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TX35A_PHORI
ID   TX35A_PHORI             Reviewed;          40 AA.
AC   P0DPG7;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2018, sequence version 1.
DT   25-MAY-2022, entry version 10.
DE   RecName: Full=Beta/delta-ctenitoxin-Pr1a {ECO:0000305};
DE            Short=Beta/delta-CNTX-Pr1a {ECO:0000305};
DE   AltName: Full=Beta/delta-PrIT1 {ECO:0000303|PubMed:26220799};
DE   Flags: Fragment;
OS   Phoneutria reidyi (Brazilian Amazonian armed spider) (Ctenus reidyi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Entelegynae; Lycosoidea; Ctenidae; Phoneutria.
OX   NCBI_TaxID=272752;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, TOXIC DOSE, MASS SPECTROMETRY, SUBCELLULAR
RP   LOCATION, AND BIOASSAY.
RC   TISSUE=Venom;
RX   PubMed=26220799; DOI=10.1016/j.toxicon.2015.07.010;
RA   de Oliveira L.C., Campos F.V., Figueiredo S.G., Cordeiro M.N., Adaime B.R.,
RA   Richardson M., Pimenta A.M., Martin-Eauclaire M.F., Beirao P.S.,
RA   De Lima M.E.;
RT   "beta/delta-PrIT1, a highly insecticidal toxin from the venom of the
RT   Brazilian spider Phoneutria reidyi (F.O. Pickard-Cambridge, 1897).";
RL   Toxicon 104:73-82(2015).
CC   -!- FUNCTION: Potent insecticidal toxin that binds to two distinct sites in
CC       insect sodium channels, with close affinity (Kd1=34.7 pM and Kd2=35.1
CC       pM) (PubMed:26220799). Its association is rather fast (1.4 and 8.5
CC       minutes, respectively for sites 1 and 2) and its dissociation is a
CC       slower process (5.4 and 32.8 minutes, respectively) (PubMed:26220799).
CC       On rat brain synaptosomes the toxin partially competes (~30%) with the
CC       beta-toxin CssIV, but does not compete with the alpha-toxin AaII, nor
CC       with the beta-toxin Ts VII (PubMed:26220799). On cockroach nerve cord
CC       synaptosomes, the toxin does not compete with the anti-insect toxin
CC       LqqIT1, but it competes with the 'alpha-like' toxin BomIV (IC(50)=80
CC       pM) (PubMed:26220799). In cockroach neurons, the toxin inhibits the
CC       inactivation of sodium channels and it shifts the sodium channel
CC       activation to hyperpolarizing potentials (PubMed:26220799). Hence, it
CC       behaves like an 'alpha-like' toxin and binds preferentially to site 3
CC       on the insect Nav channel, located on the domain IV (PubMed:26220799).
CC       The toxin may also inhibit the N-methyl-D-aspartate (NMDA)-subtype of
CC       ionotropic glutamate receptor (GRIN) (By similarity). In vivo, the
CC       toxin causes excitatory effects on insects (PubMed:26220799).
CC       {ECO:0000250|UniProtKB:P59367, ECO:0000269|PubMed:26220799}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26220799}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:26220799}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=5597.86; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:26220799};
CC   -!- TOXIC DOSE: LD(50) is 4 nmol/g in flies (M.domestica).
CC       {ECO:0000269|PubMed:26220799}.
CC   -!- TOXIC DOSE: LD(50) is 230 pmol/g in cockroaches (P.americana).
CC       {ECO:0000269|PubMed:26220799}.
CC   -!- MISCELLANEOUS: Is not toxic to mice (30 ug per mouse tested by
CC       intracerebroventricular injection). {ECO:0000269|PubMed:26220799}.
CC   -!- SIMILARITY: Belongs to the neurotoxin 03 (Tx2) family. 05 subfamily.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P0DPG7; -.
DR   SMR; P0DPG7; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0035792; C:host cell postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Ionotropic glutamate receptor inhibitor; Knottin; Neurotoxin;
KW   Postsynaptic neurotoxin; Secreted; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   CHAIN           1..>40
FT                   /note="Beta/delta-ctenitoxin-Pr1a"
FT                   /evidence="ECO:0000305|PubMed:26220799"
FT                   /id="PRO_0000444577"
FT   DISULFID        1..15
FT                   /evidence="ECO:0000305"
FT   DISULFID        8..21
FT                   /evidence="ECO:0000305"
FT   DISULFID        12..?
FT                   /evidence="ECO:0000305"
FT   DISULFID        14..31
FT                   /evidence="ECO:0000305"
FT   DISULFID        23..29
FT                   /evidence="ECO:0000305"
FT   NON_TER         40
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   40 AA;  4366 MW;  5EC28322DACFCB4D CRC64;
     CGDINAPCQS DCDCCGYSVT CDCYWGNECK CRESNFAIGM
 
 
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