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Cytotoxin 2 (Cytotoxin II) (CTII)

 3SA2_NAJOX              Reviewed;          60 AA.
P01441;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
05-JUL-2017, entry version 92.
RecName: Full=Cytotoxin 2;
AltName: Full=Cytotoxin II;
Short=CTII;
Naja oxiana (Central Asian cobra) (Oxus cobra).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
NCBI_TaxID=8657;
[1]
PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
TISSUE=Venom;
PubMed=4435217; DOI=10.1016/0014-5793(74)80462-X;
Grishin E.V., Sukhikh A.P., Adamovich T.B., Ovchinnikov Y.A.,
Yukelson L.Y.;
"The isolation and sequence determination of a cytotoxin from the
venom of the Middle-Asian cobra Naja naja oxiana.";
FEBS Lett. 48:179-183(1974).
[2]
FUNCTION.
PubMed=11357394; DOI=10.1023/A:1011329002584;
Dubinnyi M.A., Dubovskii P.V., Utkin Y.N., Simonova T.N.,
Barsukov L.I., Arseniev A.S.;
"ESR study of the interaction of cytotoxin II with model membranes.";
Bioorg. Khim. 27:102-113(2001).
[3]
FUNCTION, AND INTERACTION WITH PHOSPHOLIPID MEMBRANES.
PubMed=12709064; DOI=10.1046/j.1432-1033.2003.03580.x;
Dubovskii P.V., Lesovoy D.M., Dubinnyi M.A., Utkin Y.N.,
Arseniev A.S.;
"Interaction of the P-type cardiotoxin with phospholipid membranes.";
Eur. J. Biochem. 270:2038-2046(2003).
[4]
FUNCTION, AND APPARTENANCE TO P-TYPE CYTOTOXINS.
PubMed=15584897; DOI=10.1042/BJ20041814;
Dubovskii P.V., Lesovoy D.M., Dubinnyi M.A., Konshina A.G.,
Utkin Y.N., Efremov R.G., Arseniev A.S.;
"Interaction of three-finger toxins with phospholipid membranes:
comparison of S- and P-type cytotoxins.";
Biochem. J. 387:807-815(2005).
[5]
STRUCTURE BY NMR, AND DISULFIDE BONDS.
PubMed=10429199; DOI=10.1046/j.1432-1327.1999.00478.x;
Dementieva D.V., Bocharov E.V., Arseniev A.S.;
"Two forms of cytotoxin II (cardiotoxin) from Naja naja oxiana in
aqueous solution: spatial structures with tightly bound water
molecules.";
Eur. J. Biochem. 263:152-162(1999).
[6]
STRUCTURE BY NMR, AND DISULFIDE BONDS.
PubMed=11114253; DOI=10.1006/jmbi.2000.4283;
Dubovskii P.V., Dementieva D.V., Bocharov E.V., Utkin Y.N.,
Arseniev A.S.;
"Membrane binding motif of the P-type cardiotoxin.";
J. Mol. Biol. 305:137-149(2001).
-!- FUNCTION: This three-finger cytotoxin is a basic protein that
interacts and penetrates into the cell membrane, with the tips of
all the three loops. Cytotoxins which have a Pro-30 (P-type)
interacts with membrane stronger that those which have a 'Ser-28'
(S-type). CTII interacts with membrane stronger than CTI.
{ECO:0000269|PubMed:11357394, ECO:0000269|PubMed:12709064,
ECO:0000269|PubMed:15584897}.
-!- 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|PubMed:4435217}.
Target cell membrane {ECO:0000250|UniProtKB:P60301}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
-!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-
chain subfamily. Type IA cytotoxin sub-subfamily. {ECO:0000305}.
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PIR; A01709; H3NJ2R.
PDB; 1CB9; NMR; -; A=1-60.
PDB; 1CCQ; NMR; -; A=1-60.
PDB; 1FFJ; NMR; -; A=1-60.
PDBsum; 1CB9; -.
PDBsum; 1CCQ; -.
PDBsum; 1FFJ; -.
ProteinModelPortal; P01441; -.
SMR; P01441; -.
HOVERGEN; HBG006553; -.
EvolutionaryTrace; P01441; -.
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 2.
/FTId=PRO_0000093517.
DISULFID 3 21 {ECO:0000269|PubMed:10429199,
ECO:0000269|PubMed:11114253}.
DISULFID 14 38 {ECO:0000269|PubMed:10429199,
ECO:0000269|PubMed:11114253}.
DISULFID 42 53 {ECO:0000269|PubMed:10429199,
ECO:0000269|PubMed:11114253}.
DISULFID 54 59 {ECO:0000269|PubMed:10429199,
ECO:0000269|PubMed:11114253}.
STRAND 2 4 {ECO:0000244|PDB:1CB9}.
STRAND 11 13 {ECO:0000244|PDB:1CB9}.
STRAND 20 26 {ECO:0000244|PDB:1CB9}.
STRAND 33 41 {ECO:0000244|PDB:1CB9}.
STRAND 47 56 {ECO:0000244|PDB:1CB9}.
SEQUENCE 60 AA; 6636 MW; 3512FDB5EED2C5F7 CRC64;
LKCKKLVPLF SKTCPAGKNL CYKMFMVAAP HVPVKRGCID VCPKSSLLVK YVCCNTDKCN


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