FALX5_LITFA
ID FALX5_LITFA Reviewed; 68 AA.
AC B5LUQ6;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 25-MAY-2022, entry version 18.
DE RecName: Full=Preprofallaxidin-5 {ECO:0000303|PubMed:18803332, ECO:0000312|EMBL:ACH53449.1};
DE Contains:
DE RecName: Full=Fallaxidin-5.1;
DE Flags: Precursor;
OS Litoria fallax (Eastern dwarf tree frog) (Hylomantis fallax).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Pelodryadinae; Litoria.
OX NCBI_TaxID=115422;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ACH53449.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Skin {ECO:0000312|EMBL:ACH53449.1};
RX PubMed=18803332; DOI=10.1002/rcm.3723;
RA Jackway R.J., Bowie J.H., Bilusich D., Musgrave I.F., Surinya-Johnson K.H.,
RA Tyler M.J., Eichinger P.C.H.;
RT "The fallaxidin peptides from the skin secretion of the eastern dwarf tree
RT frog Litoria fallax. Sequence determination by positive and negative ion
RT electrospray mass spectrometry: antimicrobial activity and cDNA cloning of
RT the fallaxidins.";
RL Rapid Commun. Mass Spectrom. 22:3207-3216(2008).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P82881}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000269|PubMed:18803332}.
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Brevinin subfamily. {ECO:0000255}.
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; EU912531; ACH53449.1; -; mRNA.
DR AlphaFoldDB; B5LUQ6; -.
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 2: Evidence at transcript level;
KW Amidation; Amphibian defense peptide; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255, ECO:0000312|EMBL:ACH53449.1"
FT PROPEP 23..51
FT /evidence="ECO:0000269|PubMed:18803332"
FT /id="PRO_0000361719"
FT PEPTIDE 52..64
FT /note="Fallaxidin-5.1"
FT /id="PRO_0000361720"
FT PROPEP 68
FT /evidence="ECO:0000269|PubMed:18803332"
FT /id="PRO_0000361721"
FT REGION 24..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..42
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 64
FT /note="Leucine amide"
FT /evidence="ECO:0000250|UniProtKB:P82881"
SQ SEQUENCE 68 AA; 7741 MW; 51CD49A5761F5FF8 CRC64;
MASLKKSLFL VLFLGFVSLS ICEEEKREDK EDEGENEEAE ENHEERSEEK RFLPLLASLV
GGLLGKRS