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Cytotoxin A5 (CTX A5) (CT A5) (Cardiotoxin A5) (Cardiotoxin V) (CTX V) (CTXV) (Cardiotoxin-like basic polypeptide) (CLBP)

 3SOF5_NAJAT             Reviewed;          83 AA.
P62375; P14554;
05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
22-NOV-2017, entry version 66.
RecName: Full=Cytotoxin A5 {ECO:0000305};
AltName: Full=CTX A5 {ECO:0000303|PubMed:8182052};
Short=CT A5 {ECO:0000303|PubMed:14743531};
AltName: Full=Cardiotoxin A5 {ECO:0000303|PubMed:14743531, ECO:0000303|PubMed:8182052};
AltName: Full=Cardiotoxin V {ECO:0000303|PubMed:8347605};
Short=CTX V;
Short=CTXV;
AltName: Full=Cardiotoxin-like basic polypeptide {ECO:0000303|PubMed:4091854};
Short=CLBP {ECO:0000303|PubMed:4091854};
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=8679666;
Chang L.-S., Lin J., Wu P.F.;
"cDNA sequence analysis and expression of cardiotoxin V and a new
cardiotoxin VII from Naja naja atra (Taiwan cobra).";
Biochim. Biophys. Acta 1295:1-4(1996).
[2]
PRELIMINARY PROTEIN SEQUENCE OF 22-83, AND SUBCELLULAR LOCATION.
TISSUE=Venom;
PubMed=4091854;
Takechi M., Tanaka Y., Hayashi K.;
"Amino acid sequence of a cardiotoxin-like basic polypeptide (CLBP)
with low cytotoxic activity isolated from the venom of the Formosan
cobra (Naja naja atra).";
Biochem. Int. 11:795-802(1985).
[3]
FUNCTION, AND P-TYPE CYTOTOXIN GROUP MISASSIGNATION.
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).
[4]
FUNCTION, AND INACTIVATION BY ACIDIC PH.
PubMed=8703922; DOI=10.1021/bi952823k;
Chiang C.-M., Chien K.-Y., Lin H.-J., Lin J.-F., Yeh H.-C., Ho P.-L.,
Wu W.-G.;
"Conformational change and inactivation of membrane phospholipid-
related activity of cardiotoxin V from Taiwan cobra venom at acidic
pH.";
Biochemistry 35:9167-9176(1996).
[5]
ROLE OF ACIDIC AMINO ACID RESIDUES.
PubMed=8703923; DOI=10.1021/bi960077t;
Chiang C.-M., Chang S.-L., Lin H.-J., Wu W.-G.;
"The role of acidic amino acid residues in the structural stability of
snake cardiotoxins.";
Biochemistry 35:9177-9186(1996).
[6]
FUNCTION.
PubMed=14743531; DOI=10.1023/B:RUBI.0000008892.75272.ab;
Konshina A.G., Volynskii P.E., Arsen'ev A.S., Efremov R.G.;
"Interaction of cardiotoxin A5 with a membrane: role of conformational
heterogeneity and hydrophilic properties.";
Bioorg. Khim. 29:577-588(2003).
[7]
FUNCTION, AND 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).
[8]
STRUCTURE BY NMR OF 22-83, AND DISULFIDE BONDS.
PubMed=8347605; DOI=10.1021/bi00082a026;
Singhal A.K., Chien K.-Y., Wu W.-G., Rule G.S.;
"Solution structure of cardiotoxin V from Naja naja atra.";
Biochemistry 32:8036-8044(1993).
[9]
X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 22-83, AND DISULFIDE BONDS.
TISSUE=Venom;
PubMed=9054545; DOI=10.1021/bi962594h;
Sun Y.-J., Wu W.-G., Chiang C.-M., Hsin A.-Y., Hsiao C.-D.;
"Crystal structure of cardiotoxin V from Taiwan cobra venom: pH-
dependent conformational change and a novel membrane-binding motif
identified in the three-finger loops of P-type cardiotoxin.";
Biochemistry 36:2403-2413(1997).
-!- FUNCTION: Non-cytotoxic protein that does not show lytic and
hemolytic activities, but can induce aggregation and fusion of
sphingomyelin vesicles (PubMed:8182052). It binds to integrin
alpha-V/beta-3 (ITGAV/ITGB3) with high affinity, and it inhibits
osteoclast differentiation and bone resorption in mice, probably
due to binding to integrin alpha-V/beta-3 (PubMed:16407244).
{ECO:0000269|PubMed:14743531, ECO:0000269|PubMed:16407244,
ECO:0000269|PubMed:8182052, ECO:0000269|PubMed:8703922}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:4091854}.
Target cell membrane {ECO:0000269|PubMed:8703922}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
-!- MISCELLANEOUS: Has been classified as a P-type cytotoxin, which
may be incorrect since P-type cytotoxins are members of the type
IA cytotoxin sub-subfamily and not orphan group XV.
{ECO:0000305|PubMed:8182052}.
-!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-
chain subfamily. Orphan group XV sub-subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Z54228; CAA90964.1; -; mRNA.
PDB; 1CVO; NMR; -; A=22-83.
PDB; 1KXI; X-ray; 2.19 A; A/B=22-83.
PDBsum; 1CVO; -.
PDBsum; 1KXI; -.
ProteinModelPortal; P62375; -.
SMR; P62375; -.
HOVERGEN; HBG006553; -.
EvolutionaryTrace; P62375; -.
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.
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; Direct protein sequencing; Disulfide bond; Membrane;
Secreted; Signal; Target cell membrane; Target membrane; Toxin.
SIGNAL 1 21
CHAIN 22 83 Cytotoxin A5.
/FTId=PRO_0000035404.
DISULFID 24 43
DISULFID 36 61
DISULFID 65 76
DISULFID 77 82
STRAND 23 25 {ECO:0000244|PDB:1KXI}.
STRAND 27 31 {ECO:0000244|PDB:1KXI}.
STRAND 33 35 {ECO:0000244|PDB:1KXI}.
STRAND 42 51 {ECO:0000244|PDB:1KXI}.
STRAND 57 64 {ECO:0000244|PDB:1KXI}.
STRAND 70 77 {ECO:0000244|PDB:1KXI}.
SEQUENCE 83 AA; 9323 MW; 5FA396A4808D5099 CRC64;
MKTLLLTMVV VTIVCLDLGY TLKCHNTQLP FIYKTCPEGK NLCFKATLKK FPLKFPVKRG
CADNCPKNSA LLKYVCCSTD KCN


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