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Cytotoxin 5 (CTX M5) (CTX V)

 3SA5_NAJMO              Reviewed;          60 AA.
P25517;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
25-NOV-2002, sequence version 3.
05-JUL-2017, entry version 76.
RecName: Full=Cytotoxin 5;
AltName: Full=CTX M5 {ECO:0000303|PubMed:8182052};
AltName: Full=CTX V;
Naja mossambica (Mozambique spitting cobra).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
NCBI_TaxID=8644;
[1]
PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND LETHAL DOSE.
TISSUE=Venom;
PubMed=6353198; DOI=10.1007/BF00229242;
Bougis P.E., Tessier M., van Rietschoten J., Rochat H., Faucon J.F.,
Dufourcq J.;
"Are interactions with phospholipids responsible for pharmacological
activities of cardiotoxins?";
Mol. Cell. Biochem. 55:49-64(1983).
[2]
FUNCTION, AND APPARTENANCE TO P-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).
-!- FUNCTION: Shows cytolytic activity on many different cells by
forming pore in lipid membranes (PubMed:8182052). In vivo,
increases heart rate or kills the animal by cardiac arrest. In
addition, it binds to heparin with high affinity, interacts with
Kv channel-interacting protein 1 (KCNIP1) in a calcium-independent
manner, and binds to integrin alpha-V/beta-3 (ITGAV/ITGB3) with
moderate affinity. {ECO:0000250|UniProtKB:P60301,
ECO:0000250|UniProtKB:P60304, ECO:0000269|PubMed:8182052}.
-!- 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:6353198}.
Target cell membrane {ECO:0000250|UniProtKB:P60301}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
-!- TOXIC DOSE: LD(50) is 2.85 mg/kg by intravenous injection.
{ECO:0000269|PubMed:6353198}.
-!- MISCELLANEOUS: Is classified as a P-type cytotoxin, since a
proline residue stands at position 30 (Pro-31 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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ProteinModelPortal; P25517; -.
SMR; P25517; -.
HOVERGEN; HBG006553; -.
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:0019835; P:cytolysis; IEA:UniProtKB-KW.
GO; GO:0009405; P:pathogenesis; IEA:InterPro.
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;
Cardiotoxin; Cytolysis; Direct protein sequencing; Disulfide bond;
Membrane; Secreted; Target cell membrane; Target membrane; Toxin.
CHAIN 1 60 Cytotoxin 5.
/FTId=PRO_0000093509.
DISULFID 3 21 {ECO:0000250}.
DISULFID 14 38 {ECO:0000250}.
DISULFID 42 53 {ECO:0000250}.
DISULFID 54 59 {ECO:0000250}.
SEQUENCE 60 AA; 6845 MW; C7CBE306CC1BC8FD CRC64;
LKCKKLIPLF SKTCPEGKNL CYKMTMRLAP KVPVKRGCID VCPKSSFLVK YECCDTDRCN


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