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LDN2_ODOLI
ID   LDN2_ODOLI              Reviewed;          76 AA.
AC   Q2UXR3;
DT   12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Lividin-2 {ECO:0000303|PubMed:16713657};
DE   Flags: Precursor;
OS   Odorrana livida (Green mountain frog) (Polypedates lividus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Odorrana.
OX   NCBI_TaxID=121160 {ECO:0000312|EMBL:CAJ01671.1};
RN   [1] {ECO:0000312|EMBL:CAJ01671.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 44-76, SUBCELLULAR
RP   LOCATION, MASS SPECTROMETRY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Skin secretion {ECO:0000303|PubMed:16713657};
RX   PubMed=16713657; DOI=10.1016/j.peptides.2006.04.007;
RA   Zhou M., Chen T., Walker B., Shaw C.;
RT   "Lividins: novel antimicrobial peptide homologs from the skin secretion of
RT   the Chinese Large Odorous frog, Rana (Odorrana) livida. Identification by
RT   'shotgun' cDNA cloning and sequence analysis.";
RL   Peptides 27:2118-2123(2006).
CC   -!- FUNCTION: Antimicrobial peptide. {ECO:0000250|UniProtKB:E7EKE0}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255,
CC       ECO:0000269|PubMed:16713657}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:16713657}.
CC   -!- MASS SPECTROMETRY: Mass=3355.20; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16713657};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Brevinin subfamily. {ECO:0000255}.
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DR   EMBL; AM039663; CAJ01671.1; -; mRNA.
DR   AlphaFoldDB; Q2UXR3; -.
DR   SMR; Q2UXR3; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0006952; P:defense response; 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   1: Evidence at protein level;
KW   Amphibian defense peptide; 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                   /evidence="ECO:0000305|PubMed:16713657"
FT                   /id="PRO_0000439436"
FT   PEPTIDE         44..76
FT                   /note="Lividin-2"
FT                   /evidence="ECO:0000269|PubMed:16713657"
FT                   /id="PRO_0000439437"
FT   DISULFID        70..76
FT                   /evidence="ECO:0000250|UniProtKB:A0AEI6"
SQ   SEQUENCE   76 AA;  8259 MW;  3387D8FAA8496B7C CRC64;
     MFTLKKSLLL LFFLGTISLS LCQEERNADE EDGGEVTEEE VKRSFLDTLK NLAISAAKGA
     GQSVLSTLSC KLSKTC
 
 
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