3SA2_NAJOX
ID 3SA2_NAJOX Reviewed; 60 AA.
AC P01441;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Cytotoxin 2;
DE AltName: Full=Cytotoxin II;
DE Short=CTII;
OS Naja oxiana (Central Asian cobra) (Oxus cobra).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=8657;
RN [1]
RP PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=4435217; DOI=10.1016/0014-5793(74)80462-x;
RA Grishin E.V., Sukhikh A.P., Adamovich T.B., Ovchinnikov Y.A.,
RA Yukelson L.Y.;
RT "The isolation and sequence determination of a cytotoxin from the venom of
RT the Middle-Asian cobra Naja naja oxiana.";
RL FEBS Lett. 48:179-183(1974).
RN [2]
RP FUNCTION.
RX PubMed=11357394; DOI=10.1023/a:1011329002584;
RA Dubinnyi M.A., Dubovskii P.V., Utkin Y.N., Simonova T.N., Barsukov L.I.,
RA Arseniev A.S.;
RT "ESR study of the interaction of cytotoxin II with model membranes.";
RL Bioorg. Khim. 27:102-113(2001).
RN [3]
RP FUNCTION, AND INTERACTION WITH PHOSPHOLIPID MEMBRANES.
RX PubMed=12709064; DOI=10.1046/j.1432-1033.2003.03580.x;
RA Dubovskii P.V., Lesovoy D.M., Dubinnyi M.A., Utkin Y.N., Arseniev A.S.;
RT "Interaction of the P-type cardiotoxin with phospholipid membranes.";
RL Eur. J. Biochem. 270:2038-2046(2003).
RN [4]
RP FUNCTION, AND APPARTENANCE TO P-TYPE CYTOTOXINS.
RX PubMed=15584897; DOI=10.1042/bj20041814;
RA Dubovskii P.V., Lesovoy D.M., Dubinnyi M.A., Konshina A.G., Utkin Y.N.,
RA Efremov R.G., Arseniev A.S.;
RT "Interaction of three-finger toxins with phospholipid membranes: comparison
RT of S- and P-type cytotoxins.";
RL Biochem. J. 387:807-815(2005).
RN [5]
RP STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX PubMed=10429199; DOI=10.1046/j.1432-1327.1999.00478.x;
RA Dementieva D.V., Bocharov E.V., Arseniev A.S.;
RT "Two forms of cytotoxin II (cardiotoxin) from Naja naja oxiana in aqueous
RT solution: spatial structures with tightly bound water molecules.";
RL Eur. J. Biochem. 263:152-162(1999).
RN [6]
RP STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX PubMed=11114253; DOI=10.1006/jmbi.2000.4283;
RA Dubovskii P.V., Dementieva D.V., Bocharov E.V., Utkin Y.N., Arseniev A.S.;
RT "Membrane binding motif of the P-type cardiotoxin.";
RL J. Mol. Biol. 305:137-149(2001).
CC -!- FUNCTION: This three-finger cytotoxin is a basic protein that interacts
CC and penetrates into the cell membrane, with the tips of all the three
CC loops. Cytotoxins which have a Pro-30 (P-type) interacts with membrane
CC stronger that those which have a 'Ser-28' (S-type). CTII interacts with
CC membrane stronger than CTI. {ECO:0000269|PubMed:11357394,
CC ECO:0000269|PubMed:12709064, ECO:0000269|PubMed:15584897}.
CC -!- SUBUNIT: Monomer in solution; Homodimer and oligomer in the presence of
CC negatively charged lipids forming a pore with a size ranging between 20
CC and 30 Angstroms. {ECO:0000250|UniProtKB:P60301}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:4435217}. Target
CC cell membrane {ECO:0000250|UniProtKB:P60301}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- MISCELLANEOUS: Is classified as a P-type cytotoxin, since a proline
CC residue stands at position 30 (Pro-31 in standard classification).
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain
CC subfamily. Type IA cytotoxin sub-subfamily. {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 PIR; A01709; H3NJ2R.
DR PDB; 1CB9; NMR; -; A=1-60.
DR PDB; 1CCQ; NMR; -; A=1-60.
DR PDB; 1FFJ; NMR; -; A=1-60.
DR PDBsum; 1CB9; -.
DR PDBsum; 1CCQ; -.
DR PDBsum; 1FFJ; -.
DR AlphaFoldDB; P01441; -.
DR BMRB; P01441; -.
DR SMR; P01441; -.
DR EvolutionaryTrace; P01441; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR CDD; cd00206; snake_toxin; 1.
DR Gene3D; 2.10.60.10; -; 1.
DR InterPro; IPR003572; Cytotoxin_Cobra.
DR InterPro; IPR003571; Snake_3FTx.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR InterPro; IPR018354; Snake_toxin_con_site.
DR PRINTS; PR00282; CYTOTOXIN.
DR SUPFAM; SSF57302; SSF57302; 1.
DR PROSITE; PS00272; SNAKE_TOXIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cardiotoxin; Cytolysis; Direct protein sequencing;
KW Disulfide bond; Membrane; Secreted; Target cell membrane; Target membrane;
KW Toxin.
FT CHAIN 1..60
FT /note="Cytotoxin 2"
FT /evidence="ECO:0000269|PubMed:4435217"
FT /id="PRO_0000093517"
FT DISULFID 3..21
FT /evidence="ECO:0000269|PubMed:10429199,
FT ECO:0000269|PubMed:11114253, ECO:0000312|PDB:1CB9,
FT ECO:0000312|PDB:1CCQ, ECO:0000312|PDB:1FFJ"
FT DISULFID 14..38
FT /evidence="ECO:0000269|PubMed:10429199,
FT ECO:0000269|PubMed:11114253, ECO:0000312|PDB:1CB9,
FT ECO:0000312|PDB:1CCQ, ECO:0000312|PDB:1FFJ"
FT DISULFID 42..53
FT /evidence="ECO:0000269|PubMed:10429199,
FT ECO:0000269|PubMed:11114253, ECO:0000312|PDB:1CB9,
FT ECO:0000312|PDB:1CCQ, ECO:0000312|PDB:1FFJ"
FT DISULFID 54..59
FT /evidence="ECO:0000269|PubMed:10429199,
FT ECO:0000269|PubMed:11114253, ECO:0000312|PDB:1CB9,
FT ECO:0000312|PDB:1CCQ, ECO:0000312|PDB:1FFJ"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:1CB9"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:1CB9"
FT STRAND 20..26
FT /evidence="ECO:0007829|PDB:1CB9"
FT STRAND 33..41
FT /evidence="ECO:0007829|PDB:1CB9"
FT STRAND 47..56
FT /evidence="ECO:0007829|PDB:1CB9"
SQ SEQUENCE 60 AA; 6636 MW; 3512FDB5EED2C5F7 CRC64;
LKCKKLVPLF SKTCPAGKNL CYKMFMVAAP HVPVKRGCID VCPKSSLLVK YVCCNTDKCN
