ID   MYX_CRODR               Reviewed;          42 AA.
AC   P63327;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2013, sequence version 2.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Crotamine Ile-19 {ECO:0000303|PubMed:24100315, ECO:0000303|Ref.1};
DE            Short=CRO_Ile-19 {ECO:0000303|Ref.1};
OS   Crotalus durissus ruruima (South American rattlesnake) (Mt. Roraima
OS   rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=221570;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RA   Dos Santos M.C., Morhy L., Ferreira L.C.L., Oliveira E.B.;
RT   "Purification and properties of a crotamine analog from Crotalus durissus
RT   ruruima venom.";
RL   Toxicon 31:166-166(1993).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), AND DISULFIDE BOND.
RC   TISSUE=Venom;
RX   PubMed=24100315; DOI=10.1107/s0907444913018003;
RA   Coronado M.A., Gabdulkhakov A., Georgieva D., Sankaran B., Murakami M.T.,
RA   Arni R.K., Betzel C.;
RT   "Structure of the polypeptide crotamine from the Brazilian rattlesnake
RT   Crotalus durissus terrificus.";
RL   Acta Crystallogr. D 69:1958-1964(2013).
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 induces severe muscle necrosis by
CC       a non-enzymatic mechanism and exhibits antimicrobial activities (By
CC       similarity). It also elicits a short-lasting hyperextension of the hind
CC       limb (Ref.1). It does not cause observable tissue damage (whereas the
CC       whole venom causes severe myonecrosis accompanied by edema and
CC       hemorrhage) (Ref.1). {ECO:0000250|UniProtKB:Q9PWF3, ECO:0000269|Ref.1}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|Ref.1}.
CC   -!- SIMILARITY: Belongs to the crotamine-myotoxin family. {ECO:0000305}.
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DR   PDB; 4GV5; X-ray; 1.70 A; A/B/C=1-42.
DR   PDBsum; 4GV5; -.
DR   AlphaFoldDB; P63327; -.
DR   BMRB; P63327; -.
DR   SMR; P63327; -.
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   3D-structure; 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="Crotamine Ile-19"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="PRO_0000221563"
FT   DISULFID        4..36
FT                   /evidence="ECO:0000269|PubMed:24100315,
FT                   ECO:0000312|PDB:4GV5"
FT   DISULFID        11..30
FT                   /evidence="ECO:0000269|PubMed:24100315,
FT                   ECO:0000312|PDB:4GV5"
FT   DISULFID        18..37
FT                   /evidence="ECO:0000269|PubMed:24100315,
FT                   ECO:0000312|PDB:4GV5"
SQ   SEQUENCE   42 AA;  4890 MW;  A268861EE6AE69D0 CRC64;
     YKQCHKKGGH CFPKEKICIP PSSDFGKMDC RWRWKCCKKG SG