3SA1_NAJNA
ID 3SA1_NAJNA Reviewed; 60 AA.
AC P01447; Q9PSN2;
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 1;
DE AltName: Full=Cobramine-A {ECO:0000303|PubMed:4332596};
DE AltName: Full=Cytotoxin I {ECO:0000303|PubMed:4332596};
DE AltName: Full=Cytotoxin XI;
DE AltName: Full=Cytotoxin-like basic protein {ECO:0000303|PubMed:7558599};
DE Short=CLBP {ECO:0000303|PubMed:7558599};
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=4332596; DOI=10.1016/0006-291x(71)90169-0;
RA Hayashi K., Takechi M., Sasaki T.;
RT "Amino acid sequence of cytotoxin I from the venom of the Indian cobra
RT (Naja naja).";
RL Biochem. Biophys. Res. Commun. 45:1357-1362(1971).
RN [2]
RP PROTEIN SEQUENCE.
RX PubMed=7558599; DOI=10.1111/j.1399-3011.1995.tb00583.x;
RA Babu A.S., Puri K.D., Gowda T.V.;
RT "Primary structure of a cytotoxin-like basic protein from Naja naja naja
RT (Indian cobra) venom.";
RL Int. J. Pept. Protein Res. 46:69-72(1995).
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:4332596}. 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 PIR; A01713; H3NJ1I.
DR AlphaFoldDB; P01447; -.
DR SMR; P01447; -.
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 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 1"
FT /evidence="ECO:0000269|PubMed:4332596,
FT ECO:0000269|PubMed:7558599"
FT /id="PRO_0000093510"
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"
FT CONFLICT 48..50
FT /note="VLK -> LVT (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="N -> NL (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 60 AA; 6791 MW; 938D5AD20674D5E2 CRC64;
LKCNKLIPLA YKTCPAGKNL CYKMYMVSNK TVPVKRGCID VCPKNSLVLK YECCNTDRCN
