FALX7_LITFA
ID FALX7_LITFA Reviewed; 132 AA.
AC B5LUQ9;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 25-MAY-2022, entry version 14.
DE RecName: Full=Preprofallaxidin-7 {ECO:0000303|PubMed:18803332, ECO:0000312|EMBL:ACH53452.1};
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-3.3;
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:ACH53452.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 47-62; 71-74; 83-88;
RP 97-102; 111-116 AND 125-130, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, MASS SPECTROMETRY, AND AMIDATION AT PHE-74; PHE-88; ILE-102;
RP ILE-116 AND ILE-130.
RC TISSUE=Skin {ECO:0000312|EMBL:ACH53452.1}, 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 -!- 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-1.2]: Mass=782; Method=Electrospray;
CC Note=The measured mass is that of Fallaxidin-1.2.;
CC Evidence={ECO:0000269|PubMed:18803332};
CC -!- MASS SPECTROMETRY: [Fallaxidin-1.1]: Mass=748; Method=Electrospray;
CC Note=The measured mass is that of Fallaxidin-1.1.;
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; EU912534; ACH53452.1; -; mRNA.
DR AlphaFoldDB; B5LUQ9; -.
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; Direct protein sequencing; Secreted;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255, ECO:0000312|EMBL:ACH53452.1"
FT PROPEP 23..46
FT /evidence="ECO:0000269|PubMed:18803332"
FT /id="PRO_0000361730"
FT PEPTIDE 47..62
FT /note="Fallaxidin-3.3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000361731"
FT PROPEP 66..70
FT /evidence="ECO:0000269|PubMed:18803332"
FT /id="PRO_0000361732"
FT PEPTIDE 71..74
FT /note="Fallaxidin-1.3"
FT /id="PRO_0000361733"
FT PROPEP 78..82
FT /evidence="ECO:0000269|PubMed:18803332"
FT /id="PRO_0000361734"
FT PEPTIDE 83..88
FT /note="Fallaxidin-1.2"
FT /id="PRO_0000361735"
FT PROPEP 91..96
FT /evidence="ECO:0000269|PubMed:18803332"
FT /id="PRO_0000361736"
FT PEPTIDE 97..102
FT /note="Fallaxidin-1.1"
FT /id="PRO_0000361737"
FT PROPEP 106..110
FT /evidence="ECO:0000269|PubMed:18803332"
FT /id="PRO_0000361738"
FT PEPTIDE 111..116
FT /note="Fallaxidin-1.1"
FT /id="PRO_0000361739"
FT PROPEP 120..124
FT /evidence="ECO:0000269|PubMed:18803332"
FT /id="PRO_0000361740"
FT PEPTIDE 125..130
FT /note="Fallaxidin-1.1"
FT /id="PRO_0000361741"
FT REGION 25..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 62
FT /note="Leucine amide"
FT /evidence="ECO:0000250|UniProtKB:B5LUQ3"
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 MOD_RES 130
FT /note="Isoleucine amide"
FT /evidence="ECO:0000269|PubMed:18803332"
SQ SEQUENCE 132 AA; 15542 MW; 4B8F402CE7037F0B CRC64;
MASLKKSFFL VLFLGLVSLS MCEEKKRENE DDAEDGNHEE ESEEKRGLVD FAKHVIGIAS
KLGKRSEEKR YHPFGKRSEE KRYFPIPFGK RSEEKRYFPI PIGKRSEEKR YFPIPIGKRS
EEKRYFPIPI GK
