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 02-SEP-2026, entry version 103. 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}. 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; 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 SMR; P01357; -. DR DNASU; 394315; -. DR GeneID; 394315; -. DR KEGG; xla:394315; -. DR AGR; Xenbase:XB-GENE-6254459; -. DR CTD; 394315; -. DR Xenbase; XB-GENE-6254459; xt6l.L. DR Proteomes; UP000186698; Chromosome 6L. DR Bgee; 394315; Expressed in zone of skin and 11 other cell types or tissues. DR GO; GO:0030424; C:axon; IEA:TreeGrafter. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005184; F:neuropeptide hormone activity; IEA:InterPro. DR GO; GO:0002777; P:antimicrobial peptide biosynthetic process; TAS:Xenbase. DR GO; GO:0007586; P:digestion; IEA:InterPro. DR InterPro; IPR015499; CCK-like. DR InterPro; IPR001651; Gastrin/CCK. DR InterPro; IPR013152; Gastrin/cholecystokinin_CS. DR PANTHER; PTHR10786; CHOLECYSTOKININ; 1. DR PANTHER; PTHR10786:SF0; CHOLECYSTOKININ; 1. DR Pfam; PF00918; Gastrin; 3. DR SMART; SM00029; GASTRIN; 4. 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 //