SCX9_MESMA
ID SCX9_MESMA Reviewed; 79 AA.
AC P45698;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Neurotoxin BmK-M9;
DE Short=BmK9;
DE Short=Bmk M9;
DE Short=BmkM9;
DE AltName: Full=BmK-IX;
DE Flags: Precursor;
OS Mesobuthus martensii (Manchurian scorpion) (Buthus martensii).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Mesobuthus.
OX NCBI_TaxID=34649;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=12219227;
RA Xiong Y.-M., Ling M.-H., Chi C.-W., Wang D.-C.;
RT "cDNA sequences of two anti-mammal neurotoxins from Scorpion Buthus
RT martensii Karsch.";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 29:200-205(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 15-78, AND DISULFIDE BONDS.
RX PubMed=1522588; DOI=10.1016/0022-2836(92)90694-f;
RA Zhao B., Carson M., Ealick S.E., Bugg C.E.;
RT "Structure of scorpion toxin variant-3 at 1.2-A resolution.";
RL J. Mol. Biol. 227:239-252(1992).
CC -!- FUNCTION: Binds to sodium channels (Nav) and inhibits the inactivation
CC of the activated channels, thereby blocking neuronal transmission. This
CC toxin is active against mammals.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to
CC antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC Sodium channel inhibitor family. Alpha subfamily. {ECO:0000305}.
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DR EMBL; U28660; AAA69558.1; -; mRNA.
DR AlphaFoldDB; P45698; -.
DR SMR; P45698; -.
DR EvolutionaryTrace; P45698; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:InterPro.
DR CDD; cd00107; Knot1; 1.
DR Gene3D; 3.30.30.10; -; 1.
DR InterPro; IPR044062; LCN-type_CS_alpha_beta_dom.
DR InterPro; IPR003614; Scorpion_toxin-like.
DR InterPro; IPR036574; Scorpion_toxin-like_sf.
DR InterPro; IPR018218; Scorpion_toxinL.
DR InterPro; IPR002061; Scorpion_toxinL/defensin.
DR Pfam; PF00537; Toxin_3; 1.
DR PRINTS; PR00285; SCORPNTOXIN.
DR SMART; SM00505; Knot1; 1.
DR SUPFAM; SSF57095; SSF57095; 1.
DR PROSITE; PS51863; LCN_CSAB; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Ion channel impairing toxin; Neurotoxin; Secreted; Signal;
KW Toxin; Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..14
FT CHAIN 15..78
FT /note="Neurotoxin BmK-M9"
FT /id="PRO_0000035238"
FT PROPEP 79
FT /note="Removed by a carboxypeptidase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000035239"
FT DOMAIN 16..78
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 26..77
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT ECO:0000269|PubMed:1522588"
FT DISULFID 30..50
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT ECO:0000269|PubMed:1522588"
FT DISULFID 36..60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT ECO:0000269|PubMed:1522588"
FT DISULFID 40..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT ECO:0000269|PubMed:1522588"
SQ SEQUENCE 79 AA; 8756 MW; 2F633B33F66882B7 CRC64;
MISFALLLMT GVESVRDAYI AKPENCVYHC ATNEGCNKLC TDNGAESGYC QWGGRYGNAC
WCIKLPDRVP IRVPGKCHR
