PELO4_PELFU
ID PELO4_PELFU Reviewed; 62 AA.
AC Q2WCN5;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=Pelophylaxin-4 {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:CAI99628.1};
RN [1] {ECO:0000312|EMBL:CAI99628.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 48-60, AMIDATION AT LEU-60,
RP SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND IDENTIFICATION BY MASS
RP 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:B3VZU4}.
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=1431.01; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16139927};
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Brevinin subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ972870; CAI99628.1; -; mRNA.
DR AlphaFoldDB; Q2WCN5; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; 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; Antimicrobial;
KW Cleavage on pair of basic residues; Direct protein sequencing; Secreted;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..45
FT /evidence="ECO:0000305|PubMed:16139927"
FT /id="PRO_0000439446"
FT PEPTIDE 48..60
FT /note="Pelophylaxin-4"
FT /evidence="ECO:0000269|PubMed:16139927"
FT /id="PRO_0000439447"
FT PROPEP 61
FT /evidence="ECO:0000305|PubMed:16139927"
FT /id="PRO_0000439448"
FT MOD_RES 60
FT /note="Leucine amide"
FT /evidence="ECO:0000303|PubMed:16139927"
SQ SEQUENCE 62 AA; 7286 MW; 0E964064114A383F CRC64;
MLTLKKSMLL IFFLGTINFS LCEQERNADE EERRDEPEER DVEVQKRILP FLAGLFSKIL
GK