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TOPC5_PHONI
ID   TOPC5_PHONI             Reviewed;          80 AA.
AC   P84093;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=U20-ctenitoxin-Pn1a;
DE            Short=U20-CNTX-Pn1a;
DE   AltName: Full=Omega-phonetoxin PNTx22C5;
DE   Flags: Fragment;
OS   Phoneutria nigriventer (Brazilian armed spider) (Ctenus nigriventer).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Entelegynae; Lycosoidea; Ctenidae; Phoneutria.
OX   NCBI_TaxID=6918;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Venom {ECO:0000269|PubMed:16278100};
RX   PubMed=16278100; DOI=10.1016/j.cbpc.2005.09.010;
RA   Richardson M., Pimenta A.M., Bemquerer M.P., Santoro M.M., Beirao P.S.,
RA   Lima M.E., Figueiredo S.G., Bloch C. Jr., Vasconcelos E.A., Campos F.A.,
RA   Gomes P.C., Cordeiro M.N.;
RT   "Comparison of the partial proteomes of the venoms of Brazilian spiders of
RT   the genus Phoneutria.";
RL   Comp. Biochem. Physiol. 142:173-187(2006).
RN   [2] {ECO:0000305}
RP   FUNCTION.
RA   Richardson M., Pimenta A.M.C., Bemquerer M.P., Santoro M.M.,
RA   Figueiredo S.G., Cordeiro M.N.;
RT   "New lethal neurotoxin PNTx22C5 from venom of the Phoneutria nigriventer
RT   has sequence similarities with toxins PNTx1 and PNTx3-4 from the same
RT   spider and the omega agatoxins from Agelenopsis aperta.";
RL   Submitted (JUL-2004) to UniProtKB.
CC   -!- FUNCTION: Omega-agatoxin are antagonists of voltage-gated calcium
CC       channels (Cav). Induces rapid general flaccid paralysis followed by
CC       death when injected into the cerebral ventricle of mice at dose levels
CC       of 3 ug per mouse. {ECO:0000269|Ref.2}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16278100}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:16278100}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=9215.3; Mass_error=0.06; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:16278100};
CC   -!- SIMILARITY: Belongs to the neurotoxin 04 (omega-agtx) family. 03 (type
CC       II/III omega-agtx) subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P84093; -.
DR   ArachnoServer; AS000190; U20-ctenitoxin-Pn1a.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005246; F:calcium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR005853; Omega-agatoxin_II/III_CS.
DR   InterPro; IPR013605; Toxin_34.
DR   Pfam; PF08396; Toxin_34; 1.
DR   PROSITE; PS60023; OMEGA_AGA_II_III; 1.
PE   1: Evidence at protein level;
KW   Calcium channel impairing toxin; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Knottin; Neurotoxin; Secreted; Toxin;
KW   Voltage-gated calcium channel impairing toxin.
FT   CHAIN           1..>80
FT                   /note="U20-ctenitoxin-Pn1a"
FT                   /id="PRO_0000087612"
FT   DISULFID        3..20
FT                   /evidence="ECO:0000305"
FT   DISULFID        10..26
FT                   /evidence="ECO:0000305"
FT   DISULFID        17..52
FT                   /evidence="ECO:0000305"
FT   DISULFID        19..40
FT                   /evidence="ECO:0000305"
FT   DISULFID        28..38
FT                   /evidence="ECO:0000305"
FT   DISULFID        58..71
FT                   /evidence="ECO:0000255"
FT   DISULFID        75..80
FT                   /evidence="ECO:0000255"
FT   NON_TER         80
FT                   /evidence="ECO:0000303|Ref.2"
SQ   SEQUENCE   80 AA;  8869 MW;  2FFB79AA26501C5C CRC64;
     GNCIELNNDC DGSKDDCQCC RDNAYCSCYN FFGIKSGCKC SVGNSGTGYS VCLKKLECPN
     RRAWTSWKKE CTKPCIGKRC
 
 
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