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 22-FEB-2023, entry version 81. 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}. 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 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; Anthopleurin-A; 1. DR InterPro; IPR023355; Myo_ane_neurotoxin_sf. DR InterPro; IPR000881; Myotoxin. DR Pfam; PF00819; Myotoxins; 1. DR PRINTS; PR00283; MYOTOXIN. DR SUPFAM; SSF57392; Defensin-like; 1. 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 //