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Venom plasminogen activator TSV-PA (EC 3.4.21.-) (Snake venom serine protease) (SVSP)

 VSPPA_TRIST             Reviewed;         258 AA.
Q91516;
04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
10-MAY-2017, entry version 98.
RecName: Full=Venom plasminogen activator TSV-PA;
EC=3.4.21.-;
AltName: Full=Snake venom serine protease;
Short=SVSP;
Flags: Precursor;
Trimeresurus stejnegeri (Chinese green tree viper) (Viridovipera
stejnegeri).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae;
Trimeresurus.
NCBI_TaxID=39682;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Venom, and Venom gland;
PubMed=7730329; DOI=10.1074/jbc.270.17.9813;
Zhang Y., Wisner A., Xiong Y.L., Bon C.;
"A novel plasminogen activator from snake venom. Purification,
characterization, and molecular cloning.";
J. Biol. Chem. 270:10246-10255(1995).
[2]
MUTAGENESIS OF 104-ASP--GLU-106.
PubMed=9252366; DOI=10.1074/jbc.272.33.20531;
Zhang Y., Wisner A., Maroun R.C., Choumet V., Xiong Y., Bon C.;
"Trimeresurus stejnegeri snake venom plasminogen activator. Site-
directed mutagenesis and molecular modeling.";
J. Biol. Chem. 272:20531-20537(1997).
[3]
MUTAGENESIS OF ASN-44; 44-ASN--ASN-46 AND PHE-202, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=12081498; DOI=10.1021/bi016069g;
Braud S., Le Bonniec B.F., Bon C., Wisner A.;
"The stratagem utilized by the plasminogen activator from the snake
Trimeresurus stejnegeri to escape serpins.";
Biochemistry 41:8478-8484(2002).
[4]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 25-258, ACTIVE SITES, AND
DISULFIDE BONDS.
PubMed=9753698; DOI=10.1016/S0969-2126(98)00119-1;
Parry M.A., Jacob U., Huber R., Wisner A., Bon C., Bode W.;
"The crystal structure of the novel snake venom plasminogen activator
TSV-PA: a prototype structure for snake venom serine proteinases.";
Structure 6:1195-1206(1998).
-!- FUNCTION: Snake venom serine protease that activates plasminogen.
{ECO:0000269|PubMed:7730329}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=26.0 uM for S-2238 {ECO:0000269|PubMed:12081498};
KM=55 nM for plasminogen {ECO:0000269|PubMed:12081498};
-!- SUBUNIT: Monomer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7730329}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
{ECO:0000269|PubMed:7730329}.
-!- MISCELLANEOUS: Does not activate nor degrade prothrombin (F2),
factor X (F10), or protein C (PROC) and does not clot fibrinogen.
{ECO:0000305|PubMed:7730329}.
-!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
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EMBL; U21903; AAC59686.1; -; mRNA.
PIR; A57290; A57290.
PDB; 1BQY; X-ray; 2.50 A; A/B=25-258.
PDBsum; 1BQY; -.
ProteinModelPortal; Q91516; -.
SMR; Q91516; -.
MEROPS; S01.186; -.
HOVERGEN; HBG013304; -.
EvolutionaryTrace; Q91516; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Disulfide bond;
Fibrinolytic toxin; Glycoprotein; Hemostasis impairing toxin;
Hydrolase; Plasminogen activation; Protease; Secreted;
Serine protease; Signal; Toxin; Zymogen.
SIGNAL 1 18 {ECO:0000250}.
PROPEP 19 24
/FTId=PRO_0000028421.
CHAIN 25 258 Venom plasminogen activator TSV-PA.
/FTId=PRO_0000028422.
DOMAIN 25 249 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 65 65 Charge relay system.
{ECO:0000269|PubMed:9753698}.
ACT_SITE 110 110 Charge relay system.
{ECO:0000269|PubMed:9753698}.
ACT_SITE 204 204 Charge relay system.
{ECO:0000269|PubMed:9753698}.
CARBOHYD 185 185 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 31 163 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:9753698}.
DISULFID 50 66 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:9753698}.
DISULFID 98 256 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:9753698}.
DISULFID 142 210 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:9753698}.
DISULFID 174 189 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:9753698}.
DISULFID 200 225 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:9753698}.
MUTAGEN 44 46 NSN->AKHRRSP: Is inhibited by plasma
inhibitors. Is more inhibited by plasma
inhibitors; when associated with G-202.
{ECO:0000269|PubMed:12081498}.
MUTAGEN 44 44 N->AAAAGG: Is inhibited by plasma
inhibitors. Is more inhibited by plasma
inhibitors; when associated with G-202.
{ECO:0000269|PubMed:12081498}.
MUTAGEN 44 44 N->RRHRGG: Is inhibited by plasma
inhibitors. Is more inhibited by plasma
inhibitors; when associated with G-202.
{ECO:0000269|PubMed:12081498}.
MUTAGEN 104 106 DDE->NVI: Loss of plasminogenolytic and
fibrinogenolytic activities.
{ECO:0000269|PubMed:9252366}.
MUTAGEN 202 202 F->G: Is inhibited by plasma inhibitors.
Is more inhibited by plasma inhibitors;
when associated with 44-N--N-46 or N-44.
{ECO:0000269|PubMed:12081498}.
TURN 33 38 {ECO:0000244|PDB:1BQY}.
STRAND 39 44 {ECO:0000244|PDB:1BQY}.
STRAND 47 54 {ECO:0000244|PDB:1BQY}.
STRAND 56 62 {ECO:0000244|PDB:1BQY}.
HELIX 64 66 {ECO:0000244|PDB:1BQY}.
STRAND 72 76 {ECO:0000244|PDB:1BQY}.
STRAND 80 82 {ECO:0000244|PDB:1BQY}.
STRAND 88 90 {ECO:0000244|PDB:1BQY}.
STRAND 92 96 {ECO:0000244|PDB:1BQY}.
TURN 106 109 {ECO:0000244|PDB:1BQY}.
STRAND 112 118 {ECO:0000244|PDB:1BQY}.
STRAND 141 148 {ECO:0000244|PDB:1BQY}.
STRAND 150 154 {ECO:0000244|PDB:1BQY}.
STRAND 162 169 {ECO:0000244|PDB:1BQY}.
HELIX 171 177 {ECO:0000244|PDB:1BQY}.
TURN 178 180 {ECO:0000244|PDB:1BQY}.
STRAND 185 191 {ECO:0000244|PDB:1BQY}.
STRAND 207 210 {ECO:0000244|PDB:1BQY}.
STRAND 213 220 {ECO:0000244|PDB:1BQY}.
STRAND 232 236 {ECO:0000244|PDB:1BQY}.
HELIX 237 240 {ECO:0000244|PDB:1BQY}.
HELIX 241 249 {ECO:0000244|PDB:1BQY}.
SEQUENCE 258 AA; 28334 MW; AB1ACF6461C98A24 CRC64;
MELIRVLANL LILQLSYAQK SSELVFGGDE CNINEHRSLV VLFNSNGFLC GGTLINQDWV
VTAAHCDSNN FQLLFGVHSK KILNEDEQTR DPKEKFFCPN RKKDDEVDKD IMLIKLDSSV
SNSEHIAPLS LPSSPPSVGS VCRIMGWGKT IPTKEIYPDV PHCANINILD HAVCRTAYSW
RQVANTTLCA GILQGGRDTC HFDSGGPLIC NGIFQGIVSW GGHPCGQPGE PGVYTKVFDY
LDWIKSIIAG NKDATCPP


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