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TXDT1_ATRRO
ID   TXDT1_ATRRO             Reviewed;          42 AA.
AC   P01478;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Delta-hexatoxin-Ar1a {ECO:0000305};
DE            Short=Delta-HXTX-Ar1a {ECO:0000305};
DE   AltName: Full=Delta-atracotoxin-Ar1 {ECO:0000303|PubMed:9560455, ECO:0000303|PubMed:9845331};
DE   AltName: Full=Delta-atracotoxin-Ar1a {ECO:0000303|PubMed:14596608};
DE            Short=Delta-ACTX-Ar1a {ECO:0000303|PubMed:14596608};
DE   AltName: Full=Robustoxin {ECO:0000303|PubMed:10080353, ECO:0000303|PubMed:2728033, ECO:0000303|PubMed:3972101, ECO:0000303|PubMed:9560455};
DE            Short=RBX {ECO:0000303|PubMed:10080353, ECO:0000303|PubMed:9428632};
OS   Atrax robustus (Sydney funnel-web spider).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Hexathelidae; Atrax.
OX   NCBI_TaxID=6903;
RN   [1]
RP   PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=3972101; DOI=10.1016/0014-5793(85)81132-7;
RA   Sheumack D.D., Claassens R., Whiteley N.M., Howden M.E.H.;
RT   "Complete amino acid sequence of a new type of lethal neurotoxin from the
RT   venom of the funnel-web spider Atrax robustus.";
RL   FEBS Lett. 181:154-156(1985).
RN   [2]
RP   FUNCTION.
RX   PubMed=2728033; DOI=10.1016/0041-0101(89)90211-0;
RA   Mylecharane E.J., Spence I., Sheumack D.D., Claassens R., Howden M.E.;
RT   "Actions of robustoxin, a neurotoxic polypeptide from the venom of the male
RT   funnel-web spider (Atrax robustus), in anaesthetized monkeys.";
RL   Toxicon 27:481-492(1989).
RN   [3]
RP   FUNCTION.
RX   PubMed=9845331; DOI=10.1016/s0014-5793(98)01378-7;
RA   Little M.J., Wilson H., Zappia C., Cestele S., Tyler M.I.,
RA   Martin-Eauclaire M.-F., Gordon D., Nicholson G.M.;
RT   "Delta-atracotoxins from Australian funnel-web spiders compete with
RT   scorpion alpha-toxin binding on both rat brain and insect sodium
RT   channels.";
RL   FEBS Lett. 439:246-252(1998).
RN   [4]
RP   FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=9560455; DOI=10.1007/s004240050612;
RA   Nicholson G.M., Walsh R., Little M.J., Tyler M.I.;
RT   "Characterisation of the effects of robustoxin, the lethal neurotoxin from
RT   the Sydney funnel-web spider Atrax robustus, on sodium channel activation
RT   and inactivation.";
RL   Pflugers Arch. 436:117-126(1998).
RN   [5]
RP   FUNCTION, MASS SPECTROMETRY, AND SYNTHESIS.
RX   PubMed=14596608; DOI=10.1021/bi030091n;
RA   Alewood D., Birinyi-Strachan L.C., Pallaghy P.K., Norton R.S.,
RA   Nicholson G.M., Alewood P.F.;
RT   "Synthesis and characterization of delta-atracotoxin-Ar1a, the lethal
RT   neurotoxin from venom of the Sydney funnel-web spider (Atrax robustus).";
RL   Biochemistry 42:12933-12940(2003).
RN   [6]
RP   STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX   PubMed=9428632; DOI=10.1016/s0014-5793(97)01452-x;
RA   Pallaghy P.K., Alewood D., Alewood P.F., Norton R.S.;
RT   "Solution structure of robustoxin, the lethal neurotoxin from the funnel-
RT   web spider Atrax robustus.";
RL   FEBS Lett. 419:191-196(1997).
RN   [7]
RP   STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX   PubMed=10080353; DOI=10.1016/s0041-0101(98)00186-x;
RA   Temple M.D., Hinds M.G., Sheumack D.D., Howden M.E., Norton R.S.;
RT   "1H NMR study of robustoxin, the lethal neurotoxin from the funnel web
RT   spider Atrax robustus.";
RL   Toxicon 37:485-506(1999).
CC   -!- FUNCTION: Inhibits tetrodotoxin-sensitive voltage-gated sodium channels
CC       (Nav) by binding to site 3. It slows the inactivation, causes a
CC       prolongation of action potential duration resulting in repetitive
CC       firing in autonomic and motor nerve fibers. Does not depolarize the
CC       resting potential. Does not affect tetrodotoxin-resistant sodium
CC       channels. This lethal neurotoxin is active on both insect and mammalian
CC       voltage-gated sodium channels. {ECO:0000269|PubMed:14596608,
CC       ECO:0000269|PubMed:2728033, ECO:0000269|PubMed:9560455,
CC       ECO:0000269|PubMed:9845331}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3972101}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:3972101}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000269|PubMed:10080353, ECO:0000269|PubMed:9428632}.
CC   -!- MASS SPECTROMETRY: Mass=4848.7; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:14596608};
CC   -!- MISCELLANEOUS: In this species, the venom of the male is lethal rather
CC       than that of the female.
CC   -!- SIMILARITY: Belongs to the neurotoxin 06 (delta-actx) family.
CC       {ECO:0000305}.
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DR   PIR; A01738; NTIIRF.
DR   PDB; 1QDP; NMR; -; A=1-42.
DR   PDBsum; 1QDP; -.
DR   AlphaFoldDB; P01478; -.
DR   SMR; P01478; -.
DR   ArachnoServer; AS000305; delta-hexatoxin-Ar1a.
DR   EvolutionaryTrace; P01478; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR008017; Atracotoxin_delta.
DR   Pfam; PF05353; Atracotoxin; 1.
DR   PROSITE; PS60018; DELTA_ACTX; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Knottin; Neurotoxin; Secreted; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   CHAIN           1..42
FT                   /note="Delta-hexatoxin-Ar1a"
FT                   /evidence="ECO:0000269|PubMed:3972101"
FT                   /id="PRO_0000087653"
FT   DISULFID        1..15
FT                   /evidence="ECO:0000269|PubMed:10080353,
FT                   ECO:0000269|PubMed:9428632, ECO:0000312|PDB:1QDP"
FT   DISULFID        8..20
FT                   /evidence="ECO:0000269|PubMed:10080353,
FT                   ECO:0000269|PubMed:9428632, ECO:0000312|PDB:1QDP"
FT   DISULFID        14..31
FT                   /evidence="ECO:0000269|PubMed:10080353,
FT                   ECO:0000269|PubMed:9428632, ECO:0000312|PDB:1QDP"
FT   DISULFID        16..42
FT                   /evidence="ECO:0000269|PubMed:10080353,
FT                   ECO:0000269|PubMed:9428632, ECO:0000312|PDB:1QDP"
FT   STRAND          19..21
FT                   /evidence="ECO:0007829|PDB:1QDP"
FT   STRAND          30..33
FT                   /evidence="ECO:0007829|PDB:1QDP"
FT   TURN            37..39
FT                   /evidence="ECO:0007829|PDB:1QDP"
SQ   SEQUENCE   42 AA;  4857 MW;  093CF5D89540E284 CRC64;
     CAKKRNWCGK NEDCCCPMKC IYAWYNQQGS CQTTITGLFK KC
 
 
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