MYX_CROAD
ID MYX_CROAD Reviewed; 70 AA.
AC P24330; F8S0Z6; J3RY57;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 2.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Myotoxin;
DE AltName: Full=CAM-toxin;
DE Flags: Precursor;
OS Crotalus adamanteus (Eastern diamondback rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=8729;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=23025625; DOI=10.1186/1471-2164-13-312;
RA Rokyta D.R., Lemmon A.R., Margres M.J., Aronow K.;
RT "The venom-gland transcriptome of the eastern diamondback rattlesnake
RT (Crotalus adamanteus).";
RL BMC Genomics 13:312-312(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-63.
RX PubMed=21255598; DOI=10.1016/j.toxicon.2011.01.008;
RA Rokyta D.R., Wray K.P., Lemmon A.R., Lemmon E.M., Caudle S.B.;
RT "A high-throughput venom-gland transcriptome for the eastern diamondback
RT rattlesnake (Crotalus adamanteus) and evidence for pervasive positive
RT selection across toxin classes.";
RL Toxicon 57:657-671(2011).
RN [3]
RP PROTEIN SEQUENCE OF 23-67, TOXIC DOSE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=1862521; DOI=10.1016/0041-0101(91)90020-r;
RA Samejima Y., Aoki Y., Mebs D.;
RT "Amino acid sequence of a myotoxin from venom of the eastern diamondback
RT rattlesnake (Crotalus adamanteus).";
RL Toxicon 29:461-468(1991).
RN [4]
RP PROTEIN SEQUENCE OF 23-34, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=24231107; DOI=10.1016/j.jprot.2013.11.001;
RA Margres M.J., McGivern J.J., Wray K.P., Seavy M., Calvin K., Rokyta D.R.;
RT "Linking the transcriptome and proteome to characterize the venom of the
RT eastern diamondback rattlesnake (Crotalus adamanteus).";
RL J. Proteomics 96:145-158(2014).
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:1862521}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:1862521}.
CC -!- TOXIC DOSE: LD(50) is 0.96 mg/kg by subcutaneous injection.
CC {ECO:0000269|PubMed:1862521}.
CC -!- MISCELLANEOUS: This myotoxin is the most abundant transcript in the
CC venom of the specimen analyzed in PubMed:23025625.
CC -!- MISCELLANEOUS: Individuals of C.adamanteus from populations in southern
CC and central Florida lack this toxin in their venoms.
CC {ECO:0000305|PubMed:23025625}.
CC -!- SIMILARITY: Belongs to the crotamine-myotoxin family. {ECO:0000305}.
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DR EMBL; HQ414100; AEJ31978.1; -; mRNA.
DR EMBL; JU173668; AFJ49194.1; -; mRNA.
DR PIR; A37909; A37909.
DR AlphaFoldDB; P24330; -.
DR SMR; P24330; -.
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:1862521,
FT ECO:0000269|PubMed:24231107"
FT CHAIN 23..70
FT /note="Myotoxin"
FT /evidence="ECO:0000305|PubMed:1862521"
FT /id="PRO_0000221562"
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"
FT CONFLICT 63
FT /note="S -> V (in Ref. 2; AEJ31978)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 70 AA; 8017 MW; 21432AE06B0989EE CRC64;
MKILYLLFAF LFLAFLSEPG NAYKRCHKKG GHCFPKTVIC LPPSSDFGKM DCRWRWKCCK
KGSVNNAISI
