VSPSX_GLOSA
ID VSPSX_GLOSA Reviewed; 258 AA.
AC Q7SZE1;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Thrombin-like enzyme saxthrombin;
DE Short=SVTLE;
DE EC=3.4.21.-;
DE AltName: Full=Fibrinogen-clotting enzyme;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
DE AltName: Full=Thrombin-like enzyme defibrase;
DE Flags: Precursor;
OS Gloydius saxatilis (Rock mamushi) (Gloydius intermedius saxatilis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX NCBI_TaxID=92067;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBUNIT.
RC TISSUE=Venom, and Venom gland;
RA Sun D.J., Yang C.W., Yang T.S., Yan W.Q., Wang W.;
RT "Purification, cDNA cloning and sequence analysis of thrombin-like enzyme
RT from Gloydius saxatilis.";
RL Dong Wu Xue Bao 49:878-882(2003).
RN [2]
RP FUNCTION, AND CRYSTALLIZATION.
RC TISSUE=Venom;
RX PubMed=17671373; DOI=10.1107/s1744309107031429;
RA Wei W., Zhao W., Wang X., Teng M., Niu L.;
RT "Purification, crystallization and preliminary X-ray diffraction analysis
RT of saxthrombin, a thrombin-like enzyme from Gloydius saxatilis venom.";
RL Acta Crystallogr. F 63:704-707(2007).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS), DISULFIDE BOND, AND ACTIVE SITES.
RC TISSUE=Venom;
RX PubMed=21821882; DOI=10.1107/s1744309111022548;
RA Huang K., Zhao W., Gao Y., Wei W., Teng M., Niu L.;
RT "Structure of saxthrombin, a thrombin-like enzyme from Gloydius
RT saxatilis.";
RL Acta Crystallogr. F 67:862-865(2011).
CC -!- FUNCTION: Thrombin-like snake venom serine protease that shows strong
CC blood coagulation activity in vitro. {ECO:0000269|PubMed:17671373}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|Ref.1}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; AY204243; AAP20638.1; -; mRNA.
DR PDB; 3S69; X-ray; 1.43 A; A=25-258.
DR PDBsum; 3S69; -.
DR AlphaFoldDB; Q7SZE1; -.
DR SMR; Q7SZE1; -.
DR MEROPS; S01.347; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Blood coagulation cascade activating toxin; Disulfide bond;
KW Glycoprotein; Hemostasis impairing toxin; Hydrolase; Protease; Secreted;
KW Serine protease; Signal; Toxin; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..24
FT /evidence="ECO:0000305"
FT /id="PRO_0000296366"
FT CHAIN 25..258
FT /note="Thrombin-like enzyme saxthrombin"
FT /evidence="ECO:0000305|PubMed:21821882, ECO:0000305|Ref.1"
FT /id="PRO_0000296367"
FT DOMAIN 25..249
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 65
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:21821882"
FT ACT_SITE 110
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:21821882"
FT ACT_SITE 204
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:21821882"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..163
FT /evidence="ECO:0000269|PubMed:21821882,
FT ECO:0007744|PDB:3S69"
FT DISULFID 50..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:21821882, ECO:0007744|PDB:3S69"
FT DISULFID 98..256
FT /evidence="ECO:0000269|PubMed:21821882,
FT ECO:0007744|PDB:3S69"
FT DISULFID 142..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:21821882, ECO:0007744|PDB:3S69"
FT DISULFID 174..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:21821882, ECO:0007744|PDB:3S69"
FT DISULFID 200..225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:21821882, ECO:0007744|PDB:3S69"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:3S69"
FT STRAND 48..56
FT /evidence="ECO:0007829|PDB:3S69"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:3S69"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:3S69"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:3S69"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:3S69"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:3S69"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:3S69"
FT STRAND 112..118
FT /evidence="ECO:0007829|PDB:3S69"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:3S69"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:3S69"
FT STRAND 162..169
FT /evidence="ECO:0007829|PDB:3S69"
FT HELIX 171..177
FT /evidence="ECO:0007829|PDB:3S69"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:3S69"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:3S69"
FT STRAND 213..220
FT /evidence="ECO:0007829|PDB:3S69"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:3S69"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:3S69"
FT HELIX 241..249
FT /evidence="ECO:0007829|PDB:3S69"
SQ SEQUENCE 258 AA; 28172 MW; 401F9260EC46CBF2 CRC64;
MVLIRVLANL LILQLSYAQK SSELVIGGDE CNINEHRSLV AFFNSTGFFC SGTLINEEWV
LTAAHCDNTN FQMKLGVHSK KVLNEDEQTR NPKEKFICPN KKNDEVLDKD IMLIKLDSRV
SNSEHIVPLS LPSSPPSVGS VCHIMGWGSI TPIKVTYPDV PYCAYINLLD DAVCQAGYPE
LLTEYRTLCA GILEGGKDTC GGDSGGPLIC NGQFQGIVSF GAHPCGQGLK PGVYTKVFDY
NHWIQSIIAG NTTVTCPQ
