FALX6_LITFA
ID FALX6_LITFA Reviewed; 103 AA.
AC B5LUQ8;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 25-MAY-2022, entry version 21.
DE RecName: Full=Preprofallaxidin-6 {ECO:0000312|EMBL:ACH53451.1};
DE Contains:
DE RecName: Full=Fallaxidin-1.3;
DE Contains:
DE RecName: Full=Fallaxidin-1.4;
DE Contains:
DE RecName: Full=Fallaxidin-3.1;
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:ACH53451.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 74-77; 86-89 AND 98-101,
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY, AND
RP AMIDATION AT LEU-65; PHE-77; PHE-89 AND ILE-101.
RC TISSUE=Skin {ECO:0000312|EMBL:ACH53451.1}, 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-1.3 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-1.4 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-3.1 shows antibacterial activity against the Gram-
CC positive bacteria E.faecalis (MIC=100 uM) and L.lactis (MIC=100 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 -!- MASS SPECTROMETRY: [Fallaxidin-1.3]: Mass=562; Method=Electrospray;
CC Note=The measured mass is that of Fallaxidin-1.3.;
CC Evidence={ECO:0000269|PubMed:18803332};
CC -!- MASS SPECTROMETRY: [Fallaxidin-3.1]: Mass=1646; Method=Electrospray;
CC Note=The measured mass is that of Fallaxidin-3.1.;
CC Evidence={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; EU912533; ACH53451.1; -; mRNA.
DR AlphaFoldDB; B5LUQ8; -.
DR TCDB; 1.C.52.1.11; the dermaseptin (dermaseptin) family.
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:ACH53451.1"
FT PROPEP 23..49
FT /evidence="ECO:0000269|PubMed:18803332"
FT /id="PRO_0000361722"
FT PEPTIDE 50..65
FT /note="Fallaxidin-3.1"
FT /id="PRO_0000361723"
FT PROPEP 69..73
FT /evidence="ECO:0000269|PubMed:18803332"
FT /id="PRO_0000361724"
FT PEPTIDE 74..77
FT /note="Fallaxidin-1.3"
FT /id="PRO_0000361725"
FT PROPEP 81..85
FT /evidence="ECO:0000269|PubMed:18803332"
FT /id="PRO_0000361726"
FT PEPTIDE 86..89
FT /note="Fallaxidin-1.3"
FT /id="PRO_0000361727"
FT PROPEP 93..97
FT /evidence="ECO:0000269|PubMed:18803332"
FT /id="PRO_0000361728"
FT PEPTIDE 98..101
FT /note="Fallaxidin-1.4"
FT /id="PRO_0000361729"
FT REGION 24..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 65
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:18803332"
FT MOD_RES 77
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:18803332"
FT MOD_RES 89
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:18803332"
FT MOD_RES 101
FT /note="Isoleucine amide"
FT /evidence="ECO:0000269|PubMed:18803332"
SQ SEQUENCE 103 AA; 11991 MW; E7F44B34C4910612 CRC64;
MASLKKSLFL VLFLGFVSLS ICEEEKRENE GNENEEEDEN HEEGSEEKRG LLDLAKHVIG
IASKLGKRSE EKRYHPFGKR SEEKRYHPFG KRSEEKRYPP IGK
