ID   PELO1_PELFU             Reviewed;          73 AA.
AC   Q2WCN8;
DT   12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Pelophylaxin-1 {ECO:0000303|PubMed:16139927};
DE   Flags: Precursor;
OS   Pelophylax fukienensis (Fukien gold-striped pond frog) (Rana fukienensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Pelophylax.
OX   NCBI_TaxID=88448 {ECO:0000312|EMBL:CAI99625.1};
RN   [1] {ECO:0000312|EMBL:CAI99625.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 44-73, SUBCELLULAR
RP   LOCATION, MASS SPECTROMETRY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Skin secretion {ECO:0000303|PubMed:16139927};
RX   PubMed=16139927; DOI=10.1016/j.peptides.2005.07.007;
RA   Zhou M., Chen T., Walker B., Shaw C.;
RT   "Pelophylaxins: novel antimicrobial peptide homologs from the skin
RT   secretion of the Fukien gold-striped pond frog, Pelophylax plancyi
RT   fukienensis: identification by 'shotgun' cDNA cloning and sequence
RT   analysis.";
RL   Peptides 27:36-41(2006).
CC   -!- FUNCTION: Antimicrobial peptide. {ECO:0000250|UniProtKB:Q8QFQ4}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255,
CC       ECO:0000269|PubMed:16139927}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:16139927}.
CC   -!- MASS SPECTROMETRY: Mass=2999.24; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16139927};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Brevinin subfamily. {ECO:0000255}.
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DR   EMBL; AJ972867; CAI99625.1; -; mRNA.
DR   AlphaFoldDB; Q2WCN8; -.
DR   SMR; Q2WCN8; -.
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; IPR018247; EF_Hand_1_Ca_BS.
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:16139927"
FT                   /id="PRO_0000439442"
FT   PEPTIDE         44..73
FT                   /note="Pelophylaxin-1"
FT                   /evidence="ECO:0000269|PubMed:16139927"
FT                   /id="PRO_0000439443"
FT   DISULFID        67..73
FT                   /evidence="ECO:0000250|UniProtKB:A0AEI6"
SQ   SEQUENCE   73 AA;  7820 MW;  836862E1FB339ED1 CRC64;
     MFTMKKSLLL VFFLGTIALS LCEEERGADD DNGGEITDEE IKRGILTDTL KGAAKNVAGV
     LLDKLKCKIT GGC