MYX2_CROVV
ID MYX2_CROVV Reviewed; 45 AA.
AC P63175; P19861;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 1.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=Myotoxin-2;
DE Contains:
DE RecName: Full=Myotoxin-4;
OS Crotalus viridis viridis (Prairie rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=8742;
RN [1]
RP PROTEIN SEQUENCE, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=2253781; DOI=10.1016/0014-5793(90)81325-i;
RA Griffin P.R., Aird S.D.;
RT "A new small myotoxin from the venom of the prairie rattlesnake (Crotalus
RT viridis viridis).";
RL FEBS Lett. 274:43-47(1990).
CC -!- FUNCTION: Cationic peptide that possesses multiple functions. It acts
CC as a cell-penetrating peptide (CPP), and as a potent voltage-gated
CC potassium channel (Kv) inhibitor. It exhibits antimicrobial activities,
CC hind limb paralysis, and severe muscle necrosis by a non-enzymatic
CC mechanism. {ECO:0000250|UniProtKB:Q9PWF3}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2253781}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:2253781}.
CC -!- MASS SPECTROMETRY: [Myotoxin-2]: Mass=5240; Mass_error=1.57;
CC Method=FAB; Evidence={ECO:0000269|PubMed:2253781};
CC -!- MASS SPECTROMETRY: [Myotoxin-4]: Mass=5055.4; Mass_error=1.52;
CC Method=FAB; Evidence={ECO:0000269|PubMed:2253781};
CC -!- SIMILARITY: Belongs to the crotamine-myotoxin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; S12909; S12909.
DR AlphaFoldDB; P63175; -.
DR SMR; P63175; -.
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.
DR GO; GO:0044564; P:envenomation resulting in occlusion of the pore of voltage-gated potassium channel in another organism; ISS:UniProtKB.
DR Gene3D; 2.20.20.10; -; 1.
DR InterPro; IPR023355; Myo_ane_neurotoxin_sf.
DR InterPro; IPR000881; Myotoxin.
DR Pfam; PF00819; Myotoxins; 1.
DR PRINTS; PR00283; MYOTOXIN.
DR PROSITE; PS00459; MYOTOXINS_1; 1.
DR PROSITE; PS51345; MYOTOXINS_2; 1.
PE 1: Evidence at protein level;
KW Antimicrobial; Direct protein sequencing; Disulfide bond;
KW Ion channel impairing toxin; Myotoxin; Neurotoxin;
KW Potassium channel impairing toxin; Secreted; Toxin;
KW Voltage-gated potassium channel impairing toxin.
FT CHAIN 1..45
FT /note="Myotoxin-2"
FT /evidence="ECO:0000269|PubMed:2253781"
FT /id="PRO_0000035177"
FT CHAIN 1..43
FT /note="Myotoxin-4"
FT /evidence="ECO:0000269|PubMed:2253781"
FT /id="PRO_0000035178"
FT DISULFID 4..36
FT /evidence="ECO:0000250|UniProtKB:Q9PWF3"
FT DISULFID 11..30
FT /evidence="ECO:0000250|UniProtKB:Q9PWF3"
FT DISULFID 18..37
FT /evidence="ECO:0000250|UniProtKB:Q9PWF3"
SQ SEQUENCE 45 AA; 5246 MW; D012DD3B5D9B890F CRC64;
YKRCHKKEGH CFPKTVICLP PSSDFGKMDC RWKWKCCKKG SVNNA