ID   TP2_ODOHA               Reviewed;          59 AA.
AC   E7EKD4;
DT   18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   25-MAY-2022, entry version 19.
DE   RecName: Full=Temporin-HN2 {ECO:0000312|EMBL:ADV36134.1};
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:ADV36134.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 44-57, SYNTHESIS OF 44-57,
RP   FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND AMIDATION AT LEU-57.
RC   TISSUE=Skin {ECO:0000269|PubMed:22450466}, and
RC   Skin secretion {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. Active against the Gram-positive bacteria
CC       S.aureus ATCC 25923 (MIC=4.8 uM), S.carnosus KHS (MIC=19 uM),
CC       B.licheniformis X39 (MIC=19 uM) and R.rhodochrous X15 (MIC=2.4 uM) but
CC       is inactive against E.faecium 091299 and E.faecalis 981. Has a less
CC       potent antimicrobial activity against the Gram-negative bacterium
CC       P.faecalis X29 (MIC=37.5 uM) and is inactive against E.coli,
CC       P.aeruginosa and S.typhi. Has antifungal activity against C.albicans
CC       ATCC 2002 (MIC=9.5 uM) and is also active against the slime mold 090223
CC       (MIC=9.5 uM). Has extremely low hemolytic activity against human
CC       erythrocytes (LC(50)=300 uM). {ECO:0000269|PubMed:22450466}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22450466}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:22450466}.
CC   -!- MASS SPECTROMETRY: Mass=1580.00; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:22450466};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Temporin subfamily. {ECO:0000255}.
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DR   EMBL; HQ735111; ADV36134.1; -; mRNA.
DR   AlphaFoldDB; E7EKD4; -.
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; IPR004275; Frog_antimicrobial_propeptide.
DR   Pfam; PF03032; FSAP_sig_propep; 1.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Cleavage on pair of basic residues; Coiled coil; Cytolysis;
KW   Direct protein sequencing; Fungicide; Hemolysis; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..41
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:22450466"
FT                   /id="PRO_0000423527"
FT   PEPTIDE         44..57
FT                   /note="Temporin-HN2"
FT                   /evidence="ECO:0000269|PubMed:22450466"
FT                   /id="PRO_0000423528"
FT   COILED          16..44
FT                   /evidence="ECO:0000255"
FT   MOD_RES         57
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:22450466"
SQ   SEQUENCE   59 AA;  6873 MW;  27EC9FB8894381FB CRC64;
     MFTLKKSLLL LLFLGTINLS LSEQERDAKE ERRDEMDVEV EKRNILNTII NLAKKILGK