SCAS_MESMA
ID SCAS_MESMA Reviewed; 85 AA.
AC Q9UAC9;
DT 19-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Beta-toxin BmKAS;
DE Short=BmK AS;
DE Short=BmK-AS;
DE AltName: Full=BmK-PL;
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 [GENOMIC DNA].
RC TISSUE=Venom gland;
RX PubMed=10219991; DOI=10.1016/s0041-0101(98)00221-9;
RA Lan Z.-D., Dai L., Zhuo X.-L., Feng J.-C., Xu K., Chi C.-W.;
RT "Gene cloning and sequencing of BmK AS and BmK AS-1, two novel neurotoxins
RT from the scorpion Buthus martensi Karsch.";
RL Toxicon 37:815-823(1999).
RN [2]
RP PROTEIN SEQUENCE OF 20-85, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=10080355; DOI=10.1016/s0041-0101(98)00190-1;
RA Ji Y.-H., Li Y.-J., Zhang J.-W., Song B.-L., Yamaki T., Mochizuki T.,
RA Hoshino M., Yanaihara N.;
RT "Covalent structures of BmK AS and BmK AS-1, two novel bioactive
RT polypeptides purified from Chinese scorpion Buthus martensi Karsch.";
RL Toxicon 37:519-536(1999).
RN [3]
RP FUNCTION.
RA Ji Y.-H., Huang H.-Y., Zhou C.-W., Liu Y., Hoshino M., Mochizuki T.,
RA Yanaihara N.;
RT "BmK AS, an active scorpion polypeptide, enhance [3H]-noradrenaline release
RT from rat hippocampal slices.";
RL Biomed. Res. 18:257-260(1997).
RN [4]
RP FUNCTION.
RX PubMed=10191265; DOI=10.1042/bj3390343;
RA Kuniyasu A., Kawano S., Hirayama Y., Ji Y.-H., Xu K., Ohkura M.,
RA Furukawa K., Ohizumi Y., Hiraoka M., Nakayama H.;
RT "A new scorpion toxin (BmK-PL) stimulates Ca2+-release channel activity of
RT the skeletal-muscle ryanodine receptor by an indirect mechanism.";
RL Biochem. J. 339:343-350(1999).
RN [5]
RP FUNCTION.
RX PubMed=10956424;
RX DOI=10.1002/1097-4547(20000901)61:5<541::aid-jnr9>3.0.co;2-#;
RA Li Y.-J., Liu Y., Ji Y.-H.;
RT "BmK AS: new scorpion neurotoxin binds to distinct receptor sites of mammal
RT and insect voltage-gated sodium channels.";
RL J. Neurosci. Res. 61:541-548(2000).
RN [6]
RP FUNCTION.
RX PubMed=12376194; DOI=10.1016/s0006-8993(02)03241-9;
RA Chen B., Ji Y.-H.;
RT "Antihyperalgesia effect of BmK AS, a scorpion toxin, in rat by
RT intraplantar injection.";
RL Brain Res. 952:322-326(2002).
RN [7]
RP FUNCTION.
RX PubMed=12668252; DOI=10.1016/s0304-3940(03)00094-6;
RA Tan Z.-Y., Chen J., Shun H.-Y., Feng X.-H., Ji Y.-H.;
RT "Modulation of BmK AS, a scorpion neurotoxic polypeptide, on voltage-gated
RT Na+ channels in B104 neuronal cell line.";
RL Neurosci. Lett. 340:123-126(2003).
RN [8]
RP FUNCTION.
RX PubMed=15106823; DOI=10.1097/00001756-200401190-00004;
RA Tan Z.-Y., Chen J., Feng X.-H., Susumu T., Ji Y.-H.;
RT "Modulation of intracellular Na+ concentration by BmK AS, a scorpion toxin,
RT in B104 cell line.";
RL NeuroReport 15:13-16(2004).
RN [9]
RP FUNCTION.
RX PubMed=16716457; DOI=10.1016/j.peptides.2006.03.026;
RA Chen J., Feng X.-H., Shi J., Tan Z.-Y., Bai Z.-T., Liu T., Ji Y.-H.;
RT "The anti-nociceptive effect of BmK AS, a scorpion active polypeptide, and
RT the possible mechanism on specifically modulating voltage-gated Na+
RT currents in primary afferent neurons.";
RL Peptides 27:2182-2192(2006).
CC -!- FUNCTION: Beta toxins bind voltage-independently at site-4 of sodium
CC channels (Nav) and shift the voltage of activation toward more negative
CC potentials thereby affecting sodium channel activation and promoting
CC spontaneous and repetitive firing. It binds to distinct receptor sites
CC of mammal and insect voltage-gated sodium channels. It displays
CC antinociceptive effect in rat models, which is due to its specific
CC modulation of sodium channels of sensory neurons. It also significantly
CC stimulates the binding of [3H]-ryanodine to ryanodine receptors on the
CC sarcoplasmic reticulum of the skeletal muscle through an indirect
CC mechanism. And it promotes noradrenaline release from the rat
CC hippocampus slice. {ECO:0000269|PubMed:10191265,
CC ECO:0000269|PubMed:10956424, ECO:0000269|PubMed:12376194,
CC ECO:0000269|PubMed:12668252, ECO:0000269|PubMed:15106823,
CC ECO:0000269|PubMed:16716457, ECO:0000269|Ref.3}.
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 -!- MASS SPECTROMETRY: Mass=7693.7; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10080355};
CC -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC Sodium channel inhibitor family. {ECO:0000305}.
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DR EMBL; AF079060; AAD47374.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9UAC9; -.
DR SMR; Q9UAC9; -.
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 Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Neurotoxin; Secreted; Signal; Toxin;
KW Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:10080355"
FT CHAIN 20..85
FT /note="Beta-toxin BmKAS"
FT /id="PRO_0000035262"
FT DOMAIN 20..82
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 31..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 35..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 42..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 46..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT CONFLICT 82
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 85 AA; 9759 MW; 41286F9DDCD4FE90 CRC64;
MKTVIFLIVS SLLLIGVKTD NGYLLDKYTG CKVWCVINNE SCNSECKIRG GYYGYCYFWK
LACFCQGARK SELWNYNTNK CNGKL
