ID   3SOFB_NAJHA             Reviewed;          62 AA.
AC   P62390; P01472;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Cytotoxin 11;
DE   AltName: Full=Toxin CM-13a {ECO:0000303|PubMed:1278155};
OS   Naja annulifera (Banded Egyptian cobra) (Naja haje annulifera).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX   NCBI_TaxID=96794;
RN   [1]
RP   PROTEIN SEQUENCE, TOXIC DOSE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=1278155; DOI=10.1111/j.1432-1033.1976.tb10291.x;
RA   Joubert F.J.;
RT   "Snake venom toxins. The amino-acid sequences of three toxins (CM-8, CM-11
RT   and CM-13a) from Naja haje annulifera (Egyptian cobra) venom.";
RL   Eur. J. Biochem. 64:219-232(1976).
RN   [2]
RP   SEQUENCE REVISION TO 53-62.
RC   TISSUE=Venom;
RX   PubMed=710433; DOI=10.1111/j.1432-1033.1978.tb12612.x;
RA   Joubert F.J., Taljaard N.;
RT   "Naja haje haje (Egyptian cobra) venom. Some properties and the complete
RT   primary structure of three toxins (CM-2, CM-11 and CM-12).";
RL   Eur. J. Biochem. 90:359-367(1978).
CC   -!- FUNCTION: Has low cytotoxic activity. {ECO:0000250|UniProtKB:P14541}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1278155}. Target
CC       cell membrane {ECO:0000250|UniProtKB:P62375}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- TOXIC DOSE: LD(50) is 25.2 mg/kg by intravenous injection.
CC       {ECO:0000269|PubMed:1278155}.
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; A01732; H3NJZE.
DR   AlphaFoldDB; P62390; -.
DR   SMR; P62390; -.
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 11"
FT                   /evidence="ECO:0000269|PubMed:1278155"
FT                   /id="PRO_0000093495"
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;  6842 MW;  7BBADD9BD39C0264 CRC64;
     LKCHNTQLPF IYKTCPEGKN LCFKTTLKKL PLKIPIKRGC AATCPKSSAL LKVVCCSTDK
     CN