ID   MTX2_GRARO              Reviewed;          31 AA.
AC   P60273;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Kappa-theraphotoxin-Gr2a {ECO:0000305};
DE            Short=Kappa-TRTX-Gr2a {ECO:0000305};
DE   AltName: Full=Toxin GsMTx-2 {ECO:0000303|PubMed:12082099};
DE            Short=MTx2 {ECO:0000303|PubMed:12082099};
OS   Grammostola rosea (Chilean rose tarantula) (Grammostola spatulata).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Theraphosidae; Grammostola.
OX   NCBI_TaxID=432528;
RN   [1]
RP   PROTEIN SEQUENCE, STRUCTURE BY NMR, DISULFIDE BONDS, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=12082099; DOI=10.1074/jbc.m202715200;
RA   Oswald R.E., Suchyna T.M., McFeeters R., Gottlieb P.A., Sachs F.;
RT   "Solution structure of peptide toxins that block mechanosensitive ion
RT   channels.";
RL   J. Biol. Chem. 277:34443-34450(2002).
CC   -!- FUNCTION: Blocks mammalian Kv4.2/KCND2 and Kv4.3/KCND3 (By similarity).
CC       Blocks mechanosensitive ion channels in rat astrocytes, without having
CC       effect on whole-cell voltage-sensitive currents (By similarity).
CC       {ECO:0000250|UniProtKB:P61231}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12082099}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:12082099}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000269|PubMed:12082099}.
CC   -!- MISCELLANEOUS: The primary structure of this mature peptide is
CC       identical to that of kappa-theraphotoxin-Ps1b (Phrixotoxin-2) from
CC       Paraphysa scrofa (AC P61231). {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the neurotoxin 30 (phrixotoxin) family.
CC       {ECO:0000305}.
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DR   PDB; 1LUP; NMR; -; A=1-31.
DR   PDBsum; 1LUP; -.
DR   AlphaFoldDB; P60273; -.
DR   SMR; P60273; -.
DR   ArachnoServer; AS000067; kappa-theraphotoxin-Gr2a.
DR   EvolutionaryTrace; P60273; -.
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:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Knottin; Neurotoxin;
KW   Potassium channel impairing toxin; Secreted; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   PEPTIDE         1..31
FT                   /note="Kappa-theraphotoxin-Gr2a"
FT                   /evidence="ECO:0000269|PubMed:12082099"
FT                   /id="PRO_0000045014"
FT   DISULFID        2..16
FT                   /evidence="ECO:0000269|PubMed:12082099,
FT                   ECO:0007744|PDB:1LUP"
FT   DISULFID        9..21
FT                   /evidence="ECO:0000269|PubMed:12082099,
FT                   ECO:0007744|PDB:1LUP"
FT   DISULFID        15..25
FT                   /evidence="ECO:0000269|PubMed:12082099,
FT                   ECO:0007744|PDB:1LUP"
FT   STRAND          4..6
FT                   /evidence="ECO:0007829|PDB:1LUP"
FT   STRAND          17..20
FT                   /evidence="ECO:0007829|PDB:1LUP"
FT   STRAND          22..24
FT                   /evidence="ECO:0007829|PDB:1LUP"
SQ   SEQUENCE   31 AA;  3929 MW;  AAECBB87A92AAC1B CRC64;
     YCQKWMWTCD EERKCCEGLV CRLWCKRIIN M