3SP1_DENJA
ID 3SP1_DENJA Reviewed; 61 AA.
AC P01413;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Toxin S5C1;
OS Dendroaspis jamesoni kaimosae (Eastern Jameson's mamba).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Dendroaspis.
OX NCBI_TaxID=8619;
RN [1]
RP PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=465532; DOI=10.1016/0005-2795(79)90101-6;
RA Joubert F.J., Taljaard N.;
RT "Some properties and the complete primary structures of two reduced and S-
RT carboxymethylated polypeptides (S5C1 and S5C10) from Dendroaspis jamesoni
RT kaimosae (Jameson's mamba) venom.";
RL Biochim. Biophys. Acta 579:228-233(1979).
CC -!- FUNCTION: Inhibits ADP-induced platelet aggregation and inhibits the
CC binding of purified platelet fibrinogen receptor alpha-IIb/beta-3
CC (ITGA2B/ITGB3) to immobilized fibrinogen.
CC {ECO:0000250|UniProtKB:P28375}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:465532}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain
CC subfamily. Antiplatelet toxin sub-subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P01413; -.
DR SMR; P01413; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR Gene3D; 2.10.60.10; -; 1.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR SUPFAM; SSF57302; SSF57302; 1.
PE 1: Evidence at protein level;
KW Cell adhesion impairing toxin; Direct protein sequencing; Disulfide bond;
KW Hemostasis impairing toxin; Platelet aggregation inhibiting toxin;
KW Secreted; Toxin.
FT CHAIN 1..61
FT /note="Toxin S5C1"
FT /evidence="ECO:0000269|PubMed:465532"
FT /id="PRO_0000093658"
FT MOTIF 45..47
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT DISULFID 3..22
FT /evidence="ECO:0000250|UniProtKB:P28375"
FT DISULFID 16..39
FT /evidence="ECO:0000250|UniProtKB:P28375"
FT DISULFID 41..53
FT /evidence="ECO:0000250|UniProtKB:P28375"
FT DISULFID 54..59
FT /evidence="ECO:0000250|UniProtKB:P28375"
SQ SEQUENCE 61 AA; 7024 MW; 34B25A68D48F7EAA CRC64;
RICYNHLGTK PPTTECTQED SCYKNIWRNI TFDNIRRGCG CFTPRGDMPG PYCCESDKCN
L