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NA12D_ANEVI
ID   NA12D_ANEVI             Reviewed;          79 AA.
AC   B1NWT7;
DT   16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Delta-actitoxin-Avd1c 4 {ECO:0000303|PubMed:22683676};
DE            Short=Delta-AITX-Avd1c 4 {ECO:0000303|PubMed:22683676};
DE   AltName: Full=Toxin 2c2 {ECO:0000312|EMBL:ABW97353.1};
DE   AltName: Full=Toxin 2c3 {ECO:0000312|EMBL:ABW97354.1};
DE   Flags: Precursor;
OS   Anemonia viridis (Snakelocks anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Actiniidae; Anemonia.
OX   NCBI_TaxID=51769;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=18222944; DOI=10.1093/molbev/msn021;
RA   Moran Y., Weinberger H., Sullivan J.C., Reitzel A.M., Finnerty J.R.,
RA   Gurevitz M.;
RT   "Concerted evolution of sea anemone neurotoxin genes is revealed through
RT   analysis of the Nematostella vectensis genome.";
RL   Mol. Biol. Evol. 25:737-747(2008).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=22683676; DOI=10.1016/j.toxicon.2012.05.020;
RA   Oliveira J.S., Fuentes-Silva D., King G.F.;
RT   "Development of a rational nomenclature for naming peptide and protein
RT   toxins from sea anemones.";
RL   Toxicon 60:539-550(2012).
CC   -!- FUNCTION: Binds specifically to voltage-gated sodium channels (Nav)
CC       (site 3), thereby delaying their inactivation during signal
CC       transduction. Has a strong effect on crustaceans and insects and a
CC       weaker effect on mammals. It strongly inhibits D.melanogaster sodium
CC       channel (DmNav1). It weakly inhibits the brain sodium channel
CC       Nav1.2/SCN2A. It strongly affects the heart sodium channels
CC       (Nav1.5/SCN5A). {ECO:0000250|UniProtKB:P01528}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}.
CC   -!- MISCELLANEOUS: This protein is encoded by at least 3 different genes.
CC       At least 3 other genes code for a similar Av2 with an Ile (instead a
CC       Val) at position 34. {ECO:0000250|UniProtKB:P0DL49}.
CC   -!- SIMILARITY: Belongs to the sea anemone sodium channel inhibitory toxin
CC       family. Type I subfamily. {ECO:0000305}.
CC   -!- CAUTION: Opinions are divided on whether Anemonia viridis (Forsskal,
CC       1775) and Anemonia sulcata (Pennant, 1777) are separate species.
CC       {ECO:0000305}.
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DR   EMBL; EU124474; ABW97353.1; -; mRNA.
DR   EMBL; EU124475; ABW97354.1; -; mRNA.
DR   AlphaFoldDB; B1NWT7; -.
DR   SMR; B1NWT7; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR   GO; GO:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.20.20.10; -; 1.
DR   InterPro; IPR023355; Myo_ane_neurotoxin_sf.
PE   3: Inferred from homology;
KW   Cleavage on pair of basic residues; Disulfide bond;
KW   Ion channel impairing toxin; Nematocyst; Neurotoxin; Secreted; Signal;
KW   Toxin; Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..30
FT                   /evidence="ECO:0000250|UniProtKB:P01528"
FT                   /id="PRO_0000433685"
FT   CHAIN           33..79
FT                   /note="Delta-actitoxin-Avd1c 4"
FT                   /evidence="ECO:0000250|UniProtKB:P0DL49"
FT                   /id="PRO_5000319682"
FT   DISULFID        36..76
FT                   /evidence="ECO:0000250|UniProtKB:P01528"
FT   DISULFID        38..66
FT                   /evidence="ECO:0000250|UniProtKB:P01528"
FT   DISULFID        59..77
FT                   /evidence="ECO:0000250|UniProtKB:P01528"
SQ   SEQUENCE   79 AA;  8534 MW;  D638145476163328 CRC64;
     MMNRLLVFLM LGAAFMLVVS AIDQDANDIN KRGVPCLCDS DGPSVRGNTL SGIIWLAGCP
     SGWHNCKKHG PTIGWCCKQ
 
 
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