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TX20A_PHORI
ID   TX20A_PHORI             Reviewed;          43 AA.
AC   P83911;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Omega-ctenitoxin-Pr1a {ECO:0000305};
DE            Short=Omega-CNTX-Pr1a {ECO:0000305};
DE   AltName: Full=Neurotoxin PRTx17C3;
DE   AltName: Full=Neurotoxin PRTx3-7;
DE            Short=Tx3-7;
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 {ECO:0000305};
RN   [1]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND AMIDATION AT
RP   GLY-43.
RC   TISSUE=Venom;
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]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AMIDATION AT GLY-43, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=17151945; DOI=10.1007/s10571-006-9123-z;
RA   Vieira L.B., Pimenta A.M.C., Richardson M., Bemquerer M.P., Reis H.J.,
RA   Cruz J.S., Gomez M.V., Santoro M.M., Ferreira-de-Oliveira R.,
RA   Figueiredo S.G., Snutch T.P., Cordeiro M.N.;
RT   "Leftward shift in the voltage-dependence for Ca(2+) currents activation
RT   induced by a new toxin from Phoneutria reidyi (Aranae, ctenidae) Venom.";
RL   Cell. Mol. Neurobiol. 27:129-146(2007).
CC   -!- FUNCTION: Inhibits high-voltage activated calcium channels. Shifts the
CC       voltage-dependence for activation towards hyperpolarized membrane
CC       potentials for L- (Cav1), P/Q- (Cav2.1/CACNA1A) and R-type
CC       (Cav2.3/CACNA1E) calcium currents. Causes immediate agitation and
CC       clockwise gyration, followed by the gradual development of general
CC       flaccid paralysis when injected intracerebroventricular into mice at
CC       dose levels of 5 ug per mouse. {ECO:0000269|PubMed:17151945}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16278100,
CC       ECO:0000269|PubMed:17151945}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:16278100, ECO:0000305|PubMed:17151945}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000250|UniProtKB:P30288}.
CC   -!- MASS SPECTROMETRY: Mass=4627.26; Mass_error=0.3; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:17151945, ECO:0000305};
CC   -!- MASS SPECTROMETRY: Mass=4627.9; Method=Unknown;
CC       Evidence={ECO:0000269|PubMed:16278100, ECO:0000305};
CC   -!- SIMILARITY: Belongs to the neurotoxin 02 (plectoxin) family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P83911; -.
DR   SMR; P83911; -.
DR   ArachnoServer; AS000270; omega-ctenitoxin-Pr1a.
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:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   CDD; cd12960; Spider_toxin; 1.
DR   InterPro; IPR004169; Spidertoxin.
DR   Pfam; PF02819; Toxin_9; 1.
PE   1: Evidence at protein level;
KW   Amidation; Calcium channel impairing toxin; Direct protein sequencing;
KW   Disulfide bond; Ion channel impairing toxin; Knottin; Neurotoxin; Secreted;
KW   Toxin; Voltage-gated calcium channel impairing toxin.
FT   CHAIN           1..43
FT                   /note="Omega-ctenitoxin-Pr1a"
FT                   /evidence="ECO:0000269|PubMed:16278100,
FT                   ECO:0000269|PubMed:17151945"
FT                   /id="PRO_0000087639"
FT   MOD_RES         43
FT                   /note="Glycine amide"
FT                   /evidence="ECO:0000269|PubMed:16278100,
FT                   ECO:0000269|PubMed:17151945"
FT   DISULFID        2..17
FT                   /evidence="ECO:0000250|UniProtKB:P30288"
FT   DISULFID        9..22
FT                   /evidence="ECO:0000250|UniProtKB:P30288"
FT   DISULFID        16..33
FT                   /evidence="ECO:0000250|UniProtKB:P30288"
FT   DISULFID        24..31
FT                   /evidence="ECO:0000250|UniProtKB:P30288"
SQ   SEQUENCE   43 AA;  4640 MW;  52293FC743EFE2D8 CRC64;
     ACAGLYKKCG KGVNTCCENR PCKCDLAMGN CICKKKFVEF FGG
 
 
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