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Mu-theraphotoxin-Hs1a (Mu-TRTX-Hs1a) (Huwentoxin-3) (Huwentoxin-III) (HwTx-III) [Cleaved into: U2-theraphotoxin-Hs1b (U2-TRTX-Hs1b) (HWTX-IIIa) (Mutant of huwentoxin-3) (Mutant of huwentoxin-III) (mHWTX-III)]

 TXH3_HAPSC              Reviewed;          87 AA.
P61103;
26-APR-2004, integrated into UniProtKB/Swiss-Prot.
23-NOV-2004, sequence version 2.
20-JUN-2018, entry version 59.
RecName: Full=Mu-theraphotoxin-Hs1a;
Short=Mu-TRTX-Hs1a;
AltName: Full=Huwentoxin-3;
AltName: Full=Huwentoxin-III {ECO:0000303|PubMed:14614533};
Short=HwTx-III {ECO:0000303|PubMed:14614533};
Contains:
RecName: Full=U2-theraphotoxin-Hs1b;
Short=U2-TRTX-Hs1b;
AltName: Full=HWTX-IIIa;
AltName: Full=Mutant of huwentoxin-3;
AltName: Full=Mutant of huwentoxin-III;
Short=mHWTX-III;
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 53-85, FUNCTION, DISULFIDE BONDS, PARALYTIC DOSE,
MASS SPECTROMETRY, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
TISSUE=Venom;
PubMed=14614533;
Huang R.-H., Liu Z.-H., Liang S.-P.;
"Purification and characterization of a neurotoxic peptide huwentoxin-
III and a natural inactive mutant from the venom of the spider
Selenocosmia huwena Wang (Ornithoctonus huwena Wang).";
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 35:976-980(2003).
[3]
FUNCTION.
PubMed=20506577; DOI=10.1631/jzus.B0900393;
Wang R.L., Yi S., Liang S.P.;
"Mechanism of action of two insect toxins huwentoxin-III and
hainantoxin-VI on voltage-gated sodium channels.";
J. Zhejiang Univ. Sci. B 11:451-457(2010).
-!- FUNCTION: Huwentoxin-3: Probable sodium channel pore blocker that
dose-dependently inhibits voltage-gated sodium channels (VGSC) on
DUM neurons in a way similar to tetrodotoxin (PubMed:20506577).
Has no effect on the kinetics of activation and inactivation
(PubMed:20506577). Seems not to interact with VGSC in an
inactivated state (PubMed:20506577). In vivo, reversibly paralyzes
cockroaches, and can enhance the muscular contraction elicited by
stimulating its nerve (PubMed:14614533).
{ECO:0000269|PubMed:14614533, ECO:0000269|PubMed:20506577}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14614533}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
-!- DOMAIN: The presence of a 'disulfide through disulfide knot'
structurally defines this protein as a knottin. {ECO:0000250}.
-!- MASS SPECTROMETRY: Mass=3853.35; Method=MALDI; Range=53-85;
Evidence={ECO:0000269|PubMed:14614533};
-!- MASS SPECTROMETRY: Mass=3667.40; Method=MALDI; Range=53-84;
Evidence={ECO:0000269|PubMed:14614533};
-!- DISRUPTION PHENOTYPE: The natural mutant mHwTx-III does not
reversibly paralyze cockroaches. {ECO:0000269|PubMed:14614533}.
-!- TOXIC DOSE: PD(50) of HwTx-III is 192.95 +/- 120.84 mg/kg to
locusts. {ECO:0000269|PubMed:14614533}.
-!- MISCELLANEOUS: Does not inhibit sodium channels of adult rat DRG
neurons (PubMed:20506577). Neither HwTx-III, nor mHwTx-III
agglutinate erythrocytes (PubMed:14614533).
{ECO:0000269|PubMed:14614533, ECO:0000269|PubMed:20506577}.
-!- SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 51
(Hntx-8) subfamily. Hntx-8 sub-subfamily. {ECO:0000305}.
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ProteinModelPortal; P61103; -.
SMR; P61103; -.
ArachnoServer; AS000331; mu-theraphotoxin-Hs1a.
ArachnoServer; AS000754; U2-theraphotoxin-Hs1b.
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;
Cleavage on pair of basic residues; Direct protein sequencing;
Disulfide bond; Ion channel impairing toxin; Knottin; Neurotoxin;
Secreted; Signal; Toxin; Voltage-gated sodium channel impairing toxin.
SIGNAL 1 24 {ECO:0000255}.
PROPEP 25 52 {ECO:0000269|PubMed:14614533}.
/FTId=PRO_0000035564.
CHAIN 53 85 Mu-theraphotoxin-Hs1a.
{ECO:0000269|PubMed:14614533}.
/FTId=PRO_0000035565.
CHAIN 53 84 U2-theraphotoxin-Hs1b.
/FTId=PRO_0000035566.
DISULFID 54 67 {ECO:0000250}.
DISULFID 61 72 {ECO:0000250}.
DISULFID 66 79 {ECO:0000250}.
SEQUENCE 87 AA; 10155 MW; E9ABB859D99BB8FE CRC64;
MVNMKASMFL TFAGLVLLFV VCYASESEEK EFPKEMLSSI FAVDNDFKQE ERDCAGYMRE
CKEKLCCSGY VCSSRWKWCV LPAPWRR


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