3SAT_NAJAT
ID 3SAT_NAJAT Reviewed; 60 AA.
AC P07525;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Cytotoxin 5;
DE AltName: Full=Cardiotoxin A4b;
DE Short=CTX-A4b;
DE AltName: Full=Cardiotoxin T;
DE AltName: Full=Cardiotoxin analog V;
DE Short=CTX V;
DE AltName: Full=Cytotoxin D-1;
DE AltName: Full=Membrane toxin D1;
OS Naja atra (Chinese cobra).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=8656;
RN [1]
RP PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RA Wu W.Y., Du Y.C.;
RT "The complete amino acid sequence of cytotoxin D-1.";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 16:310-315(1984).
RN [2]
RP STRUCTURE BY NMR, AND DISULFIDE BONDS.
RC TISSUE=Venom;
RX PubMed=10794406; DOI=10.1110/ps.9.4.637;
RA Jayaraman G., Kumar T.K.S., Tsai C.-C., Srisailam S., Chou S.-H., Ho C.-L.,
RA Yu C.;
RT "Elucidation of the solution structure of cardiotoxin analogue V from the
RT Taiwan cobra (Naja naja atra) -- identification of structural features
RT important for the lethal action of snake venom cardiotoxins.";
RL Protein Sci. 9:637-646(2000).
CC -!- FUNCTION: Basic protein that binds to cell membrane and depolarizes
CC cardiomyocytes. It also possesses lytic activity on many other cells,
CC including red blood cells. Interaction with sulfatides in the cell
CC membrane induces pore formation and cell internalization and is
CC responsible for cytotoxicity in cardiomyocytes. It targets the
CC mitochondrial membrane and induces mitochondrial swelling and
CC fragmentation. Inhibits protein kinases C. It binds to the integrin
CC alpha-V/beta-3 with a moderate affinity (By similarity). Is cardiotoxic
CC and cytocidal to Yoshida sarcoma cells. {ECO:0000250|UniProtKB:P01443}.
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|Ref.1}. Target cell
CC membrane {ECO:0000250|UniProtKB:P60301}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
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}.
CC -!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain
CC subfamily. Type IA cytotoxin sub-subfamily. {ECO:0000305}.
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DR PIR; JC0001; H3NJ5F.
DR PDB; 1CHV; NMR; -; S=1-60.
DR PDBsum; 1CHV; -.
DR AlphaFoldDB; P07525; -.
DR SMR; P07525; -.
DR EvolutionaryTrace; P07525; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in another organism; 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; Hemolysis; Ion channel impairing toxin; Membrane; Secreted;
KW Target cell membrane; Target membrane; Toxin.
FT CHAIN 1..60
FT /note="Cytotoxin 5"
FT /evidence="ECO:0000269|Ref.1"
FT /id="PRO_0000093480"
FT DISULFID 3..21
FT /evidence="ECO:0000269|PubMed:10794406,
FT ECO:0000312|PDB:1CHV"
FT DISULFID 14..38
FT /evidence="ECO:0000269|PubMed:10794406,
FT ECO:0000312|PDB:1CHV"
FT DISULFID 42..53
FT /evidence="ECO:0000269|PubMed:10794406,
FT ECO:0000312|PDB:1CHV"
FT DISULFID 54..59
FT /evidence="ECO:0000269|PubMed:10794406,
FT ECO:0000312|PDB:1CHV"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:1CHV"
FT STRAND 20..26
FT /evidence="ECO:0007829|PDB:1CHV"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:1CHV"
FT STRAND 32..40
FT /evidence="ECO:0007829|PDB:1CHV"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:1CHV"
SQ SEQUENCE 60 AA; 6810 MW; 513D5F8D50B78F1C CRC64;
LKCNKLVPLF YKTCPAGKNL CYKMFMVSNK MVPVKRGCID VCPKSSLLVK YVCCNTDRCN
