TX14A_SCODE
ID TX14A_SCODE Reviewed; 577 AA.
AC P0DPU3;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 10-APR-2019, sequence version 1.
DT 25-MAY-2022, entry version 10.
DE RecName: Full=Scoloptoxin SSD14 {ECO:0000303|PubMed:23148443};
DE Short=SLPTX-SSD14 {ECO:0000303|PubMed:23148443};
DE Short=Toxin-SSD14 {ECO:0000303|PubMed:23148443};
DE Contains:
DE RecName: Full=SLPTX-SSD14 subunit alpha {ECO:0000303|PubMed:23148443};
DE Contains:
DE RecName: Full=SLPTX-SSD14 subunit beta {ECO:0000303|PubMed:23148443};
DE Flags: Precursor;
OS Scolopendra dehaani (Thai centipede) (Scolopendra subspinipes dehaani).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC Pleurostigmophora; Scolopendromorpha; Scolopendridae; Scolopendra.
OX NCBI_TaxID=2609776;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-34 AND 387-395,
RP SUBCELLULAR LOCATION, AND FUNCTION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=23148443; DOI=10.1021/pr300881d;
RA Liu Z.C., Zhang R., Zhao F., Chen Z.M., Liu H.W., Wang Y.J., Jiang P.,
RA Zhang Y., Wu Y., Ding J.P., Lee W.H., Zhang Y.;
RT "Venomic and transcriptomic analysis of centipede Scolopendra subspinipes
RT dehaani.";
RL J. Proteome Res. 11:6197-6212(2012).
CC -!- FUNCTION: Dose-dependently induces human platelet aggregation on both
CC plasma rich platelet and washed platelet (max. response at 3.2 ug/mL)
CC and causes hemolysis against mouse and rabbit erythrocytes (35 and 65%
CC respectively at 5 ug/mL). Does not show hemolytic activity against
CC human erythrocytes (even at 100 ug/mL). {ECO:0000269|PubMed:23148443}.
CC -!- SUBUNIT: Heterodimer composed of subunits alpha and beta; probably
CC disulfide-linked. {ECO:0000269|PubMed:23148443}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23148443}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:23148443}.
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DR EMBL; KC144034; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; P0DPU3; -.
DR SMR; P0DPU3; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0036374; F:glutathione hydrolase activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006751; P:glutathione catabolic process; IEA:InterPro.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR Gene3D; 1.10.246.130; -; 1.
DR Gene3D; 3.60.20.40; -; 1.
DR InterPro; IPR043138; GGT_lsub_C.
DR InterPro; IPR000101; GGT_peptidase.
DR InterPro; IPR043137; GGT_ssub.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR PANTHER; PTHR11686; PTHR11686; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR00066; g_glut_trans; 1.
PE 1: Evidence at protein level;
KW Cytolysis; Direct protein sequencing; Disulfide bond; Hemolysis;
KW Hemostasis impairing toxin; Platelet aggregation activating toxin;
KW Secreted; Signal; Toxin.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:23148443"
FT CHAIN 26..386
FT /note="SLPTX-SSD14 subunit alpha"
FT /evidence="ECO:0000305"
FT /id="PRO_0000446690"
FT CHAIN 387..577
FT /note="SLPTX-SSD14 subunit beta"
FT /evidence="ECO:0000305"
FT /id="PRO_0000446691"
SQ SEQUENCE 577 AA; 62689 MW; C0A76A402D4662A2 CRC64;
MGTSYRKLGY VLFLMLGMIV EEGIAYVRVK EKQSSPSFMG IYDESAVASD AVPCAEAGQS
MLRQKGSAVD AAIATLLCIG VYNPQSSGIG GGSFMVIYDR STRTPEVIDA REEAPAAATQ
KMFKGDKKLS SEGGLSIAVP GELRGMALAH ERHGKLDWET LFQPAIRLAK EGFPVGSELA
MALREQRSHI LNSPTLKAVF TDPVSGDILK ENDIVIRTKL GETLEKIAKN GADEFYEGQV
AKDLINDIKS FGGIITAEDL KNYQPVLKNA TVAHLSGCLT LYSVPPPSSG YILSFILRVL
DKFHFSKASV SDIENATLTY HRFLETLKYA YAYRTKLGDE RIENVSSVIA ELTSEDVIEK
TKQKIEDGKT YEPLHYGAQL ATNDHGTAHI SVVSREGDAV VVTTTINYWF GSGLRSPSTG
VILNDEMDDF SAPDIQNIYG VPPSKANFIV PGKRPQSSTC PSIFVNKGGD VVMAIGASGG
TRITSSVSLT SMRVLWLGRN IKEAIDEPRL HHQLLPDEIE YESKFPNEIL EKLKAIGHKT
KPAGAFGSLV VGIKRMKGGT LTANYDYRRG GSVDGSK