BR2IA_ODOIS
ID BR2IA_ODOIS Reviewed; 76 AA.
AC F1T153;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 25-MAY-2022, entry version 30.
DE RecName: Full=Brevinin-2ISa {ECO:0000303|PubMed:21193000};
DE Flags: Precursor;
OS Odorrana ishikawae (Ishikawa's frog) (Rana ishikawae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Odorrana.
OX NCBI_TaxID=310659 {ECO:0000303|PubMed:21193000};
RN [1] {ECO:0000312|EMBL:BAK08585.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 44-76, FUNCTION, SYNTHESIS,
RP AND MASS SPECTROMETRY.
RC TISSUE=Skin {ECO:0000303|PubMed:21193000};
RX PubMed=21193000; DOI=10.1016/j.peptides.2010.12.013;
RA Iwakoshi-Ukena E., Ukena K., Okimoto A., Soga M., Okada G., Sano N.,
RA Fujii T., Sugawara Y., Sumida M.;
RT "Identification and characterization of antimicrobial peptides from the
RT skin of the endangered frog Odorrana ishikawae.";
RL Peptides 32:670-676(2011).
CC -!- FUNCTION: Has antimicrobial activity against Gram-negative bacterium
CC E.coli ATCC 8739 (MIC=50 ug), against Gram positive bacteria S.aureus
CC ATCC 6538 (MIC=12.5 ug), methicillin-resistant S.aureus ATCC 43300
CC (MIC=100 ug) and B.subtilis ATCC 6633 (MIC=12.5 ug). Has no activity
CC against fungus C.albicans ATCC 90028. {ECO:0000269|PubMed:21193000}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:21193000}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000305|PubMed:21193000}.
CC -!- MASS SPECTROMETRY: Mass=3394.1; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:21193000};
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Brevinin subfamily. {ECO:0000255}.
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DR EMBL; AB602055; BAK08585.1; -; mRNA.
DR AlphaFoldDB; F1T153; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR InterPro; IPR012521; Antimicrobial_frog_2.
DR InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR Pfam; PF08023; Antimicrobial_2; 1.
DR Pfam; PF03032; FSAP_sig_propep; 1.
PE 1: Evidence at protein level;
KW Amphibian defense peptide; Antibiotic; Antimicrobial;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..41
FT /note="Removed in mature form"
FT /evidence="ECO:0000305|PubMed:21193000"
FT /id="PRO_0000439601"
FT PEPTIDE 44..76
FT /note="Brevinin-2ISa"
FT /evidence="ECO:0000269|PubMed:21193000"
FT /id="PRO_0000439602"
FT DISULFID 70..76
FT /evidence="ECO:0000250|UniProtKB:P80398"
SQ SEQUENCE 76 AA; 8391 MW; 37315C35F812746F CRC64;
MFNMKKSLLL LFFLGTISLS LCEEERDADE DDGVEMTEEE VKRSLLDTFK NLAVNAAKSA
GVSVLNALSC KISRTC