYTGW MDFGRRDDED DVNERDVRGF GSFLGKALKA GLKIGTHFLG
     GAPQQREAND ERRFADGQQD YTGWMDFGRR DGQQDYTGWM DFGRRDDEDD VHERDVRGFG
     SFLGKALKAA LKIGANALGG SPQQREANDE RRFADGQQDY TGWMDFGRRN GEDD