B2H2B_ODOHA
ID B2H2B_ODOHA Reviewed; 75 AA.
AC E7EKE1;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 25-MAY-2022, entry version 20.
DE RecName: Full=Brevinin-2HS2B;
DE Flags: Precursor;
OS Odorrana hainanensis (Odor frog) (Rana hainanensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Odorrana.
OX NCBI_TaxID=431935;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ADV36141.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Skin {ECO:0000269|PubMed:22450466};
RX PubMed=22450466; DOI=10.1016/j.peptides.2012.03.007;
RA Wang H., Yu Z., Hu Y., Li F., Liu L., Zheng H., Meng H., Yang S., Yang X.,
RA Liu J.;
RT "Novel antimicrobial peptides isolated from the skin secretions of Hainan
RT odorous frog, Odorrana hainanensis.";
RL Peptides 35:285-290(2012).
CC -!- FUNCTION: Has antimicrobial activity against some Gram-positive
CC bacteria and fungi but has no activity against a range of Gram-negative
CC bacteria except P.faecalis. Has antimicrobial activity against the
CC Gram-positive bacteria S.aureus ATCC 25923 (MIC=19 uM), B.licheniformis
CC X39 (MIC=37.5 uM) and R.rhodochrous X15 (MIC=9.5 uM), is virtually
CC inactive against E.faecium 091299 (MIC=150 uM) and S.carnosus KHS
CC (MIC=150 uM) and inactive against E.faecalis 981. Active against the
CC Gram-negative bacterium P.faecalis X29 (MIC=9.5 uM) and is inactive
CC against E.coli, P.aeruginosa and S.typhi. Active against C.albicans
CC ATCC 2002 (MIC=19 uM) and is also active against the slime mold 090223
CC (MIC=37.5 uM). Has extremely low hemolytic activity against human
CC erythrocytes (LC(50)=300 uM). {ECO:0000269|PubMed:22450466}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:A0AEI5}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000305|PubMed:22450466}.
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Brevinin subfamily. {ECO:0000255}.
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DR EMBL; HQ735118; ADV36141.1; -; mRNA.
DR AlphaFoldDB; E7EKE1; -.
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.
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 3: Inferred from homology;
KW Amphibian defense peptide; Antibiotic; Antimicrobial;
KW Cleavage on pair of basic residues; Cytolysis; Disulfide bond; Fungicide;
KW Hemolysis; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..40
FT /evidence="ECO:0000250|UniProtKB:A0AEI5"
FT /id="PRO_0000423535"
FT PEPTIDE 43..75
FT /note="Brevinin-2HS2B"
FT /evidence="ECO:0000250|UniProtKB:A0AEI5"
FT /id="PRO_0000423536"
FT DISULFID 69..75
FT /evidence="ECO:0000250|UniProtKB:A0AEI5"
SQ SEQUENCE 75 AA; 8123 MW; BFD3344051188E7C CRC64;
MFTMKKPLLL IVLLGIISLS LCEQERAADE EEGEMIEEEV KRSLLGTVKD LLIGAGKSAA
QSVLKGLSCK LSKDC