ID   CPFB1_XENBO             Reviewed;          28 AA.
AC   C0HK89;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2016, sequence version 1.
DT   25-MAY-2022, entry version 4.
DE   RecName: Full=Caerulein precursor fragment B1 {ECO:0000303|PubMed:20656059};
DE            Short=CPF-B1 {ECO:0000303|PubMed:20656059};
DE   Contains:
DE     RecName: Full=Caerulein precursor fragment B2 {ECO:0000303|PubMed:20656059};
DE              Short=CPF-B2 {ECO:0000303|PubMed:20656059};
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 {ECO:0000303|PubMed:20656059};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   TISSUE=Skin secretion {ECO:0000303|PubMed:20656059};
RX   PubMed=20656059; DOI=10.1016/j.cbpc.2010.07.007;
RA   Mechkarska M., Ahmed E., Coquet L., Leprince J., Jouenne T., Vaudry H.,
RA   King J.D., Conlon J.M.;
RT   "Antimicrobial peptides with therapeutic potential from skin secretions of
RT   the Marsabit clawed frog Xenopus borealis (Pipidae).";
RL   Comp. Biochem. Physiol. 152:467-472(2010).
CC   -!- FUNCTION: Peptide CPF-B1: Has antimicrobial activity against Gram-
CC       negative bacteria E.coli ATCC 25922 (MIC=5 uM) and multidrug-resistant
CC       A.baumannii (MIC=4-8 uM), against Gram-positive bacteria S.aureus ATCC
CC       25923 (MIC=5 uM) and methicillin-resistant S.aureus and against fungus
CC       C.albicans ATCC 90028 (MIC=25 uM). Has some hemolytic activity against
CC       human erythrocytes at high concentrations.
CC       {ECO:0000269|PubMed:20656059}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20656059}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:20656059}.
CC   -!- MASS SPECTROMETRY: [Caerulein precursor fragment B1]: Mass=2844.5;
CC       Method=MALDI; Evidence={ECO:0000269|PubMed:20656059};
CC   -!- MASS SPECTROMETRY: [Caerulein precursor fragment B2]: Mass=2587.6;
CC       Method=MALDI; Evidence={ECO:0000269|PubMed:20656059};
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   AlphaFoldDB; C0HK89; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Cytolysis; Direct protein sequencing; Fungicide;
KW   Hemolysis; Secreted.
FT   PEPTIDE         1..28
FT                   /note="Caerulein precursor fragment B1"
FT                   /evidence="ECO:0000269|PubMed:20656059"
FT                   /id="PRO_0000438429"
FT   PEPTIDE         1..26
FT                   /note="Caerulein precursor fragment B2"
FT                   /evidence="ECO:0000269|PubMed:20656059"
FT                   /id="PRO_0000438430"
SQ   SEQUENCE   28 AA;  2845 MW;  6BB6431E06DA3218 CRC64;
     GLGSLLGKAF KIGLKTVGKM MGGAPREQ