3SOFL_NAJNA
ID 3SOFL_NAJNA Reviewed; 62 AA.
AC P62377; P14554;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Cytotoxin-like basic protein {ECO:0000303|PubMed:2311757, ECO:0000303|PubMed:2583280};
DE Short=CLBP {ECO:0000303|PubMed:2311757, ECO:0000303|PubMed:2583280};
DE AltName: Full=Less-cytotoxic basic polypeptide {ECO:0000303|PubMed:3566773};
DE Short=LCBP {ECO:0000303|PubMed:3566773};
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.
RC TISSUE=Venom;
RX PubMed=2583280; DOI=10.1016/0014-5793(89)81561-3;
RA Inoue S., Okumura K., Tsujino M., Ohkura K., Ikeda K., Takechi M.,
RA Tanaka Y., Hayashi K.;
RT "Amino acid sequences of cytotoxin-like basic proteins derived from cobra
RT venoms.";
RL FEBS Lett. 257:319-323(1989).
RN [2]
RP PROTEIN SEQUENCE.
RC TISSUE=Venom;
RX PubMed=2311757; DOI=10.1016/0014-5793(90)80563-x;
RA Shafqat J., Zaidi Z.H., Joernvall H.;
RT "Characterization of a cytotoxin-like basic protein from the cobra (Naja
RT naja naja) venom.";
RL FEBS Lett. 261:245-246(1990).
RN [3]
RP PRELIMINARY PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=3566773;
RA Takechi M., Tanaka Y., Hayashi K.;
RT "Amino acid sequence of a less-cytotoxic basic polypeptide (LCBP) isolated
RT from the venom of the Indian cobra (Naja naja).";
RL Biochem. Int. 14:145-152(1987).
CC -!- FUNCTION: Has low cytotoxic activity. {ECO:0000250|UniProtKB:P14541}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3566773}. Target
CC cell membrane {ECO:0000250|UniProtKB:P62375}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- TOXIC DOSE: LD(50) is 60 mg/kg by subcutaneous injection.
CC -!- MISCELLANEOUS: Is classified as a P-type cytotoxin, since a proline
CC residue stands at position 31 (Pro-31 in standard classification).
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain
CC subfamily. Orphan group XV sub-subfamily. {ECO:0000305}.
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DR PIR; S06674; S06674.
DR AlphaFoldDB; P62377; -.
DR BMRB; P62377; -.
DR SMR; P62377; -.
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:0044179; P:hemolysis in another organism; 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 InterPro; IPR035076; Toxin/TOLIP.
DR Pfam; PF00087; Toxin_TOLIP; 1.
DR PRINTS; PR00282; CYTOTOXIN.
DR SUPFAM; SSF57302; SSF57302; 1.
DR PROSITE; PS00272; SNAKE_TOXIN; 1.
PE 1: Evidence at protein level;
KW Cytolysis; Direct protein sequencing; Disulfide bond; Hemolysis; Membrane;
KW Reference proteome; Secreted; Target cell membrane; Target membrane; Toxin.
FT CHAIN 1..62
FT /note="Cytotoxin-like basic protein"
FT /evidence="ECO:0000269|PubMed:2311757,
FT ECO:0000269|PubMed:2583280"
FT /id="PRO_0000093525"
FT DISULFID 3..22
FT /evidence="ECO:0000250|UniProtKB:P60301"
FT DISULFID 15..40
FT /evidence="ECO:0000250|UniProtKB:P60301"
FT DISULFID 44..55
FT /evidence="ECO:0000250|UniProtKB:P60301"
FT DISULFID 56..61
FT /evidence="ECO:0000250|UniProtKB:P60301"
SQ SEQUENCE 62 AA; 7014 MW; 0E88D09AEFA7FBA5 CRC64;
LKCHNTQLPF IYKTCPEGKN LCFKATLKKF PLKFPVKRGC ADNCPKNSAL LKYVCCSTDK
CN