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Cytotoxin 2 (Cardiotoxin 1A) (Cardiotoxin 2) (CTX-2) (Cardiotoxin A2) (CTX A2) (Cardiotoxin II) (Cardiotoxin analog II)

 3SA2_NAJAT              Reviewed;          81 AA.
P01442;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
22-NOV-2017, entry version 104.
RecName: Full=Cytotoxin 2;
AltName: Full=Cardiotoxin 1A;
AltName: Full=Cardiotoxin 2;
Short=CTX-2 {ECO:0000303|PubMed:10708798};
AltName: Full=Cardiotoxin A2 {ECO:0000303|PubMed:16407244, ECO:0000303|PubMed:8182052};
Short=CTX A2 {ECO:0000303|PubMed:16407244, ECO:0000303|PubMed:8182052};
AltName: Full=Cardiotoxin II {ECO:0000303|PubMed:8089116, ECO:0000303|PubMed:9425035};
AltName: Full=Cardiotoxin analog II {ECO:0000303|PubMed:849468};
Flags: Precursor;
Naja atra (Chinese cobra).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
NCBI_TaxID=8656;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Venom gland;
Chu R.C., Yang C.-C.;
Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Liver;
PubMed=10708798; DOI=10.1016/S0041-0101(99)00218-4;
Chang L.-S., Huang H.-B., Lin S.-R.;
"The multiplicity of cardiotoxins from Naja naja atra (Taiwan cobra)
venom.";
Toxicon 38:1065-1076(2000).
[3]
PROTEIN SEQUENCE OF 22-81, LETHAL DOSE, AND SUBCELLULAR LOCATION.
TISSUE=Venom;
PubMed=849468; DOI=10.1016/0005-2795(77)90040-X;
Kaneda N., Sasaki T., Hayashi K.;
"Primary structures of cardiotoxin analogues II and IV from the venom
of Naja naja atra.";
Biochim. Biophys. Acta 491:53-66(1977).
[4]
FUNCTION, AND APPARTENANCE TO S-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).
[5]
BINDING TO INTEGRIN ALPHA-V/BETA-3.
PubMed=16407244; DOI=10.1074/jbc.M513035200;
Wu P.-L., Lee S.-C., Chuang C.-C., Mori S., Akakura N., Wu W.-G.,
Takada Y.;
"Non-cytotoxic cobra cardiotoxin A5 binds to alpha(v)beta3 integrin
and inhibits bone resorption. Identification of cardiotoxins as non-
RGD integrin-binding proteins of the Ly-6 family.";
J. Biol. Chem. 281:7937-7945(2006).
[6]
STRUCTURE BY NMR, AND DISULFIDE BONDS.
PubMed=8089116;
Bhaskaran R., Huang C.C., Tsai Y.C., Chang K.D., Yu C.;
"Cardiotoxin II from Taiwan cobra venom, Naja naja atra. Structure in
solution and comparison among homologous cardiotoxins.";
J. Biol. Chem. 269:23500-23508(1994).
[7]
STRUCTURE BY NMR, FUNCTION, AND DISULFIDE BONDS.
PubMed=9398182; DOI=10.1021/bi971107a;
Jang J.-Y., Kumar T.K.S., Jayaraman G., Yang P.-W., Yu C.;
"Comparison of the hemolytic activity and solution structures of two
snake venom cardiotoxin analogues which only differ in their N-
terminal amino acid.";
Biochemistry 36:14635-14641(1997).
[8]
STRUCTURE BY NMR, AND DISULFIDE BONDS.
PubMed=9425035; DOI=10.1021/bi971979c;
Lee C.-S., Kumar T.K.S., Lian L.-Y., Cheng J.-W., Yu C.;
"Main-chain dynamics of cardiotoxin II from Taiwan cobra (Naja naja
atra) as studied by carbon-13 NMR at natural abundance: delineation of
the role of functionally important residues.";
Biochemistry 37:155-164(1998).
-!- FUNCTION: Basic protein that binds to cell membrane and
depolarizes cardiomyocytes. It also shows lytic activities, but 2-
fold less important than that of CTX-A4. It binds to the integrin
alpha-V/beta-3 (ITGAV/ITGB3) with a moderate affinity. It may
interact with sulfatides in the cell membrane which induces pore
formation and cell internalization and is responsible for
cytotoxicity in cardiomyocytes. It also may target the
mitochondrial membrane and induce mitochondrial swelling and
fragmentation. {ECO:0000269|PubMed:9398182}.
-!- 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:0000303|PubMed:849468}. Target
cell membrane {ECO:0000250|UniProtKB:P60301}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
-!- TOXIC DOSE: LD(50) is 2.1 mg/kg by intravenous injection into
mice. LD(50) is 56 mg/kg by subcutaneous injection into mice.
{ECO:0000269|PubMed:849468}.
-!- MISCELLANEOUS: Is classified as a S-type cytotoxin, since a serine
residue stands at position 49 (Ser-29 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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EMBL; U58485; AAB18381.1; -; mRNA.
EMBL; U58481; AAB18377.1; -; mRNA.
EMBL; AJ238734; CAB42054.1; -; Genomic_DNA.
PIR; A01710; H3NJ2F.
PDB; 1CRE; NMR; -; A=22-81.
PDB; 1CRF; NMR; -; A=22-81.
PDB; 4OM4; X-ray; 2.74 A; A/B/C/D/E=22-81.
PDBsum; 1CRE; -.
PDBsum; 1CRF; -.
PDBsum; 4OM4; -.
ProteinModelPortal; P01442; -.
SMR; P01442; -.
HOVERGEN; HBG006553; -.
EvolutionaryTrace; P01442; -.
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:UniProtKB-KW.
GO; GO:0044179; P:hemolysis in other organism; 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; Hemolysis; Membrane; Secreted; Signal;
Target cell membrane; Target membrane; Toxin.
SIGNAL 1 21 {ECO:0000269|PubMed:849468}.
CHAIN 22 81 Cytotoxin 2.
/FTId=PRO_0000035371.
DISULFID 24 42
DISULFID 35 59
DISULFID 63 74
DISULFID 75 80
STRAND 23 25 {ECO:0000244|PDB:4OM4}.
TURN 27 30 {ECO:0000244|PDB:1CRE}.
STRAND 32 34 {ECO:0000244|PDB:4OM4}.
STRAND 41 47 {ECO:0000244|PDB:4OM4}.
STRAND 49 52 {ECO:0000244|PDB:1CRE}.
STRAND 55 62 {ECO:0000244|PDB:4OM4}.
STRAND 68 75 {ECO:0000244|PDB:4OM4}.
STRAND 77 79 {ECO:0000244|PDB:1CRE}.
SEQUENCE 81 AA; 9041 MW; 182274E2FAD949BA CRC64;
MKTLLLTLVV VTIVCLDLGY TLKCNKLVPL FYKTCPAGKN LCYKMFMVSN LTVPVKRGCI
DVCPKNSALV KYVCCNTDRC N


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