SCX1_TITMA
ID SCX1_TITMA Reviewed; 65 AA.
AC C0HLL9;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2019, sequence version 1.
DT 03-AUG-2022, entry version 11.
DE RecName: Full=Beta-mammal toxin Tma1 {ECO:0000303|PubMed:31402191};
OS Tityus macrochirus (Scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX NCBI_TaxID=2599738 {ECO:0000303|PubMed:31402191};
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Venom {ECO:0000303|PubMed:31402191};
RX PubMed=31402191; DOI=10.1016/j.toxicon.2019.07.013;
RA Rincon-Cortes C.A., Olamendi-Portugal T., Carcamo-Noriega E.N.,
RA Santillan E.G., Zuniga F.Z., Reyes-Montano E.A., Vega Castro N.A.,
RA Possani L.D.;
RT "Structural and functional characterization of toxic peptides purified from
RT the venom of the Colombian scorpion Tityus macrochirus.";
RL Toxicon 169:5-11(2019).
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 (PubMed:31402191). This toxin acts on
CC human Nav1.4/SCN4A and Nav1.6/SCN8A voltage-gated sodium channels
CC (PubMed:31402191). {ECO:0000269|PubMed:31402191}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31402191}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:31402191}.
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. {ECO:0000305}.
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DR AlphaFoldDB; C0HLL9; -.
DR SMR; C0HLL9; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR GO; GO:0098542; P:defense response to other organism; IDA:UniProtKB.
DR GO; GO:0044493; P:envenomation resulting in negative regulation of voltage-gated sodium channel activity in another organism; IDA:UniProtKB.
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; Toxin; Voltage-gated sodium channel impairing toxin.
FT CHAIN 1..65
FT /note="Beta-mammal toxin Tma1"
FT /id="PRO_0000448248"
FT DOMAIN 2..64
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 12..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 16..38
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 24..44
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 28..46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ SEQUENCE 65 AA; 7396 MW; 57A6D13DCD8B2F2A CRC64;
KKEGYLVGND GCKYGCFTRP AQYCESECSL RKGTGGYCYA WLACYCYNMP DWVPTWNSAK
NRCGK
