3SL2_DENAN
ID 3SL2_DENAN Reviewed; 60 AA.
AC P25684;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Toxin C10S2C2;
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, TOXIC DOSE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=7397227; DOI=10.1016/0005-2795(80)90274-3;
RA Joubert F.J., Taljaard N.;
RT "The complete primary structures of two reduced and S-carboxymethylated
RT Angusticeps-type toxins from Dendroaspis angusticeps (green mamba) venom.";
RL Biochim. Biophys. Acta 623:449-456(1980).
CC -!- FUNCTION: This specific blocker of the L-type calcium channel
CC (Cav1/CACNA1) is a smooth muscle relaxant and an inhibitor of cardiac
CC contractions. {ECO:0000250|UniProtKB:P01414}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7397227}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- TOXIC DOSE: LD(50) is 23 +/- 3 mg/kg by intravenous injection.
CC {ECO:0000269|PubMed:7397227}.
CC -!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain
CC subfamily. L-type calcium blocker 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; P25684; -.
DR SMR; P25684; -.
DR PRIDE; P25684; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005246; F:calcium channel regulator activity; IEA:UniProtKB-KW.
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 InterPro; IPR018354; Snake_toxin_con_site.
DR SUPFAM; SSF57302; SSF57302; 1.
DR PROSITE; PS00272; SNAKE_TOXIN; 1.
PE 1: Evidence at protein level;
KW Calcium channel impairing toxin; Cardiotoxin; Direct protein sequencing;
KW Disulfide bond; Ion channel impairing toxin; Secreted; Toxin;
KW Voltage-gated calcium channel impairing toxin.
FT CHAIN 1..60
FT /note="Toxin C10S2C2"
FT /evidence="ECO:0000269|PubMed:7397227"
FT /id="PRO_0000093665"
FT REGION 41..48
FT /note="Important for binding to L-type calcium channels"
FT /evidence="ECO:0000250|UniProtKB:P01414"
FT DISULFID 3..22
FT /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT DISULFID 17..39
FT /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT DISULFID 41..52
FT /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT DISULFID 53..58
FT /evidence="ECO:0000250|UniProtKB:P0C1Z0"
SQ SEQUENCE 60 AA; 6818 MW; C7BAC44373B63CE8 CRC64;
RICYSHKASL PRATKTCVEN SCYKMFIRTS PDYISDRGCG CPTAMWPYQT ACCKGDRCNK