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MYX1_CROVV
ID   MYX1_CROVV              Reviewed;          42 AA.
AC   P01476;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Myotoxin-A;
DE   AltName: Full=Myotoxin-1;
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, DISULFIDE BONDS, AND SUBCELLULAR LOCATION.
RX   PubMed=570412; DOI=10.1021/bi00571a020;
RA   Fox J.W., Elzinga M., Tu A.T.;
RT   "Amino acid sequence and disulfide bond assignment of myotoxin a isolated
RT   from the venom of Prairie rattlesnake (Crotalus viridis viridis).";
RL   Biochemistry 18:678-684(1979).
RN   [2]
RP   PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
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).
RN   [3]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   PubMed=2048143; DOI=10.1016/0041-0101(91)90111-4;
RA   Aird S.D., Kruggel W.G., Kaiser I.I.;
RT   "Multiple myotoxin sequences from the venom of a single prairie rattlesnake
RT   (Crotalus viridis viridis).";
RL   Toxicon 29:265-268(1991).
RN   [4]
RP   FUNCTION, AND SYNTHESIS.
RX   PubMed=1329655; DOI=10.1016/0003-9861(92)90418-v;
RA   Baker B., Utaisincharoen P., Tu A.T.;
RT   "Structure-function relationship of myotoxin a using peptide fragments.";
RL   Arch. Biochem. Biophys. 298:325-331(1992).
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). It also binds to sarcoplasmic reticulum
CC       calcium-ATPase (PubMed:1329655). {ECO:0000250|UniProtKB:Q9PWF3,
CC       ECO:0000269|PubMed:1329655}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:570412}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:570412}.
CC   -!- MASS SPECTROMETRY: Mass=4824.0; Mass_error=1.45; Method=FAB;
CC       Evidence={ECO:0000269|PubMed:2253781};
CC   -!- TOXIC DOSE: LD(50) is 3.0 mg/kg by intramuscular injection.
CC   -!- SIMILARITY: Belongs to the crotamine-myotoxin family. {ECO:0000305}.
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DR   PIR; A01736; MXRSMV.
DR   PIR; C39560; C39560.
DR   AlphaFoldDB; P01476; -.
DR   SMR; P01476; -.
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..42
FT                   /note="Myotoxin-A"
FT                   /evidence="ECO:0000269|PubMed:570412"
FT                   /id="PRO_0000221566"
FT   DISULFID        4..36
FT                   /evidence="ECO:0000269|PubMed:570412"
FT   DISULFID        11..30
FT                   /evidence="ECO:0000269|PubMed:570412"
FT   DISULFID        18..37
FT                   /evidence="ECO:0000269|PubMed:570412"
FT   VARIANT         19
FT                   /note="I -> T (in fraction 5 and in 10% of fraction 2)"
FT   VARIANT         25
FT                   /note="L -> F (in fraction 5 and in 10% of fraction 2)"
FT   VARIANT         25
FT                   /note="L -> K (in 90% of fraction 2, 20% of fraction 3 and
FT                   78% of fraction 4)"
FT   VARIANT         33
FT                   /note="K -> R (in fraction 5)"
SQ   SEQUENCE   42 AA;  4828 MW;  A27AD67EE6AE69D0 CRC64;
     YKQCHKKGGH CFPKEKICIP PSSDLGKMDC RWKWKCCKKG SG
 
 
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