ID   3SOFH_NAJKA             Reviewed;          62 AA.
AC   P14541;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Cytotoxin homolog;
DE   AltName: Full=Cytotoxin-like basic protein {ECO:0000303|PubMed:3595859};
DE            Short=CLBP {ECO:0000303|PubMed:3595859};
OS   Naja kaouthia (Monocled cobra) (Naja siamensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX   NCBI_TaxID=8649;
RN   [1]
RP   PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=3595859; DOI=10.1016/0014-5793(87)81009-8;
RA   Inoue S., Ohkura K., Ikeda K., Hayashi K.;
RT   "Amino acid sequence of a cytotoxin-like basic protein with low cytotoxic
RT   activity from the venom of the Thailand cobra Naja naja siamensis.";
RL   FEBS Lett. 218:17-21(1987).
CC   -!- FUNCTION: Has low cytotoxic activity. {ECO:0000269|PubMed:3595859}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3595859}. Target
CC       cell membrane {ECO:0000250|UniProtKB:P62375}.
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 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; A27025; A27025.
DR   AlphaFoldDB; P14541; -.
DR   SMR; P14541; -.
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   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   Direct protein sequencing; Disulfide bond; Membrane; Secreted;
KW   Target cell membrane; Target membrane; Toxin.
FT   CHAIN           1..62
FT                   /note="Cytotoxin homolog"
FT                   /evidence="ECO:0000269|PubMed:3595859"
FT                   /id="PRO_0000093526"
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;  6994 MW;  0E88CE6B0F5704A5 CRC64;
     LKCHNTQLPF IYKTCPEGKN LCFKATLKKF PLKIPIKRGC ADNCPKNSAL LKYVCCSTDK
     CN