CTXL1_HOTTS
ID CTXL1_HOTTS Reviewed; 35 AA.
AC P15229;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Chlorotoxin-like peptide Bs 8 {ECO:0000303|PubMed:10048185};
DE Short=Bs8 {ECO:0000303|PubMed:10048185};
DE AltName: Full=Peptide I {ECO:0000303|PubMed:2583272};
DE AltName: Full=Small toxin;
OS Hottentotta tamulus sindicus (Scorpion) (Buthus sindicus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Mesobuthus.
OX NCBI_TaxID=42519;
RN [1]
RP PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=2583272; DOI=10.1016/0014-5793(89)81548-0;
RA Fazal A., Beg O.U., Shafqat J., Zaidi Z.H., Joernvall H.;
RT "Characterization of two different peptides from the venom of the scorpion
RT Buthus sindicus.";
RL FEBS Lett. 257:260-262(1989).
RN [2]
RP PROTEIN SEQUENCE, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=10048185; DOI=10.1016/s1095-6433(98)10140-x;
RA Ali S.A., Stoeva S., Schuetz J., Kayed R., Abbasi A., Zaidi Z.H.,
RA Voelter W.;
RT "Purification and primary structure of low molecular mass peptides from
RT scorpion (Buthus sindicus) venom.";
RL Comp. Biochem. Physiol. 121A:323-332(1998).
CC -!- FUNCTION: Toxin with unknown function in healthy organisms. On glioma
CC cells, interacts with chloride channels (probably ClC-3/CLCN3) and MMP2
CC at the surface of glioma cells. This complex is then internalized via
CC caveolae, thus inhibiting the chloride channels necessary for cell
CC shrinkage and tumor propagation (By similarity).
CC {ECO:0000250|UniProtKB:Q9UAD0}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10048185,
CC ECO:0000269|PubMed:2583272}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:10048185, ECO:0000305|PubMed:2583272}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin.
CC {ECO:0000250|UniProtKB:P15222}.
CC -!- MASS SPECTROMETRY: Mass=3745.4; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10048185};
CC -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Chloride
CC channel inhibitor family. {ECO:0000255|PROSITE-ProRule:PRU00545}.
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DR PIR; S06667; S06667.
DR AlphaFoldDB; P15229; -.
DR SMR; P15229; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0017081; F:chloride channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR036574; Scorpion_toxin-like_sf.
DR InterPro; IPR007958; Scorpion_toxinS_Cl_inh.
DR Pfam; PF05294; Toxin_5; 1.
DR SUPFAM; SSF57095; SSF57095; 1.
DR PROSITE; PS51200; SHORT_SCORPION_CHLORIDE; 1.
PE 1: Evidence at protein level;
KW Chloride channel impairing toxin; Direct protein sequencing;
KW Disulfide bond; Ion channel impairing toxin; Knottin; Secreted; Toxin;
KW Voltage-gated chloride channel impairing toxin.
FT PEPTIDE 1..35
FT /note="Chlorotoxin-like peptide Bs 8"
FT /evidence="ECO:0000269|PubMed:10048185,
FT ECO:0000269|PubMed:2583272"
FT /id="PRO_0000044940"
FT DISULFID 2..19
FT /evidence="ECO:0000250|UniProtKB:P15222,
FT ECO:0000255|PROSITE-ProRule:PRU00545"
FT DISULFID 5..28
FT /evidence="ECO:0000250|UniProtKB:P15222,
FT ECO:0000255|PROSITE-ProRule:PRU00545"
FT DISULFID 16..33
FT /evidence="ECO:0000250|UniProtKB:P15222,
FT ECO:0000255|PROSITE-ProRule:PRU00545"
FT DISULFID 20..35
FT /evidence="ECO:0000250|UniProtKB:P15222,
FT ECO:0000255|PROSITE-ProRule:PRU00545"
SQ SEQUENCE 35 AA; 3746 MW; 7E16A1524D6B83B8 CRC64;
RCKPCFTTDP QMSKKCADCC GGKGKGKCYG PQCLC
