3SAC3_NAJSP
ID 3SAC3_NAJSP Reviewed; 60 AA.
AC P60311;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Cytotoxin KJC3;
OS Naja sputatrix (Malayan spitting cobra) (Naja naja sputatrix).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=33626;
RN [1]
RP PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=9565688; DOI=10.1016/s0304-4165(97)00143-8;
RA Jeyaseelan K., Armugam A., Lachumanan R., Tan C.H., Tan N.H.;
RT "Six isoforms of cardiotoxin in malayan spitting cobra (Naja naja
RT sputatrix) venom: cloning and characterization of cDNAs.";
RL Biochim. Biophys. Acta 1380:209-222(1998).
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:9565688}. Target
CC cell 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 AlphaFoldDB; P60311; -.
DR SMR; P60311; -.
DR PRIDE; P60311; -.
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 KJC3"
FT /evidence="ECO:0000269|PubMed:9565688"
FT /id="PRO_0000093521"
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; 6753 MW; C0FDBF8558A168FD CRC64;
DKCNKLVPLF YKTCPAGKNL CYKMFMVSDL TVPVKRGCID VCPKNSALVK YVCCNTDRCN