3SAS_NAJSG
ID 3SAS_NAJSG Reviewed; 60 AA.
AC P83345;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Cytotoxin sagitoxin;
DE AltName: Full=Cardiotoxin sagitoxin;
OS Naja sagittifera (Andaman cobra).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=195058;
RN [1]
RP PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RA Sharma S., Singh R.K., Srinivasan A., Singh T.P.;
RT "Purification and sequence determination of a cardiotoxin from Naja naja
RT sagittifera (South Indian cobra).";
RL Submitted (MAY-2002) to UniProtKB.
RN [2]
RP CRYSTALLIZATION, AND SUBUNIT.
RC TISSUE=Venom;
RX PubMed=18540072; DOI=10.1107/s1744309108014334;
RA Mir R., Sinha M., Sharma S., Singh N., Kaur P., Srinivasan A., Singh T.P.;
RT "Isolation, purification, crystallization and preliminary crystallographic
RT studies of sagitoxin, an oligomeric cardiotoxin from the venom of Naja naja
RT saggitifera.";
RL Acta Crystallogr. F 64:545-547(2008).
CC -!- FUNCTION: Shows cytolytic activity on many different cells by forming
CC pore in lipid membranes. In vivo, increases heart rate or kill 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 (By similarity); Homodimer and oligomer
CC (homohexamer (PubMed:18540072)) in the presence of negatively charged
CC lipids forming a pore with a size ranging between 20 and 30 Angstroms
CC (By similarity). {ECO:0000250|UniProtKB:P60301,
CC ECO:0000269|PubMed:18540072}.
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 -!- 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 AlphaFoldDB; P83345; -.
DR SMR; P83345; -.
DR PRIDE; P83345; -.
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 Cardiotoxin; Cytolysis; Direct protein sequencing; Disulfide bond;
KW Membrane; Secreted; Target cell membrane; Target membrane; Toxin.
FT CHAIN 1..60
FT /note="Cytotoxin sagitoxin"
FT /evidence="ECO:0000269|Ref.1"
FT /id="PRO_0000093520"
FT DISULFID 3..21
FT /evidence="ECO:0000250|UniProtKB:P60301"
FT DISULFID 14..38
FT /evidence="ECO:0000250|UniProtKB:P60301"
FT DISULFID 42..53
FT /evidence="ECO:0000250|UniProtKB:P60301"
FT DISULFID 54..59
FT /evidence="ECO:0000250|UniProtKB:P60301"
SQ SEQUENCE 60 AA; 6802 MW; 13C5C4AEE88F2F64 CRC64;
LKCNKLVPLA YKTCPAGKNL CYKMYMVANK KVPVKRGCID VCPKKSLLVK YECCNTDRCN