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 03-MAY-2023, entry version 109. 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:0044218; C:other organism cell membrane; IEA:UniProtKB-KW. DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW. DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW. DR CDD; cd00206; snake_toxin; 1. DR Gene3D; 2.10.60.10; CD59; 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; Snake toxin-like; 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 //