ID   AF2_GRARO               Reviewed;          31 AA.
AC   P61409;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 1.
DT   19-JAN-2010, entry version 23.
DE   RecName: Full=Kappa-theraphotoxin-Gr2c;
DE            Short=Kappa-TRTX-Gr2c;
DE   AltName: Full=Mechanotoxin-alpha;
DE   AltName: Full=Peptide GsAF II;
OS   Grammostola rosea (Chilean rose tarantula) (Grammostola spatulata).
OC   Eukaryota; Metazoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Theraphosidae; Grammostola.
OX   NCBI_TaxID=432528;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RA   Lampe R.A.;
RT   "Analgesic peptides from venom of Grammostola spatulata and use
RT   thereof.";
RL   Patent number US5877026, 02-MAR-1999.
RN   [2]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RA   Lampe R.A.;
RT   "Antiarrhythmic peptide from venom of spider Grammostola spatulata.";
RL   Patent number US5968838, 19-OCT-1999.
CC   -!- FUNCTION: Binds the voltage-sensor domain of the potassium channel
CC       KvAP (from the archaeon Aeropyrum pernix) and affects channel
CC       gating (By similarity). Blocks mechanosensitive ion channels and
CC       the hypotonic cell swelling induced calcium increase associated
CC       with the activation of such channels. It can thus be useful in
CC       treating cardiac ventricular disturbances. Also induces analgesia
CC       in mammals. This analgesia is probably mediated by a non-opioid
CC       receptor related mechanism.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin (By similarity).
CC   -!- MASS SPECTROMETRY: Mass=3979.9; Method=Electrospray; Range=1-31;
CC       Source=Ref.1, Ref.2;
CC   -!- SIMILARITY: Belongs to the phrixotoxin family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   SMR; P61409; 1-30.
DR   ArachnoServer; AS000027; kappa-theraphotoxin-Gr2c.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019870; F:potassium channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR011696; Toxin_12.
DR   Pfam; PF07740; Toxin_12; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Knottin; Secreted; Toxin.
FT   PEPTIDE       1     31       Kappa-theraphotoxin-Gr2c.
FT                                /FTId=PRO_0000045016.
FT   DISULFID      2     16       By similarity.
FT   DISULFID      9     21       By similarity.
FT   DISULFID     15     25       By similarity.
SQ   SEQUENCE   31 AA;  3986 MW;  BF03EB84DE1AAC1B CRC64;
     YCQKWMWTCD EERKCCEGLV CRLWCKKKIE W
//