TXLA1_CYRSC
ID TXLA1_CYRSC Reviewed; 83 AA.
AC Q86C51;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=U5-theraphotoxin-Hs1a 1;
DE Short=U5-TRTX-Hs1a;
DE AltName: Full=Huwenlectin-1;
DE AltName: Full=Huwenlectin-I;
DE AltName: Full=SHLP-I;
DE Short=SHL-I;
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 50-81, AND FUNCTION.
RC TISSUE=Venom;
RX PubMed=8588212; DOI=10.1016/0041-0101(95)00033-i;
RA Liang S.-P., Pan X.;
RT "A lectin-like peptide isolated from the venom of the Chinese bird spider
RT Selenocosmia huwena.";
RL Toxicon 33:875-882(1995).
RN [3]
RP DISULFIDE BONDS, AND MASS SPECTROMETRY.
RX PubMed=10499419; DOI=10.1016/s0196-9781(99)00096-0;
RA Li F., Liang S.-P.;
RT "Assignment of the three disulfide bonds of Selenocosmia huwena lectin-I
RT from the venom of spider Selenocosmia huwena.";
RL Peptides 20:1027-1034(1999).
RN [4]
RP STRUCTURE BY NMR OF 50-81, AND DISULFIDE BOND.
RC TISSUE=Venom;
RX PubMed=10524779; DOI=10.1023/a:1020663619657;
RA Lu S.-Y., Liang S.-P., Gu X.-C.;
RT "Three-dimensional structure of Selenocosmia huwena lectin-I (SHL-I) from
RT the venom of the spider Selenocosmia huwena by 2D-NMR.";
RL J. Protein Chem. 18:609-617(1999).
CC -!- FUNCTION: Agglutinates human and mice erythrocytes. This activity can
CC be specifically inhibited by mannosamine. This lectin shows very low
CC toxicity in both mammals and insects. {ECO:0000269|PubMed:8588212}.
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.
CC -!- MASS SPECTROMETRY: Mass=3539.9; Mass_error=1; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10499419};
CC -!- MISCELLANEOUS: Exists in two forms, due to cis-trans isomerization at
CC Gly-79-Pro-80. The trans isomer is the most abundant (75%).
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; AY263708; AAP33075.1; -; mRNA.
DR PDB; 1QK7; NMR; -; A=50-81.
DR PDBsum; 1QK7; -.
DR AlphaFoldDB; Q86C51; -.
DR SMR; Q86C51; -.
DR UniLectin; Q86C51; -.
DR ArachnoServer; AS000355; U5-theraphotoxin-Hs1a.
DR EvolutionaryTrace; Q86C51; -.
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: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 3D-structure; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Knottin; Lectin; Secreted;
KW Signal; Toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..49
FT /evidence="ECO:0000269|PubMed:8588212"
FT /id="PRO_0000035562"
FT CHAIN 50..81
FT /note="U5-theraphotoxin-Hs1a 1"
FT /id="PRO_0000035563"
FT DISULFID 51..63
FT /evidence="ECO:0000269|PubMed:10499419,
FT ECO:0000269|PubMed:10524779, ECO:0000312|PDB:1QK7"
FT DISULFID 56..68
FT /evidence="ECO:0000269|PubMed:10499419,
FT ECO:0000269|PubMed:10524779, ECO:0000312|PDB:1QK7"
FT DISULFID 62..75
FT /evidence="ECO:0000269|PubMed:10499419,
FT ECO:0000269|PubMed:10524779, ECO:0000312|PDB:1QK7"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1QK7"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1QK7"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1QK7"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:1QK7"
SQ SEQUENCE 83 AA; 9379 MW; CAAF83406599B7C2 CRC64;
MKTSMFLTLT GLGLLFVVCY ASESEEKEFP KELLSSIFAA DSDFKVEERG CLGDKCDYNN
GCCSGYVCSR TWKWCVLAGP WRR
