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LDN3_ODOLI
ID   LDN3_ODOLI              Reviewed;          75 AA.
AC   Q2UXR2;
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-3 {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:CAJ01672.1};
RN   [1] {ECO:0000312|EMBL:CAJ01672.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 43-75, 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=3234.01; 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; AM039664; CAJ01672.1; -; mRNA.
DR   AlphaFoldDB; Q2UXR2; -.
DR   SMR; Q2UXR2; -.
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..40
FT                   /evidence="ECO:0000305|PubMed:16713657"
FT                   /id="PRO_0000439438"
FT   PEPTIDE         43..75
FT                   /note="Lividin-3"
FT                   /evidence="ECO:0000269|PubMed:16713657"
FT                   /id="PRO_0000439439"
FT   DISULFID        69..75
FT                   /evidence="ECO:0000250|UniProtKB:A0AEI6"
SQ   SEQUENCE   75 AA;  8114 MW;  9886CEF0BB307AA6 CRC64;
     MFTLKKSLLL LFFLGTISLS LCEEERDADE DEGEMTEEEV KRSVLGTVKD LLIGAGKSAA
     QSVLTALSCK LSNSC
 
 
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