位置:首页 > 蛋白库 > FALX7_LITFA
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}.
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; 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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024