CPFR4_XENRU
ID CPFR4_XENRU Reviewed; 27 AA.
AC C0HKM8;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2017, sequence version 1.
DT 25-MAY-2022, entry version 4.
DE RecName: Full=Caerulein precursor fragment R4 {ECO:0000303|PubMed:27290612};
DE AltName: Full=CPF-R4 {ECO:0000303|PubMed:27290612};
OS Xenopus ruwenzoriensis (Uganda clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=105430 {ECO:0000303|PubMed:27290612};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC TISSUE=Skin secretion {ECO:0000303|PubMed:27290612};
RX PubMed=27290612; DOI=10.1016/j.cbd.2016.04.006;
RA Coquet L., Kolodziejek J., Jouenne T., Nowotny N., King J.D., Conlon J.M.;
RT "Peptidomic analysis of the extensive array of host-defense peptides in
RT skin secretions of the dodecaploid frog Xenopus ruwenzoriensis (Pipidae).";
RL Comp. Biochem. Physiol. 19:18-24(2016).
CC -!- FUNCTION: Antimicrobial peptide. {ECO:0000250|UniProtKB:C0HK89}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27290612}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000305|PubMed:27290612}.
CC -!- MASS SPECTROMETRY: Mass=2601.5; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:27290612};
CC -!- SIMILARITY: Belongs to the gastrin/cholecystokinin family.
CC {ECO:0000305}.
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DR AlphaFoldDB; C0HKM8; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Amphibian defense peptide; Antimicrobial; Direct protein sequencing;
KW Secreted.
FT PEPTIDE 1..27
FT /note="Caerulein precursor fragment R4"
FT /evidence="ECO:0000269|PubMed:27290612"
FT /id="PRO_0000440914"
SQ SEQUENCE 27 AA; 2602 MW; D25088DB93321356 CRC64;
GFGSFLGKAL KAALKIGANA LGGSPQQ