ID   3SOG_ASPSC              Reviewed;          63 AA.
AC   P19003;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Cytotoxin homolog S3C2;
OS   Aspidelaps scutatus (Shield-nose snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Acanthophiinae; Aspidelaps.
OX   NCBI_TaxID=8607;
RN   [1]
RP   PROTEIN SEQUENCE, TOXIC DOSE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=3356299; DOI=10.1016/0020-711x(88)90361-8;
RA   Joubert F.J.;
RT   "Snake venom toxins -- II. The primary structures of cytotoxin homologues
RT   S3C2 and S4C8 from Aspidelaps scutatus (shield or shield-nose snake)
RT   venom.";
RL   Int. J. Biochem. 20:337-345(1988).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3356299}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- TOXIC DOSE: LD(50) is 6.6 mg/kg by intravenous injection.
CC       {ECO:0000269|PubMed:3356299}.
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 XVI sub-subfamily. {ECO:0000305}.
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DR   PIR; JS0298; JS0298.
DR   AlphaFoldDB; P19003; -.
DR   SMR; P19003; -.
DR   PRIDE; P19003; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; Secreted; Toxin.
FT   CHAIN           1..63
FT                   /note="Cytotoxin homolog S3C2"
FT                   /evidence="ECO:0000269|PubMed:3356299"
FT                   /id="PRO_0000093522"
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   63 AA;  7173 MW;  18733F32E9D1F270 CRC64;
     RKCLNTPLPL FYKTCPEGKD LCYKMNFKLL PKKLSIKRGC TDTCPKSSLL VKVVCCDTDK
     CNK