TXH10_CYRSC
ID TXH10_CYRSC Reviewed; 68 AA.
AC P68424; B3FIU3;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Omega-theraphotoxin-Hs1a;
DE Short=Omega-TRTX-Hs1a;
DE AltName: Full=Huwentoxin-10;
DE AltName: Full=Huwentoxin-X;
DE Short=HwTx-X;
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], PROTEIN SEQUENCE OF 41-68, SYNTHESIS OF 41-68,
RP FUNCTION, MASS SPECTROMETRY, STRUCTURE BY NMR OF 41-68, DISULFIDE BONDS,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=16439354; DOI=10.1074/jbc.m513542200;
RA Liu Z., Dai J., Dai L., Deng M., Hu Z., Hu W., Liang S.;
RT "Function and solution structure of Huwentoxin-X, a specific blocker of N-
RT type calcium channels, from the Chinese bird spider Ornithoctonus huwena.";
RL J. Biol. Chem. 281:8628-8635(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=18482741; DOI=10.1016/j.toxicon.2008.03.024;
RA Jiang L., Peng L., Chen J., Zhang Y., Xiong X., Liang S.;
RT "Molecular diversification based on analysis of expressed sequence tags
RT from the venom glands of the Chinese bird spider Ornithoctonus huwena.";
RL Toxicon 51:1479-1489(2008).
CC -!- FUNCTION: Reversibly blocks N-type calcium channels (Cav2.2/CACNA1B) in
CC rat dorsal root ganglion cells (IC(50)=40 nM). Elicits no toxic
CC symptoms in either vertebrates or invertebrates during a period of 48
CC hours post-injection, when it was assayed in vivo by direct injection
CC into mice and cockroaches. {ECO:0000269|PubMed:16439354}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16439354}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:16439354}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin.
CC -!- MASS SPECTROMETRY: Mass=2931.34; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16439354};
CC -!- SIMILARITY: Belongs to the neurotoxin 36 family. 02 subfamily.
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DR EMBL; EU195287; ABY77740.1; -; mRNA.
DR PDB; 1Y29; NMR; -; A=41-68.
DR PDBsum; 1Y29; -.
DR AlphaFoldDB; P68424; -.
DR SMR; P68424; -.
DR TCDB; 8.B.4.1.5; the conotoxin t (conotoxin t) family.
DR ArachnoServer; AS000325; omega-theraphotoxin-Hs1a.
DR EvolutionaryTrace; P68424; -.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium channel impairing toxin; Direct protein sequencing;
KW Disulfide bond; Ion channel impairing toxin; Knottin; Neurotoxin; Secreted;
KW Signal; Toxin; Voltage-gated calcium channel impairing toxin.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..40
FT /evidence="ECO:0000269|PubMed:16439354"
FT /id="PRO_0000249420"
FT PEPTIDE 41..68
FT /note="Omega-theraphotoxin-Hs1a"
FT /id="PRO_0000045010"
FT DISULFID 42..59
FT /evidence="ECO:0000269|PubMed:16439354,
FT ECO:0000312|PDB:1Y29"
FT DISULFID 49..62
FT /evidence="ECO:0000269|PubMed:16439354,
FT ECO:0000312|PDB:1Y29"
FT DISULFID 58..67
FT /evidence="ECO:0000269|PubMed:16439354,
FT ECO:0000312|PDB:1Y29"
FT CONFLICT 27..29
FT /note="Missing (in Ref. 2; ABY77740)"
FT /evidence="ECO:0000305"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:1Y29"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:1Y29"
SQ SEQUENCE 68 AA; 7521 MW; 5E1BB224C5B6B803 CRC64;
MNMKILVLVA VLCLVVSTHA ERHSKTDMED MEDSPMIQER KCLPPGKPCY GATQKIPCCG
VCSHNKCT
