MYXC_CROOH
ID MYXC_CROOH Reviewed; 70 AA.
AC P01477; G9DCI6;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 2.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Myotoxin;
DE AltName: Full=Crotamine-4;
DE AltName: Full=Toxic peptide C;
DE Flags: Precursor;
OS Crotalus oreganus helleri (Southern pacific rattlesnake) (Crotalus viridis
OS helleri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=8741;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Sanchez E.;
RT "cDNA clones from the library of Crotalus oreganus helleri (Southern
RT Pacific Rattlesnake) venom gland.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Fry B.G.;
RT "Clinical and biodiscovery implications of intra-specific venom variation
RT in the medically important Southern Pacific Rattlesnake (Crotalus oreganus
RT helleri).";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 23-65, TOXIC DOSE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=694946; DOI=10.1016/0041-0101(78)90140-x;
RA Maeda N., Tamiya N., Pattabhiraman T.R., Russell F.E.;
RT "Some chemical properties of the venom of the rattlesnake, Crotalus viridis
RT helleri.";
RL Toxicon 16:431-441(1978).
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 (By similarity). {ECO:0000250|UniProtKB:Q9PWF3}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:694946}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:694946}.
CC -!- TOXIC DOSE: LD(50) is 1.96 mg/kg by intravenous injection.
CC {ECO:0000269|PubMed:694946}.
CC -!- SIMILARITY: Belongs to the crotamine-myotoxin family. {ECO:0000305}.
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DR EMBL; JF895769; AEU60012.1; -; mRNA.
DR EMBL; GAKQ01000002; JAA97967.1; -; mRNA.
DR EMBL; GAKQ01000001; JAA97968.1; -; mRNA.
DR EMBL; GAKR01000001; JAA97984.1; -; mRNA.
DR EMBL; GAKS01000002; JAA98014.1; -; mRNA.
DR EMBL; GAKS01000001; JAA98015.1; -; mRNA.
DR EMBL; GALC01000001; JAA98041.1; -; mRNA.
DR PIR; A01737; CXRSCH.
DR AlphaFoldDB; P01477; -.
DR SMR; P01477; -.
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; Signal; Toxin;
KW Voltage-gated potassium channel impairing toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:694946"
FT CHAIN 23..70
FT /note="Myotoxin"
FT /evidence="ECO:0000305|PubMed:694946"
FT /id="PRO_0000221569"
FT DISULFID 26..58
FT /evidence="ECO:0000250|UniProtKB:Q9PWF3"
FT DISULFID 33..52
FT /evidence="ECO:0000250|UniProtKB:Q9PWF3"
FT DISULFID 40..59
FT /evidence="ECO:0000250|UniProtKB:Q9PWF3"
SQ SEQUENCE 70 AA; 7989 MW; 06B32AE06B0989F1 CRC64;
MKILYLLFAF LFLAFLSEPG NAYKRCHKKG GHCFPKTVIC LPPSSDFGKM DCRWKWKCCK
KGSVNNAISI