FALX3_LITFA
ID FALX3_LITFA Reviewed; 123 AA.
AC B5LUQ7;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 25-MAY-2022, entry version 17.
DE RecName: Full=Preprofallaxidin-3 {ECO:0000303|PubMed:18803332, ECO:0000312|EMBL:ACH53450.1};
DE Contains:
DE RecName: Full=Fallaxidin-1.1;
DE Contains:
DE RecName: Full=Fallaxidin-1.2;
DE Contains:
DE RecName: Full=Fallaxidin-1.3;
DE Contains:
DE RecName: Full=Fallaxidin-3.2;
DE Flags: Precursor; Fragment;
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:ACH53450.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 47-62; 71-74; 83-88; 97-102
RP AND 111-116, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP AMIDATION AT LEU-62; PHE-74; PHE-88; ILE-102 AND ILE-116.
RC TISSUE=Skin {ECO:0000312|EMBL:ACH53450.1}, and
RC Skin secretion {ECO:0000269|PubMed:18803332};
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 -!- FUNCTION: Fallaxidin-1.1 shows no antibacterial activity against Gram-
CC positive or Gram-negative bacteria. Does not inhibit the formation of
CC NO by neuronal nitric oxide synthase. Has no effect on splenocyte
CC proliferation or smooth muscle contraction.
CC {ECO:0000269|PubMed:18803332}.
CC -!- FUNCTION: Fallaxidin-1.2 shows no antibacterial activity against Gram-
CC positive or Gram-negative bacteria. Does not inhibit the formation of
CC NO by neuronal nitric oxide synthase. Has no effect on splenocyte
CC proliferation or smooth muscle contraction.
CC {ECO:0000269|PubMed:18803332}.
CC -!- FUNCTION: Fallaxidin-1.3 shows no antibacterial activity against Gram-
CC positive or Gram-negative bacteria. Does not inhibit the formation of
CC NO by neuronal nitric oxide synthase. Has no effect on splenocyte
CC proliferation or smooth muscle contraction.
CC {ECO:0000269|PubMed:18803332}.
CC -!- FUNCTION: Fallaxidin-3.2 shows antibacterial activity against the Gram-
CC positive bacteria E.faecalis (MIC=100 uM) and L.lactis (MIC=500 uM). No
CC antibacterial activity against the Gram-positive bacteria B.cereus,
CC L.innocua, M.luteus, S.epidermidis, S.uberis and S.aureus, or the Gram-
CC negative bacteria E.cloacae and E.coli. {ECO:0000269|PubMed:18803332}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18803332}.
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}.
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DR EMBL; EU912532; ACH53450.1; -; mRNA.
DR AlphaFoldDB; B5LUQ7; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; 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; Antibiotic; Antimicrobial;
KW Direct protein sequencing; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255, ECO:0000312|EMBL:ACH53450.1"
FT PROPEP 23..46
FT /evidence="ECO:0000269|PubMed:18803332"
FT /id="PRO_0000361706"
FT PEPTIDE 47..62
FT /note="Fallaxidin-3.2"
FT /id="PRO_0000361707"
FT PROPEP 66..70
FT /evidence="ECO:0000269|PubMed:18803332"
FT /id="PRO_0000361708"
FT PEPTIDE 71..74
FT /note="Fallaxidin-1.3"
FT /id="PRO_0000361709"
FT PROPEP 78..82
FT /evidence="ECO:0000269|PubMed:18803332"
FT /id="PRO_0000361710"
FT PEPTIDE 83..88
FT /note="Fallaxidin-1.2"
FT /id="PRO_0000361711"
FT PROPEP 92..96
FT /evidence="ECO:0000269|PubMed:18803332"
FT /id="PRO_0000361712"
FT PEPTIDE 97..102
FT /note="Fallaxidin-1.1"
FT /id="PRO_0000361713"
FT PROPEP 106..110
FT /evidence="ECO:0000269|PubMed:18803332"
FT /id="PRO_0000361714"
FT PEPTIDE 111..116
FT /note="Fallaxidin-1.1"
FT /id="PRO_0000361715"
FT PROPEP 120..>123
FT /evidence="ECO:0000269|PubMed:18803332"
FT /id="PRO_0000361716"
FT REGION 26..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 62
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:18803332"
FT MOD_RES 74
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:18803332"
FT MOD_RES 88
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:18803332"
FT MOD_RES 102
FT /note="Isoleucine amide"
FT /evidence="ECO:0000269|PubMed:18803332"
FT MOD_RES 116
FT /note="Isoleucine amide"
FT /evidence="ECO:0000269|PubMed:18803332"
FT NON_TER 123
FT /evidence="ECO:0000312|EMBL:ACH53450.1"
SQ SEQUENCE 123 AA; 14515 MW; 4A45451F6977D0EE CRC64;
MASLKKSLFL VLFLGLVSLS ICEEKKRENE DDAEDENHEE ESEEKRGLLD FAKHVIGIAS
KLGKRSEEKR YHPFGKRSEE KRYFPIPFGK RSEEKRYFPI PIGKRSEEKR YFPIPIGKKK
KKK
