TXH21_CYRSC
ID TXH21_CYRSC Reviewed; 85 AA.
AC P82959; Q86C50;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=U1-theraphotoxin-Hs1a;
DE Short=U1-TRTX-Hs1a;
DE AltName: Full=Huwentoxin-2 form 1;
DE AltName: Full=Huwentoxin-II;
DE Short=HwTx-II;
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 49-85, FUNCTION, MASS SPECTROMETRY, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Venom;
RX PubMed=10424342; DOI=10.1034/j.1399-3011.1999.00039.x;
RA Shu Q., Liang S.-P.;
RT "Purification and characterization of huwentoxin-II, a neurotoxic peptide
RT from the venom of the Chinese bird spider Selenocosmia huwena.";
RL J. Pept. Res. 53:486-491(1999).
RN [3]
RP DISULFIDE BONDS.
RX PubMed=11298747; DOI=10.1046/j.1432-1327.2001.02109.x;
RA Shu Q., Huang R., Liang S.-P.;
RT "Assignment of the disulfide bonds of huwentoxin-II by Edman degradation
RT sequencing and stepwise thiol modification.";
RL Eur. J. Biochem. 268:2301-2307(2001).
RN [4]
RP STRUCTURE BY NMR OF 49-85, AND DISULFIDE BONDS.
RX PubMed=11790834; DOI=10.1110/ps.30502;
RA Shu Q., Lu S.Y., Gu X.-C., Liang S.-P.;
RT "The structure of spider toxin huwentoxin-II with unique disulfide linkage:
RT evidence for structural evolution.";
RL Protein Sci. 11:245-252(2002).
CC -!- FUNCTION: Lethal neurotoxin that blocks neuromuscular transmission.
CC Acts cooperatively to potentiate the activity of huwentoxin-I. This
CC toxin is active against insects. {ECO:0000269|PubMed:10424342}.
CC -!- SUBUNIT: Heterodimer composed of the two variants Ile-58 and Gln-58.
CC {ECO:0000269|PubMed:10424342}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10424342}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:10424342}.
CC -!- MASS SPECTROMETRY: Mass=4290.3; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10424342};
CC -!- SIMILARITY: Belongs to the neurotoxin 12 (Hwtx-2) family. 02 (Hwtx-2)
CC subfamily. {ECO:0000305}.
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DR EMBL; AY263709; AAP33076.1; -; mRNA.
DR PDB; 1I25; NMR; -; A=49-85.
DR PDBsum; 1I25; -.
DR AlphaFoldDB; P82959; -.
DR SMR; P82959; -.
DR PRIDE; P82959; -.
DR ArachnoServer; AS000328; U1-theraphotoxin-Hs1a.
DR EvolutionaryTrace; P82959; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0035792; C:host cell postsynaptic membrane; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR012625; Toxin_20.
DR Pfam; PF08089; Toxin_20; 1.
DR PROSITE; PS60022; HWTX_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Neurotoxin;
KW Postsynaptic neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..48
FT /evidence="ECO:0000305|PubMed:10424342"
FT /id="PRO_0000035523"
FT CHAIN 49..85
FT /note="U1-theraphotoxin-Hs1a"
FT /evidence="ECO:0000269|PubMed:10424342"
FT /id="PRO_0000035524"
FT DISULFID 52..66
FT /evidence="ECO:0000269|PubMed:11298747,
FT ECO:0000269|PubMed:11790834, ECO:0000312|PDB:1I25"
FT DISULFID 56..77
FT /evidence="ECO:0000269|PubMed:11298747,
FT ECO:0000269|PubMed:11790834, ECO:0000312|PDB:1I25"
FT DISULFID 71..82
FT /evidence="ECO:0000269|PubMed:11298747,
FT ECO:0000269|PubMed:11790834, ECO:0000312|PDB:1I25"
FT VARIANT 58
FT /note="I -> Q"
FT /evidence="ECO:0000269|PubMed:10424342"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:1I25"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:1I25"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:1I25"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:1I25"
SQ SEQUENCE 85 AA; 9429 MW; 0681D27A17543842 CRC64;
MKVTLIAILT CAAVLVLHTT AAEELEAESQ LMEVGMPDTE LAAVDEERLF ECSFSCEIEK
EGDKPCKKKK CKGGWKCKFN MCVKV
