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SCAT_MESMA
ID   SCAT_MESMA              Reviewed;          85 AA.
AC   Q9UAC8;
DT   19-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Beta-toxin BmKAs1;
DE            Short=BmK AS-1;
DE   AltName: Full=BmK activator of skeletal-muscle ryanodine receptor;
DE   AltName: Full=Toxin BmP09;
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 DISULFIDE BONDS.
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   PROTEIN SEQUENCE OF 20-85, CHARACTERIZATION, MASS SPECTROMETRY, AND
RP   3D-STRUCTURE MODELING.
RC   TISSUE=Venom;
RX   PubMed=15695820; DOI=10.1074/jbc.m412735200;
RA   Yao J., Chen X., Li H., Zhou Y., Yao L., Wu G., Chen X., Zhang N., Zhou Z.,
RA   Xu T., Wu H., Ding J.;
RT   "BmP09, a 'long chain' scorpion peptide blocker of BK channels.";
RL   J. Biol. Chem. 280:14819-14828(2005).
RN   [4]
RP   FUNCTION.
RX   PubMed=10599845; DOI=10.1097/00001756-199911080-00019;
RA   Jia L.-Y., Zhang J.-W., Ji Y.-H.;
RT   "Biosensor binding assay of BmK AS-1, a novel Na+ channel-blocking scorpion
RT   ligand on rat brain synaptosomes.";
RL   NeuroReport 10:3359-3362(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=11780308;
RA   Xiao H., Mao X., Tan Z.-Y., Shi Y.-L., Zhao Z.-Q., Ji Y.-H.;
RT   "Modulation of BmKAS-1 and BmK1-3-2 to sodium channel in rat dorsal root
RT   ganglion neurons.";
RL   Chin. Med. J. 114:253-256(2001).
RN   [7]
RP   FUNCTION.
RX   PubMed=11491459;
RA   Wu Y., Ji Y.-H., Shi Y.-L.;
RT   "Sodium current in NG108-15 cell inhibited by scorpion toxin BmKAS-1 and
RT   restored by its specific monoclonal antibodies.";
RL   J. Nat. Toxins 10:193-198(2001).
RN   [8]
RP   FUNCTION.
RX   PubMed=11121871; DOI=10.1016/s0304-3940(00)01642-6;
RA   Tan Z.-Y., Mao X., Xiao H., Zhao Z.-Q., Ji Y.-H.;
RT   "Buthus martensi Karsch agonist of skeletal-muscle RyR-1, a scorpion active
RT   polypeptide: antinociceptive effect on rat peripheral nervous system and
RT   spinal cord, and inhibition of voltage-gated Na(+) currents in dorsal root
RT   ganglion neurons.";
RL   Neurosci. Lett. 297:65-68(2001).
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. BmKAs1 also significantly stimulates
CC       the binding of [3H]-ryanodine to ryanodine receptors on the
CC       sarcoplasmic reticulum of the skeletal muscle. It also displays
CC       antinociceptive effect in rat models.
CC   -!- FUNCTION: Toxin BmP09 (which may be post-translationally modified)
CC       specifically and reversibly blocks large conductance calcium-dependent
CC       and voltage-dependent potassium channels (BK) but has no effect on
CC       sodium channels.
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   -!- PTM: A possible sulfoxide Met-85 on BmP09 could explain the difference
CC       of function between BmK AS-1 and BmP09.
CC   -!- MASS SPECTROMETRY: Mass=7721; Method=Electrospray; Note=Toxin BmP09.;
CC       Evidence={ECO:0000269|PubMed:15695820};
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; AF079061; AAD47375.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9UAC8; -.
DR   SMR; Q9UAC8; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
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; Potassium channel impairing toxin; Secreted; Signal; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:10080355,
FT                   ECO:0000269|PubMed:15695820"
FT   CHAIN           20..85
FT                   /note="Beta-toxin BmKAs1"
FT                   /id="PRO_0000035263"
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                   ECO:0000269|PubMed:10080355"
FT   DISULFID        35..56
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT                   ECO:0000269|PubMed:10080355"
FT   DISULFID        42..63
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT                   ECO:0000269|PubMed:10080355"
FT   DISULFID        46..65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT                   ECO:0000269|PubMed:10080355"
SQ   SEQUENCE   85 AA;  9803 MW;  E2274838439E2B95 CRC64;
     MKIIIFLIVC SFVLIGVKAD NGYLLNKYTG CKIWCVINNE SCNSECKLRR GNYGYCYFWK
     LACYCEGAPK SELWAYETNK CNGKM
 
 
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