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TXH5_CYRSC
ID   TXH5_CYRSC              Reviewed;          86 AA.
AC   P61104;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 2.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Omega-theraphotoxin-Hs2a;
DE            Short=Omega-TRTX-Hs2a;
DE   AltName: Full=Huwentoxin-5;
DE   AltName: Full=Huwentoxin-V;
DE            Short=HwTx-V;
DE   Contains:
DE     RecName: Full=Omega-theraphotoxin-Hs2b;
DE              Short=Omega-TRTX-Hs2b;
DE     AltName: Full=Mutant of huwentoxin-5;
DE     AltName: Full=Mutant of huwentoxin-V;
DE              Short=mHWTX-V;
DE   Flags: Precursor;
OS   Cyriopagopus schmidti (Chinese bird spider) (Haplopelma schmidti).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Theraphosidae; Cyriopagopus.
OX   NCBI_TaxID=29017;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=14757201; DOI=10.1016/j.toxicon.2003.08.007;
RA   Diao J., Lin Y., Tang J., Liang S.-P.;
RT   "cDNA sequence analysis of seven peptide toxins from the spider
RT   Selenocosmia huwena.";
RL   Toxicon 42:715-723(2003).
RN   [2]
RP   PROTEIN SEQUENCE OF 51-85, DISULFIDE BONDS, TOXIC DOSE, MASS SPECTROMETRY,
RP   AND DISRUPTION PHENOTYPE.
RC   TISSUE=Venom;
RX   PubMed=12893056; DOI=10.1016/s0041-0101(03)00095-3;
RA   Zhang P.-F., Chen P., Hu W.-J., Liang S.-P.;
RT   "Huwentoxin-V, a novel insecticidal peptide toxin from the spider
RT   Selenocosmia huwena, and a natural mutant of the toxin: indicates the key
RT   amino acid residues related to the biological activity.";
RL   Toxicon 42:15-20(2003).
RN   [3]
RP   FUNCTION.
RX   PubMed=18234186; DOI=10.1016/j.ejphar.2007.12.014;
RA   Deng M., Luo X., Meng E., Xiao Y., Liang S.;
RT   "Inhibition of insect calcium channels by huwentoxin-V, a neurotoxin from
RT   Chinese tarantula Ornithoctonus huwena venom.";
RL   Eur. J. Pharmacol. 582:12-16(2008).
CC   -!- FUNCTION: Omega-theraphotoxin-Hs2a blocks voltage-gated calcium
CC       channels (Cav) in adult cockroach DUM neurons. Reversibly paralyzes
CC       locusts and cockroaches, and causes death at high doses,.
CC       {ECO:0000269|PubMed:18234186}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000250}.
CC   -!- MASS SPECTROMETRY: [Omega-theraphotoxin-Hs2a]: Mass=4111.4;
CC       Mass_error=0.4; Method=MALDI; Evidence={ECO:0000269|PubMed:12893056};
CC   -!- MASS SPECTROMETRY: [Omega-theraphotoxin-Hs2b]: Mass=3877.1;
CC       Mass_error=0.4; Method=MALDI; Evidence={ECO:0000269|PubMed:12893056};
CC   -!- DISRUPTION PHENOTYPE: Its natural mutant mHwTx-V shows no effect on
CC       locusts, cockroaches, and mice. {ECO:0000269|PubMed:12893056}.
CC   -!- TOXIC DOSE: PD(50) of HwTx-V is 16 +/- 5 mg/kg to locusts.
CC       {ECO:0000269|PubMed:12893056}.
CC   -!- MISCELLANEOUS: Has no effect on voltage-gated sodium or potassium
CC       channels in DUM neurons. Has no effect on mice by intraabdominal or
CC       intracerebroventricular injection (PubMed:18234186).
CC       {ECO:0000305|PubMed:18234186}.
CC   -!- SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 17 (Hntx-9)
CC       subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P61104; -.
DR   SMR; P61104; -.
DR   TCDB; 8.B.5.3.4; the na(+)/k(+)/ca(2+) channel targeting tarantula huwentoxin (tht) family.
DR   ArachnoServer; AS000333; omega-theraphotoxin-Hs2a.
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   InterPro; IPR011696; Huwentoxin-1.
DR   InterPro; IPR013140; Huwentoxin_CS1.
DR   Pfam; PF07740; Toxin_12; 1.
DR   PROSITE; PS60021; HWTX_1; 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; Signal; Toxin;
KW   Voltage-gated calcium channel impairing toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..50
FT                   /evidence="ECO:0000269|PubMed:12893056"
FT                   /id="PRO_0000035567"
FT   CHAIN           51..85
FT                   /note="Omega-theraphotoxin-Hs2a"
FT                   /id="PRO_0000035568"
FT   CHAIN           51..83
FT                   /note="Omega-theraphotoxin-Hs2b"
FT                   /id="PRO_0000035569"
FT   DISULFID        52..66
FT                   /evidence="ECO:0000250"
FT   DISULFID        59..71
FT                   /evidence="ECO:0000250"
FT   DISULFID        65..78
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   86 AA;  9659 MW;  DAFED9BE7D66FAF4 CRC64;
     MKSIVFVALF GLALLAVVCS ASEDAHKELL KEVVRAMVVD KTDAVQAEER ECRWYLGGCS
     QDGDCCKHLQ CHSNYEWCVW DGTFSK
 
 
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