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Cytotoxin 1 (Cytotoxin I) (CTI)

 3SA1_NAJOX              Reviewed;          60 AA.
P01451;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
27-SEP-2017, entry version 90.
RecName: Full=Cytotoxin 1;
AltName: Full=Cytotoxin I;
Short=CTI;
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;
Grishin E.V., Sukhikh A.P., Adamovich T.B., Ovchinnikov Y.A.;
"Isolation, properties and sequence determination of the two
cytotoxins from the venom of the Middle-Asian cobra Naja Naja
oxiana.";
Bioorg. Khim. 2:1018-1034(1976).
[2]
STRUCTURE BY NMR, AND DISULFIDE BONDS.
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).
-!- 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). CTI interacts with membrane weaker than CTII.
-!- 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}.
-!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-
chain subfamily. Type IA cytotoxin sub-subfamily. {ECO:0000305}.
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PIR; A01716; H3NJ1R.
PDB; 1RL5; NMR; -; A=1-60.
PDB; 1ZAD; NMR; -; A=1-60.
PDBsum; 1RL5; -.
PDBsum; 1ZAD; -.
ProteinModelPortal; P01451; -.
SMR; P01451; -.
HOVERGEN; HBG006553; -.
EvolutionaryTrace; P01451; -.
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:0090729; F:toxin activity; IEA:InterPro.
GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
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_0000093516.
DISULFID 3 21 {ECO:0000269|PubMed:15584897}.
DISULFID 14 38 {ECO:0000269|PubMed:15584897}.
DISULFID 42 53 {ECO:0000269|PubMed:15584897}.
DISULFID 54 59 {ECO:0000269|PubMed:15584897}.
STRAND 2 4 {ECO:0000244|PDB:1RL5}.
STRAND 11 13 {ECO:0000244|PDB:1RL5}.
STRAND 20 29 {ECO:0000244|PDB:1RL5}.
STRAND 34 41 {ECO:0000244|PDB:1RL5}.
STRAND 47 54 {ECO:0000244|PDB:1RL5}.
SEQUENCE 60 AA; 6821 MW; C0E8AE8AC6A86F11 CRC64;
LKCNKLVPIA YKTCPEGKNL CYKMFMMSDL TIPVKRGCID VCPKNSLLVK YVCCNTDRCN


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