CAER1_XENLA
ID CAER1_XENLA Reviewed; 188 AA.
AC P05222; P87485; Q91722;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Preprocaerulein type-1;
DE AltName: Full=Preprocaerulein type I;
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 [GENOMIC DNA].
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 [3]
RP NUCLEOTIDE SEQUENCE OF 1-49.
RX PubMed=2465151; DOI=10.1111/j.1432-1033.1989.tb14552.x;
RA Kuchler K., Kreil G., Sures I.;
RT "The genes for the frog skin peptides GLa, xenopsin, levitide and caerulein
RT contain a homologous export exon encoding a signal sequence and part of an
RT amphiphilic peptide.";
RL Eur. J. Biochem. 179:281-285(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 55-188 (CLONE PXC204).
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 115-188 (CLONE PUF262).
RX PubMed=11894896; DOI=10.1002/j.1460-2075.1983.tb01390.x;
RA Hoffmann W., Bach T.C., Seliger H., Kreil G.;
RT "Biosynthesis of caerulein in the skin of Xenopus laevis: partial sequences
RT of precursors as deduced from cDNA clones.";
RL EMBO J. 2:111-114(1983).
RN [6]
RP PROTEIN SEQUENCE OF 171-180.
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; M12304; AAA49686.1; -; mRNA.
DR EMBL; M27984; AAA49688.1; -; Genomic_DNA.
DR EMBL; M27980; AAA49688.1; JOINED; Genomic_DNA.
DR EMBL; M27981; AAA49688.1; JOINED; Genomic_DNA.
DR EMBL; M27982; AAA49688.1; JOINED; Genomic_DNA.
DR EMBL; M27983; AAA49688.1; JOINED; Genomic_DNA.
DR EMBL; M12454; AAA49691.1; -; mRNA.
DR EMBL; K00930; AAA49682.1; -; mRNA.
DR PIR; A23364; A23364.
DR RefSeq; NP_001081262.1; NM_001087793.1.
DR AlphaFoldDB; P05222; -.
DR GeneID; 397740; -.
DR CTD; 397740; -.
DR Xenbase; XB-GENE-6252611; xt6l.S.
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; IPR001651; Gastrin/CCK.
DR InterPro; IPR013152; Gastrin/cholecystokinin_CS.
DR Pfam; PF00918; Gastrin; 1.
DR PROSITE; PS00259; GASTRIN; 1.
PE 1: Evidence at protein level;
KW Amidation; Amphibian defense peptide; Cleavage on pair of basic residues;
KW Direct protein sequencing; Reference proteome; Secreted; Signal; Sulfation.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..170
FT /evidence="ECO:0000269|PubMed:5413288"
FT /id="PRO_0000010493"
FT PEPTIDE 171..180
FT /note="Caerulein"
FT /id="PRO_0000010494"
FT PROPEP 184..188
FT /id="PRO_0000010495"
FT REGION 152..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 174
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 180
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250"
FT VARIANT 57
FT /note="A -> S (in clone PXC204)"
FT VARIANT 85
FT /note="A -> G (in clone PXC204)"
FT VARIANT 106..107
FT /note="TP -> SL (in clone PXC204)"
FT VARIANT 112
FT /note="A -> V (in clone PXC204)"
FT CONFLICT 75
FT /note="Missing (in Ref. 2; AAA49688)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="I -> SKLEHSF (in Ref. 2; AAA49688)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 188 AA; 20505 MW; 716819DAAD46FC0A CRC64;
MFKGILLCVL FAVLSANPLS QPEGFADEER DVRGLASFLG KALKAGLKIG AHLLGGAPQQ
REANDERRFA DDDDDVNERD VRGFASFLGK ALKAALKIGA NMLGGTPQQR EANDERRFAD
DEDDVNERDV RGFGSFLGKA LKAALKIGAN ALGGSPQQRE ANDERRFADG QQDYTGWMDF
GRRNGEDD
