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Cytotoxin 1 (CTX M1) (Cardiotoxin IIB) (CTX-IIB) (Cytotoxin V(II)1)

 3SA1_NAJMO              Reviewed;          60 AA.
P01467;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
05-JUL-2017, entry version 96.
RecName: Full=Cytotoxin 1;
AltName: Full=CTX M1 {ECO:0000303|PubMed:8182052};
AltName: Full=Cardiotoxin IIB;
Short=CTX-IIB;
AltName: Full=Cytotoxin V(II)1;
Naja mossambica (Mozambique spitting cobra).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
NCBI_TaxID=8644;
[1]
PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
TISSUE=Venom;
DOI=10.1016/0005-2795(74)90429-2;
Louw A.I.;
"Snake venom toxins. The amino acid sequences of three cytotoxin
homologues from Naja mossambica mossambica venom.";
Biochim. Biophys. Acta 336:481-495(1974).
[2]
FUNCTION, AND APPARTENANCE TO P-TYPE CYTOTOXIN GROUP.
PubMed=8182052;
Chien K.-Y., Chiang C.-M., Hseu Y.-C., Vyas A.A., Rule G.S., Wu W.-G.;
"Two distinct types of cardiotoxin as revealed by the structure and
activity relationship of their interaction with zwitterionic
phospholipid dispersions.";
J. Biol. Chem. 269:14473-14483(1994).
[3]
STRUCTURE BY NMR, AND DISULFIDE BONDS.
PubMed=2822421; DOI=10.1111/j.1432-1033.1987.tb13460.x;
Otting G., Steinmetz W.E., Bougis P.E., Rochat H., Wuethrich K.;
"Sequence-specific 1H-NMR assignments and determination of the
secondary structure in aqueous solution of the cardiotoxins CTXIIa and
CTXIIb from Naja mossambica mossambica.";
Eur. J. Biochem. 168:609-620(1987).
[4]
STRUCTURE BY NMR, AND DISULFIDE BONDS.
PubMed=8504828; DOI=10.1111/j.1432-1033.1993.tb17833.x;
O'Connell J.F., Bougis P.E., Wuethrich K.;
"Determination of the nuclear-magnetic-resonance solution structure of
cardiotoxin CTX IIb from Naja mossambica mossambica.";
Eur. J. Biochem. 213:891-900(1993).
-!- FUNCTION: Shows cytolytic activity on many different cells by
forming pore in lipid membranes. In vivo, increases heart rate or
kills the animal by cardiac arrest. In addition, it binds to
heparin with high affinity, interacts with Kv channel-interacting
protein 1 (KCNIP1) in a calcium-independent manner, and binds to
integrin alpha-V/beta-3 (ITGAV/ITGB3) with moderate affinity.
{ECO:0000250|UniProtKB:P60301, ECO:0000250|UniProtKB:P60304,
ECO:0000269|PubMed:8182052}.
-!- SUBUNIT: Monomer in solution; Homodimer and oligomer in the
presence of negatively charged lipids forming a pore with a size
ranging between 20 and 30 Angstroms.
{ECO:0000250|UniProtKB:P60301}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}. Target cell
membrane {ECO:0000250|UniProtKB:P60301}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
-!- TOXIC DOSE: LD(50) is 0.83 mg/kg by intravenous injection.
-!- MISCELLANEOUS: Is classified as a P-type cytotoxin, since a
proline residue stands at position 30 (Pro-31 in standard
classification). {ECO:0000305|PubMed:8182052}.
-!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-
chain subfamily. Type IA cytotoxin sub-subfamily. {ECO:0000305}.
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PIR; A38050; H3NJ1M.
PDB; 2CCX; NMR; -; A=1-60.
PDBsum; 2CCX; -.
ProteinModelPortal; P01467; -.
SMR; P01467; -.
HOVERGEN; HBG006553; -.
EvolutionaryTrace; P01467; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0044218; C:other organism cell membrane; IEA:UniProtKB-SubCell.
GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
GO; GO:0009405; P:pathogenesis; IEA:InterPro.
CDD; cd00206; snake_toxin; 1.
InterPro; IPR003572; Cytotoxin.
InterPro; IPR003571; Snake_3FTx.
InterPro; IPR018354; Snake_toxin_con_site.
InterPro; IPR035076; Toxin/TOLIP.
Pfam; PF00087; Toxin_TOLIP; 1.
PRINTS; PR00282; CYTOTOXIN.
PROSITE; PS00272; SNAKE_TOXIN; 1.
1: Evidence at protein level;
3D-structure; Cardiotoxin; Cytolysis; Direct protein sequencing;
Disulfide bond; Membrane; Secreted; Target cell membrane;
Target membrane; Toxin.
CHAIN 1 60 Cytotoxin 1.
/FTId=PRO_0000093505.
DISULFID 3 21
DISULFID 14 38
DISULFID 42 53
DISULFID 54 59
STRAND 6 8 {ECO:0000244|PDB:2CCX}.
STRAND 21 28 {ECO:0000244|PDB:2CCX}.
STRAND 35 37 {ECO:0000244|PDB:2CCX}.
STRAND 47 54 {ECO:0000244|PDB:2CCX}.
SEQUENCE 60 AA; 6826 MW; 68BE50B776B6491C CRC64;
LKCNQLIPPF WKTCPKGKNL CYKMTMRAAP MVPVKRGCID VCPKSSLLIK YMCCNTNKCN


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