ID   3SA7_NAJNA              Reviewed;          60 AA.
AC   P86382;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Cytotoxin 7 {ECO:0000303|PubMed:26456928};
DE            Short=CTX7 {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;
RN   [1]
RP   PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
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).
RN   [2]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
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).
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). Preferentially
CC       binds acidic phospholipids like phosphatidylserine, phosphatidic acid
CC       and phosphatidyl glycerol (PubMed:26456928). Has hemolytic activity
CC       towards human erythrocytes (EC(50)=0.171 uM) and cytolytic activity
CC       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 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; P86382; -.
DR   SMR; P86382; -.
DR   PRIDE; P86382; -.
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 7"
FT                   /evidence="ECO:0000269|PubMed:20203422"
FT                   /id="PRO_0000394688"
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;  6792 MW;  9385726C6A86D5E2 CRC64;
     LKCNKLIPLA YKTCPAGKDL CYKMYMVSNK TVPVKRGCID VCPKNSLLVK YECCNTDRCN