CAER4_XENLA
ID CAER4_XENLA Reviewed; 233 AA.
AC P01357;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Preprocaerulein type-4;
DE AltName: Full=Preprocaerulein type IV;
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 137-233.
RC TISSUE=Skin;
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 [3]
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; M12495; AAA49685.1; -; mRNA.
DR EMBL; X01810; CAA25953.1; -; mRNA.
DR PIR; C23364; SCXL.
DR RefSeq; NP_001080990.1; NM_001087521.1.
DR AlphaFoldDB; P01357; -.
DR DNASU; 394315; -.
DR GeneID; 394315; -.
DR KEGG; xla:394315; -.
DR CTD; 394315; -.
DR Xenbase; XB-GENE-6254459; xt6l.L.
DR OrthoDB; 1881977at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 394315; Expressed in zone of skin and 11 other tissues.
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; 3.
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; Pyrrolidone carboxylic acid; Reference proteome;
KW Repeat; Secreted; Signal; Sulfation.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..72
FT /evidence="ECO:0000269|PubMed:5413288"
FT /id="PRO_0000010513"
FT PEPTIDE 73..82
FT /note="Caerulein"
FT /evidence="ECO:0000269|PubMed:5413288"
FT /id="PRO_0000010514"
FT PROPEP 86..87
FT /evidence="ECO:0000269|PubMed:5413288"
FT /id="PRO_0000010515"
FT PEPTIDE 88..97
FT /note="Caerulein"
FT /evidence="ECO:0000269|PubMed:5413288"
FT /id="PRO_0000010516"
FT PROPEP 101..151
FT /evidence="ECO:0000269|PubMed:5413288"
FT /id="PRO_0000010517"
FT PEPTIDE 152..161
FT /note="Caerulein"
FT /evidence="ECO:0000269|PubMed:5413288"
FT /id="PRO_0000010518"
FT PROPEP 165..215
FT /evidence="ECO:0000269|PubMed:5413288"
FT /id="PRO_0000010519"
FT PEPTIDE 216..225
FT /note="Caerulein"
FT /evidence="ECO:0000269|PubMed:5413288"
FT /id="PRO_0000010520"
FT PROPEP 229..233
FT /evidence="ECO:0000269|PubMed:5413288"
FT /id="PRO_0000010521"
FT REGION 197..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 73
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
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 88
FT /note="Pyrrolidone carboxylic acid"
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 152
FT /note="Pyrrolidone carboxylic acid"
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"
FT MOD_RES 216
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT MOD_RES 219
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 225
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250"
SQ SEQUENCE 233 AA; 25953 MW; 8BDE518027EC2FF1 CRC64;
MFKGILLCVL FAVLSANPLS QPEGFADEER DVRGLASLLG KALKATLKIG THFLGGAPQQ
REANDERRFA DGQQDYTGWM DFGRRDGQQD YTGWMDFGRR DDEDDVHERD VRGFGSFLGK
ALKAALKIGA NALGGAPQQR EANDERRFAD GQQDYTGWMD FGRRDDEDDV NERDVRGFGS
FLGKALKAAL KIGANALGGS PQQREANDER RFADGQQDYT GWMDFGRRNG EDD
