3SA2_NAJNA
ID 3SA2_NAJNA Reviewed; 60 AA.
AC P01440;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Cytotoxin 2 {ECO:0000305|PubMed:4340873};
DE AltName: Full=Cobramine-B;
DE AltName: Full=Cytotoxin II {ECO:0000303|PubMed:4340873};
OS Naja naja (Indian cobra).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=35670;
RN [1]
RP PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=4340873;
RA Takechi M., Hayashi K., Sasaki T.;
RT "The amino acid sequence of cytotoxin II from the venom of the Indian cobra
RT (Naja naja).";
RL Mol. Pharmacol. 8:446-451(1972).
RN [2]
RP DISULFIDE BONDS.
RX PubMed=4674343; DOI=10.1016/0006-291x(72)90451-2;
RA Takechi M., Hayashi K.;
RT "Localization of the four disulfide bridges in cytotoxin II from the venom
RT of the indian cobra (Naja naja).";
RL Biochem. Biophys. Res. Commun. 49:584-590(1972).
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}.
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:4340873}. Target
CC cell membrane {ECO:0000250|UniProtKB:P60301}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- MISCELLANEOUS: Is classified as a P-type cytotoxin, since a proline
CC residue stands at position 30 (Pro-31 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; A01708; H3NJ2I.
DR AlphaFoldDB; P01440; -.
DR SMR; P01440; -.
DR Proteomes; UP000694559; Unplaced.
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 InterPro; IPR035076; Toxin/TOLIP.
DR Pfam; PF00087; Toxin_TOLIP; 1.
DR PRINTS; PR00282; CYTOTOXIN.
DR SUPFAM; SSF57302; SSF57302; 1.
DR PROSITE; PS00272; SNAKE_TOXIN; 1.
PE 1: Evidence at protein level;
KW Cardiotoxin; Cytolysis; Direct protein sequencing; Disulfide bond;
KW Membrane; Reference proteome; Secreted; Target cell membrane;
KW Target membrane; Toxin.
FT CHAIN 1..60
FT /note="Cytotoxin 2"
FT /evidence="ECO:0000269|PubMed:4340873"
FT /id="PRO_0000093511"
FT DISULFID 3..21
FT /evidence="ECO:0000269|PubMed:4674343"
FT DISULFID 14..38
FT /evidence="ECO:0000269|PubMed:4674343"
FT DISULFID 42..53
FT /evidence="ECO:0000269|PubMed:4674343"
FT DISULFID 54..59
FT /evidence="ECO:0000269|PubMed:4674343"
SQ SEQUENCE 60 AA; 6763 MW; 46C121E2067865D0 CRC64;
LKCNKLVPLF YKTCPAGKNL CYKMYMVATP KVPVKRGCID VCPKSSLVLK YVCCNTDRCN
