ID   3SAA_NAJNA              Reviewed;          60 AA.
AC   P86541;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   06-JUL-2016, sequence version 2.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Cytotoxin 10 {ECO:0000303|PubMed:26456928};
DE            Short=CTX10 {ECO:0000303|PubMed:20203422};
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 {ECO:0000303|PubMed:26456928};
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom {ECO:0000303|PubMed:26456928};
RX   PubMed=26456928; DOI=10.1016/j.cbpc.2015.09.015;
RA   Suzuki-Matsubara M., Athauda S.B.P., Suzuki Y., Matsubara R.A.K.,
RA   Moriyama A.;
RT   "Comparison of the primary structures, cytotoxicities, and affinities to
RT   phospholipids of five kinds of cytotoxins from the venom of Indian cobra,
RT   Naja naja.";
RL   Comp. Biochem. Physiol. 179C:158-164(2016).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-30, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom {ECO:0000303|PubMed:20203422};
RX   PubMed=20203422; DOI=10.2220/biomedres.31.71;
RA   Suzuki M., Itoh T., Bandaranayake B.M.A.I.K., Ranasinghe J.G.,
RA   Athauda S.B., Moriyama A.;
RT   "Molecular diversity in venom proteins of the Russell's viper (Daboia
RT   russellii russellii) and the Indian cobra (Naja naja) in Sri Lanka.";
RL   Biomed. Res. 31:71-81(2010).
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 (By similarity). Has hemolytic
CC       activity towards human erythrocytes (EC(50)=0.162 uM) and cytolytic
CC       activity towards various cell lines (PubMed:26456928).
CC       {ECO:0000250|UniProtKB:P60301, ECO:0000250|UniProtKB:P60304,
CC       ECO:0000269|PubMed:26456928}.
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:20203422,
CC       ECO:0000269|PubMed:26456928}. Target cell membrane
CC       {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   AlphaFoldDB; P86541; -.
DR   SMR; P86541; -.
DR   PRIDE; P86541; -.
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 10"
FT                   /evidence="ECO:0000269|PubMed:26456928"
FT                   /id="PRO_0000394690"
FT   DISULFID        3..21
FT                   /evidence="ECO:0000250|UniProtKB:P60304"
FT   DISULFID        14..38
FT                   /evidence="ECO:0000250|UniProtKB:P60304"
FT   DISULFID        42..53
FT                   /evidence="ECO:0000250|UniProtKB:P60304"
FT   DISULFID        54..59
FT                   /evidence="ECO:0000250|UniProtKB:P60304"
SQ   SEQUENCE   60 AA;  6764 MW;  46C9095C6A8A65D0 CRC64;
     LKCNKLVPLF YKTCPAGKDL CYKMYMVATP KVPVKRGCID VCPKSSLLVK YVCCNTDRCN