3SA4_NAJMO
ID 3SA4_NAJMO Reviewed; 60 AA.
AC P01452;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Cytotoxin 4 {ECO:0000305};
DE AltName: Full=CTX M3 {ECO:0000303|PubMed:8182052};
DE AltName: Full=Cardiotoxin VII4 {ECO:0000303|PubMed:2370666};
DE AltName: Full=Cytotoxin V(II)4 {ECO:0000303|PubMed:4834686};
OS Naja mossambica (Mozambique spitting cobra).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=8644;
RN [1]
RP PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=4834686; DOI=10.1016/s0006-291x(74)80246-9;
RA Louw A.I.;
RT "Snake venom toxins. The complete amino acid sequence of cytotoxin VII4
RT from the venom of Naja mossambica mossambica.";
RL Biochem. Biophys. Res. Commun. 58:1022-1029(1974).
RN [2]
RP FUNCTION, AND APPARTENANCE TO S-TYPE CYTOTOXIN GROUP.
RX PubMed=8182052; DOI=10.1016/s0021-9258(17)36647-4;
RA Chien K.-Y., Chiang C.-M., Hseu Y.-C., Vyas A.A., Rule G.S., Wu W.-G.;
RT "Two distinct types of cardiotoxin as revealed by the structure and
RT activity relationship of their interaction with zwitterionic phospholipid
RT dispersions.";
RL J. Biol. Chem. 269:14473-14483(1994).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND DISULFIDE BONDS.
RX PubMed=2370666; DOI=10.1016/0022-2836(90)90161-e;
RA Rees B., Bilwes A., Samama J.-P., Moras D.;
RT "Cardiotoxin VII4 from Naja mossambica mossambica. The refined crystal
RT structure.";
RL J. Mol. Biol. 214:281-297(1990).
CC -!- FUNCTION: Shows cytolytic activity on many different cells by forming
CC pore in lipid membranes. In vivo, increases heart rate or kills the
CC animal by cardiac arrest. In addition, it binds to heparin with high
CC affinity, interacts with Kv channel-interacting protein 1 (KCNIP1) in a
CC calcium-independent manner, and binds to integrin alpha-V/beta-3
CC (ITGAV/ITGB3) with moderate affinity. {ECO:0000250|UniProtKB:P60301,
CC ECO:0000250|UniProtKB:P60304, ECO:0000269|PubMed:8182052}.
CC -!- SUBUNIT: Monomer in solution; Homodimer and oligomer in the presence of
CC negatively charged lipids forming a pore with a size ranging between 20
CC and 30 Angstroms. {ECO:0000250|UniProtKB:P60301}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:4834686}. Target
CC cell membrane {ECO:0000250|UniProtKB:P60301}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- TOXIC DOSE: LD(50) is 1.97 mg/kg by intravenous injection.
CC -!- MISCELLANEOUS: Is classified as a S-type cytotoxin, since a serine
CC residue stands at position 28 (Ser-29 in standard classification).
CC {ECO:0000305|PubMed:8182052}.
CC -!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain
CC subfamily. Type IA cytotoxin sub-subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; A01717; H3NJ4M.
DR PDB; 1CDT; X-ray; 2.50 A; A/B=1-60.
DR PDBsum; 1CDT; -.
DR AlphaFoldDB; P01452; -.
DR BMRB; P01452; -.
DR SMR; P01452; -.
DR PRIDE; P01452; -.
DR EvolutionaryTrace; P01452; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR CDD; cd00206; snake_toxin; 1.
DR Gene3D; 2.10.60.10; -; 1.
DR InterPro; IPR003572; Cytotoxin_Cobra.
DR InterPro; IPR003571; Snake_3FTx.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR InterPro; IPR018354; Snake_toxin_con_site.
DR PRINTS; PR00282; CYTOTOXIN.
DR SUPFAM; SSF57302; SSF57302; 1.
DR PROSITE; PS00272; SNAKE_TOXIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cardiotoxin; Cytolysis; Direct protein sequencing;
KW Disulfide bond; Membrane; Secreted; Target cell membrane; Target membrane;
KW Toxin.
FT CHAIN 1..60
FT /note="Cytotoxin 4"
FT /evidence="ECO:0000269|PubMed:4834686"
FT /id="PRO_0000093508"
FT DISULFID 3..21
FT /evidence="ECO:0000269|PubMed:2370666,
FT ECO:0000312|PDB:1CDT"
FT DISULFID 14..38
FT /evidence="ECO:0000269|PubMed:2370666,
FT ECO:0000312|PDB:1CDT"
FT DISULFID 42..53
FT /evidence="ECO:0000269|PubMed:2370666,
FT ECO:0000312|PDB:1CDT"
FT DISULFID 54..59
FT /evidence="ECO:0000269|PubMed:2370666,
FT ECO:0000312|PDB:1CDT"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:1CDT"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:1CDT"
FT STRAND 20..26
FT /evidence="ECO:0007829|PDB:1CDT"
FT TURN 27..30
FT /evidence="ECO:0007829|PDB:1CDT"
FT STRAND 32..41
FT /evidence="ECO:0007829|PDB:1CDT"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:1CDT"
SQ SEQUENCE 60 AA; 6715 MW; F37CCB912A6EA48A CRC64;
LKCNKLIPIA YKTCPEGKNL CYKMMLASKK MVPVKRGCIN VCPKNSALVK YVCCSTDRCN
