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Cytotoxin 1 (CX1) (Cardiotoxin 1) (CTX-1) (CTX1) (Cardiotoxin A1) (CTX A1) (Cardiotoxin I) (Cardiotoxin analog I) (CTX I)

 3SA1_NAJAT              Reviewed;          81 AA.
P60304; P01449; P01450; Q9PS24; Q9W6W8;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
02-FEB-2004, sequence version 1.
22-NOV-2017, entry version 73.
RecName: Full=Cytotoxin 1;
Short=CX1;
AltName: Full=Cardiotoxin 1;
Short=CTX-1;
Short=CTX1;
AltName: Full=Cardiotoxin A1 {ECO:0000303|PubMed:16407244, ECO:0000303|PubMed:8182052};
Short=CTX A1 {ECO:0000303|PubMed:16407244, ECO:0000303|PubMed:8182052};
AltName: Full=Cardiotoxin I {ECO:0000303|PubMed:8619792};
AltName: Full=Cardiotoxin analog I;
Short=CTX I;
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;
PubMed=8619792; DOI=10.1006/bbrc.1996.0191;
Chang L.-S., Wu P.-F., Lin J.;
"cDNA sequence analysis and expression of cardiotoxins from Taiwan
Cobra.";
Biochem. Biophys. Res. Commun. 219:116-121(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Venom gland;
Chu R.C., Yang C.-C.;
Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
[3]
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).
[4]
PROTEIN SEQUENCE OF 22-81, AND SUBCELLULAR LOCATION.
TISSUE=Venom;
PubMed=1147930; DOI=10.1016/0006-291X(75)90262-4;
Hayashi K., Takechi M., Sasaki T., Lee C.Y.;
"Amino acid sequence of cardiotoxin-analogue I from the venom of Naja
naja atra.";
Biochem. Biophys. Res. Commun. 64:360-366(1975).
[5]
PROTEIN SEQUENCE OF 22-81, AND FUNCTION AS AN INHIBITOR OF PKC.
PubMed=8448165; DOI=10.1021/bi00059a025;
Chiou S.-H., Raynor R.L., Zheng B., Chambers T.C., Kuo J.F.;
"Cobra venom cardiotoxin (cytotoxin) isoforms and neurotoxin:
comparative potency of protein kinase C inhibition and cancer cell
cytotoxicity and modes of enzyme inhibition.";
Biochemistry 32:2062-2067(1993).
[6]
FUNCTION AS MYOTOXIN.
TISSUE=Venom;
PubMed=8342169; DOI=10.1016/0041-0101(93)90376-T;
Ownby C.L., Fletcher J.E., Colberg T.R.;
"Cardiotoxin 1 from cobra (Naja naja atra) venom causes necrosis of
skeletal muscle in vivo.";
Toxicon 31:697-709(1993).
[7]
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).
[8]
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).
[9]
FUNCTION, AND BINDING TO HEPARIN.
PubMed=17685633; DOI=10.1021/bi700995v;
Tjong S.C., Chen T.S., Huang W.N., Wu W.G.;
"Structures of heparin-derived tetrasaccharide bound to cobra
cardiotoxins: heparin binding at a single protein site with diverse
side chain interactions.";
Biochemistry 46:9941-9952(2007).
[10]
STRUCTURE BY NMR OF 22-81, AND DISULFIDE BONDS.
PubMed=8046750; DOI=10.1006/jmbi.1994.1460;
Jahnke W., Mierke D.F., Beress L., Kessler H.;
"Structure of cobra cardiotoxin CTX I as derived from nuclear magnetic
resonance spectroscopy and distance geometry calculations.";
J. Mol. Biol. 240:445-458(1994).
-!- FUNCTION: Basic protein that binds to cell membrane and
depolarizes cardiomyocytes. It also shows lytic activities on many
other cells, including red blood cells. Interaction with
sulfatides in the cell membrane induces pore formation and cell
internalization and is responsible for cytotoxicity in
cardiomyocytes. It targets the mitochondrial membrane and induces
mitochondrial swelling and fragmentation (By similarity). It binds
to the integrin alpha-V/beta-3 (ITGAV/ITGB3) with a moderate
affinity and inhibits protein kinases C (PubMed:8448165). It also
binds with high affinity to heparin (PubMed:17685633). It also
causes skeletal muscle necrosis after intramuscular injection into
mice (PubMed:8342169). {ECO:0000250|UniProtKB:P60301,
ECO:0000269|PubMed:8342169, ECO:0000269|PubMed:8448165}.
-!- 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:1147930}.
Target cell membrane {ECO:0000250|UniProtKB:P60301}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
-!- 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; Z54226; CAA90962.1; -; mRNA.
EMBL; U42583; AAB01539.1; -; mRNA.
EMBL; AJ238736; CAB42056.1; -; Genomic_DNA.
PIR; JC4619; H3NJ1F.
PDB; 2CDX; NMR; -; A=22-81.
PDBsum; 2CDX; -.
ProteinModelPortal; P60304; -.
SMR; P60304; -.
HOVERGEN; HBG006553; -.
EvolutionaryTrace; P60304; -.
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; Myotoxin; Secreted; Signal;
Target cell membrane; Target membrane; Toxin.
SIGNAL 1 21 {ECO:0000269|PubMed:1147930,
ECO:0000269|PubMed:8448165}.
CHAIN 22 81 Cytotoxin 1.
/FTId=PRO_0000035365.
DISULFID 24 42 {ECO:0000269|PubMed:8046750}.
DISULFID 35 59 {ECO:0000269|PubMed:8046750}.
DISULFID 63 74 {ECO:0000269|PubMed:8046750}.
DISULFID 75 80 {ECO:0000269|PubMed:8046750}.
CONFLICT 10 10 V -> L (in Ref. 3; CAB42056).
{ECO:0000305}.
CONFLICT 66 67 NS -> SN (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 78 78 D -> H (in Ref. 1; CAA90962).
{ECO:0000305}.
STRAND 27 30 {ECO:0000244|PDB:2CDX}.
STRAND 41 46 {ECO:0000244|PDB:2CDX}.
STRAND 48 50 {ECO:0000244|PDB:2CDX}.
STRAND 55 62 {ECO:0000244|PDB:2CDX}.
STRAND 71 77 {ECO:0000244|PDB:2CDX}.
SEQUENCE 81 AA; 8992 MW; 19C53E88D2E2596D CRC64;
MKTLLLTLVV VTIVCLDLGY TLKCNKLIPI ASKTCPAGKN LCYKMFMMSD LTIPVKRGCI
DVCPKNSLLV KYVCCNTDRC N


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