TXLB1_CYRSC
ID TXLB1_CYRSC Reviewed; 83 AA.
AC B3FIS6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=U5-theraphotoxin-Hs1b 1 {ECO:0000305};
DE Short=U5-TRTX-Hs1b {ECO:0000305};
DE AltName: Full=Lectin SHL-Ib1 {ECO:0000303|PubMed:18482741};
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=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).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 50-81, FUNCTION, SYNTHESIS OF
RP 50-81, AND DISULFIDE BONDS.
RX PubMed=29483648; DOI=10.1038/s41594-018-0033-9;
RA Correnti C.E., Gewe M.M., Mehlin C., Bandaranayake A.D., Johnsen W.A.,
RA Rupert P.B., Brusniak M.Y., Clarke M., Burke S.E., De Van Der Schueren W.,
RA Pilat K., Turnbaugh S.M., May D., Watson A., Chan M.K., Bahl C.D.,
RA Olson J.M., Strong R.K.;
RT "Screening, large-scale production and structure-based classification of
RT cystine-dense peptides.";
RL Nat. Struct. Mol. Biol. 25:270-278(2018).
CC -!- FUNCTION: Weakly inhibits 5HT3A receptors and Kv1.3/KCNA3 voltage-gated
CC potassium channels (PubMed:29483648). Agglutinates erythrocytes (By
CC similarity). {ECO:0000250|UniProtKB:Q86C51,
CC ECO:0000269|PubMed:29483648}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:18482741}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:18482741}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin.
CC -!- SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 51 (Hntx-8)
CC subfamily. Hntx-8 sub-subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EU195270; ABY77723.1; -; mRNA.
DR PDB; 6AV8; X-ray; 1.89 A; A=50-82.
DR PDBsum; 6AV8; -.
DR AlphaFoldDB; B3FIS6; -.
DR SMR; B3FIS6; -.
DR ArachnoServer; AS000698; U5-theraphotoxin-Hs1b.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR011696; Huwentoxin-1.
DR Pfam; PF07740; Toxin_12; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cleavage on pair of basic residues; Disulfide bond;
KW Ion channel impairing toxin; Knottin; Lectin;
KW Potassium channel impairing toxin; Secreted; Signal; Toxin;
KW Voltage-gated potassium channel impairing toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..49
FT /evidence="ECO:0000305"
FT /id="PRO_0000380174"
FT CHAIN 50..81
FT /note="U5-theraphotoxin-Hs1b 1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000380175"
FT DISULFID 51..63
FT /evidence="ECO:0000312|PDB:6AV8"
FT DISULFID 56..68
FT /evidence="ECO:0000312|PDB:6AV8"
FT DISULFID 62..75
FT /evidence="ECO:0000312|PDB:6AV8"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:6AV8"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:6AV8"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:6AV8"
SQ SEQUENCE 83 AA; 9477 MW; 987E1F556585190D CRC64;
MKTSMFLTLT GLVLLFVVCY ASESEEKEFP KELLSSIFAA DSDFKEEERG CFGYKCDYYK
GCCSGYVCSP TWKWCVRPGP GRR