ID   3SIY3_DENAN             Reviewed;          63 AA.
AC   P01408;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Synergistic-type venom protein C9S3, chain 1;
OS   Dendroaspis angusticeps (Eastern green mamba) (Naja angusticeps).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Dendroaspis.
OX   NCBI_TaxID=8618;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=511106; DOI=10.1515/bchm2.1979.360.2.1075;
RA   Joubert F.J., Viljoen C.C.;
RT   "Snake venom. The amino-acid sequence of the subunits of two reduced and S-
RT   carboxymethylated proteins (C8S2 and C9S3) from Dendroaspis angusticeps
RT   venom.";
RL   Hoppe-Seyler's Z. Physiol. Chem. 360:1075-1090(1979).
CC   -!- FUNCTION: This protein shows a synergetic toxic effect in that it
CC       enhances the toxicity of other toxins. {ECO:0000269|PubMed:511106}.
CC   -!- SUBUNIT: Heterodimer of C9S3 chain 1 and chain 2 (AC P01409);
CC       disulfide-linked. {ECO:0000250|UniProtKB:P0DQP2}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:511106}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:511106}.
CC   -!- MISCELLANEOUS: Is classified as a P-type cytotoxin, since a proline
CC       residue stands at position 33 (Pro-31 in standard classification).
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain
CC       subfamily. Aminergic toxin sub-subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P01408; -.
DR   SMR; P01408; -.
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; 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   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="Synergistic-type venom protein C9S3, chain 1"
FT                   /evidence="ECO:0000269|PubMed:511106"
FT                   /id="PRO_0000093621"
FT   DISULFID        3..24
FT                   /evidence="ECO:0000250|UniProtKB:P0DQP2"
FT   DISULFID        17..42
FT                   /evidence="ECO:0000250|UniProtKB:P0DQP2"
FT   DISULFID        46..57
FT                   /evidence="ECO:0000250|UniProtKB:P0DQP2"
FT   DISULFID        54
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250|UniProtKB:P0DQP2"
SQ   SEQUENCE   63 AA;  6785 MW;  7855077E429339C0 CRC64;
     LTCVTGKSIG GISTEECAAG QKICFKKWTK MGPKLYDVSR GCTATCPKAD EYGCVKCCKT
     DRN