3SA2A_NAJNA
ID 3SA2A_NAJNA Reviewed; 60 AA.
AC P86538;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-JUL-2016, sequence version 2.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Cytotoxin 2a {ECO:0000305|PubMed:20203422};
DE Short=CTX2a {ECO:0000305|PubMed:20203422};
DE AltName: Full=Cytotoxin 2 {ECO:0000303|PubMed:20203422};
DE Short=CTX2 {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:20203422};
RN [1] {ECO:0000305}
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 1-29, 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). Preferentially
CC binds acidic phospholipids like phosphatidylserine, phosphatidic acid
CC and phosphatidyl glycerol (PubMed:26456928). Has hemolytic activity
CC towards human erythrocytes (EC(50)=1.024 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; P86538; -.
DR SMR; P86538; -.
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 2a"
FT /evidence="ECO:0000269|PubMed:20203422,
FT ECO:0000269|PubMed:26456928"
FT /id="PRO_0000394686"
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; 6711 MW; D76F1BAC3CD27500 CRC64;
LQCNKLVPIA SKTCPPGKNL CYKMFMVSDL TIPVKRGCID VCPKNSLLVK YECCNTDRCN
