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Omega-theraphotoxin-Hs2a (Omega-TRTX-Hs2a) (Huwentoxin-5) (Huwentoxin-V) (HwTx-V) [Cleaved into: Omega-theraphotoxin-Hs2b (Omega-TRTX-Hs2b) (Mutant of huwentoxin-5) (Mutant of huwentoxin-V) (mHWTX-V)]

 TXH5_HAPSC              Reviewed;          86 AA.
P61104;
26-APR-2004, integrated into UniProtKB/Swiss-Prot.
23-NOV-2004, sequence version 2.
20-JUN-2018, entry version 60.
RecName: Full=Omega-theraphotoxin-Hs2a;
Short=Omega-TRTX-Hs2a;
AltName: Full=Huwentoxin-5;
AltName: Full=Huwentoxin-V;
Short=HwTx-V;
Contains:
RecName: Full=Omega-theraphotoxin-Hs2b;
Short=Omega-TRTX-Hs2b;
AltName: Full=Mutant of huwentoxin-5;
AltName: Full=Mutant of huwentoxin-V;
Short=mHWTX-V;
Flags: Precursor;
Haplopelma schmidti (Chinese bird spider) (Ornithoctonus huwenum).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
Araneae; Mygalomorphae; Theraphosidae; Haplopelma.
NCBI_TaxID=29017;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Venom gland;
PubMed=14757201; DOI=10.1016/j.toxicon.2003.08.007;
Diao J., Lin Y., Tang J., Liang S.-P.;
"cDNA sequence analysis of seven peptide toxins from the spider
Selenocosmia huwena.";
Toxicon 42:715-723(2003).
[2]
PROTEIN SEQUENCE OF 51-85, DISULFIDE BONDS, PARALYTIC DOSE, MASS
SPECTROMETRY, AND DISRUPTION PHENOTYPE.
TISSUE=Venom;
PubMed=12893056; DOI=10.1016/S0041-0101(03)00095-3;
Zhang P.-F., Chen P., Hu W.-J., Liang S.-P.;
"Huwentoxin-V, a novel insecticidal peptide toxin from the spider
Selenocosmia huwena, and a natural mutant of the toxin: indicates the
key amino acid residues related to the biological activity.";
Toxicon 42:15-20(2003).
[3]
FUNCTION.
PubMed=18234186; DOI=10.1016/j.ejphar.2007.12.014;
Deng M., Luo X., Meng E., Xiao Y., Liang S.;
"Inhibition of insect calcium channels by huwentoxin-V, a neurotoxin
from Chinese tarantula Ornithoctonus huwena venom.";
Eur. J. Pharmacol. 582:12-16(2008).
-!- FUNCTION: Omega-theraphotoxin-Hs2a blocks voltage-gated calcium
channels (Cav) in adult cockroach DUM neurons. Reversibly
paralyzes locusts and cockroaches, and causes death at high
doses,. {ECO:0000269|PubMed:18234186}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
-!- DOMAIN: The presence of a 'disulfide through disulfide knot'
structurally defines this protein as a knottin. {ECO:0000250}.
-!- MASS SPECTROMETRY: Mass=4111.4; Mass_error=0.4; Method=MALDI;
Range=51-85; Evidence={ECO:0000269|PubMed:12893056};
-!- MASS SPECTROMETRY: Mass=3877.1; Mass_error=0.4; Method=MALDI;
Range=51-83; Evidence={ECO:0000269|PubMed:12893056};
-!- DISRUPTION PHENOTYPE: Its natural mutant mHwTx-V shows no effect
on locusts, cockroaches, and mice. {ECO:0000269|PubMed:12893056}.
-!- TOXIC DOSE: PD(50) of HwTx-V is 16 +/- 5 mg/kg to locusts.
{ECO:0000269|PubMed:12893056}.
-!- MISCELLANEOUS: Has no effect on voltage-gated sodium or potassium
channels in DUM neurons. Has no effect on mice by intraabdominal
or intracerebroventricular injection (PubMed:18234186).
{ECO:0000305|PubMed:18234186}.
-!- SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 17
(Hntx-9) subfamily. {ECO:0000305}.
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ProteinModelPortal; P61104; -.
SMR; P61104; -.
TCDB; 8.B.5.3.4; the na(+)/k(+)/ca(2+) channel targeting tarantula huwentoxin (tht) family.
ArachnoServer; AS000333; omega-theraphotoxin-Hs2a.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
InterPro; IPR011696; Huwentoxin-1.
InterPro; IPR013140; Huwentoxin_CS1.
Pfam; PF07740; Toxin_12; 1.
PROSITE; PS60021; HWTX_1; 1.
1: Evidence at protein level;
Calcium channel impairing toxin; Direct protein sequencing;
Disulfide bond; Ion channel impairing toxin; Knottin; Neurotoxin;
Secreted; Signal; Toxin;
Voltage-gated calcium channel impairing toxin.
SIGNAL 1 20 {ECO:0000255}.
PROPEP 21 50 {ECO:0000269|PubMed:12893056}.
/FTId=PRO_0000035567.
CHAIN 51 85 Omega-theraphotoxin-Hs2a.
/FTId=PRO_0000035568.
CHAIN 51 83 Omega-theraphotoxin-Hs2b.
/FTId=PRO_0000035569.
DISULFID 52 66 {ECO:0000250}.
DISULFID 59 71 {ECO:0000250}.
DISULFID 65 78 {ECO:0000250}.
SEQUENCE 86 AA; 9659 MW; DAFED9BE7D66FAF4 CRC64;
MKSIVFVALF GLALLAVVCS ASEDAHKELL KEVVRAMVVD KTDAVQAEER ECRWYLGGCS
QDGDCCKHLQ CHSNYEWCVW DGTFSK


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