ID VSPPA_TRIST Reviewed; 258 AA.
AC Q91516;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=Venom plasminogen activator TSV-PA;
DE EC=3.4.21.-;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
DE Flags: Precursor;
OS Trimeresurus stejnegeri (Chinese green tree viper) (Viridovipera
OS stejnegeri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus.
OX NCBI_TaxID=39682;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=7730329; DOI=10.1074/jbc.270.17.10246;
RA Zhang Y., Wisner A., Xiong Y.L., Bon C.;
RT "A novel plasminogen activator from snake venom. Purification,
RT characterization, and molecular cloning.";
RL J. Biol. Chem. 270:10246-10255(1995).
RN [2]
RP MUTAGENESIS OF 104-ASP--GLU-106.
RX PubMed=9252366; DOI=10.1074/jbc.272.33.20531;
RA Zhang Y., Wisner A., Maroun R.C., Choumet V., Xiong Y., Bon C.;
RT "Trimeresurus stejnegeri snake venom plasminogen activator. Site-directed
RT mutagenesis and molecular modeling.";
RL J. Biol. Chem. 272:20531-20537(1997).
RN [3]
RP MUTAGENESIS OF ASN-44; 44-ASN--ASN-46 AND PHE-202, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=12081498; DOI=10.1021/bi016069g;
RA Braud S., Le Bonniec B.F., Bon C., Wisner A.;
RT "The stratagem utilized by the plasminogen activator from the snake
RT Trimeresurus stejnegeri to escape serpins.";
RL Biochemistry 41:8478-8484(2002).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 25-258, ACTIVE SITES, AND
RP DISULFIDE BONDS.
RX PubMed=9753698; DOI=10.1016/s0969-2126(98)00119-1;
RA Parry M.A., Jacob U., Huber R., Wisner A., Bon C., Bode W.;
RT "The crystal structure of the novel snake venom plasminogen activator TSV-
RT PA: a prototype structure for snake venom serine proteinases.";
RL Structure 6:1195-1206(1998).
CC -!- FUNCTION: Snake venom serine protease that activates plasminogen.
CC {ECO:0000269|PubMed:7730329}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=26.0 uM for S-2238 {ECO:0000269|PubMed:12081498};
CC KM=55 nM for plasminogen {ECO:0000269|PubMed:12081498};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7730329}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:7730329}.
CC -!- MISCELLANEOUS: Negative results: does not activate nor degrade
CC prothrombin (F2), factor X (F10), or protein C (PROC) and does not clot
CC fibrinogen. {ECO:0000305|PubMed:7730329}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; U21903; AAC59686.1; -; mRNA.
DR PIR; A57290; A57290.
DR PDB; 1BQY; X-ray; 2.50 A; A/B=25-258.
DR PDBsum; 1BQY; -.
DR AlphaFoldDB; Q91516; -.
DR SMR; Q91516; -.
DR MEROPS; S01.186; -.
DR SABIO-RK; Q91516; -.
DR EvolutionaryTrace; Q91516; -.
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; Trypsin-like serine proteases; 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 PANTHER; PTHR24264:SF15; RIKEN CDNA 2210010C04 GENE; 1.
DR PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Fibrinolytic toxin; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
KW Plasminogen activation; Protease; Secreted; Serine protease; Signal; Toxin;
KW Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT PROPEP 19..24
FT /id="PRO_0000028421"
FT CHAIN 25..258
FT /note="Venom plasminogen activator TSV-PA"
FT /id="PRO_0000028422"
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:9753698"
FT ACT_SITE 110
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:9753698"
FT ACT_SITE 204
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:9753698"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..163
FT /evidence="ECO:0000269|PubMed:9753698,
FT ECO:0007744|PDB:1BQY"
FT DISULFID 50..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:9753698, ECO:0007744|PDB:1BQY"
FT DISULFID 98..256
FT /evidence="ECO:0000269|PubMed:9753698,
FT ECO:0007744|PDB:1BQY"
FT DISULFID 142..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:9753698, ECO:0007744|PDB:1BQY"
FT DISULFID 174..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:9753698, ECO:0007744|PDB:1BQY"
FT DISULFID 200..225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:9753698, ECO:0007744|PDB:1BQY"
FT MUTAGEN 44..46
FT /note="NSN->AKHRRSP: Is inhibited by plasma inhibitors. Is
FT more inhibited by plasma inhibitors; when associated with
FT G-202."
FT /evidence="ECO:0000269|PubMed:12081498"
FT MUTAGEN 44
FT /note="N->AAAAGG: Is inhibited by plasma inhibitors. Is
FT more inhibited by plasma inhibitors; when associated with
FT G-202."
FT /evidence="ECO:0000269|PubMed:12081498"
FT MUTAGEN 44
FT /note="N->RRHRGG: Is inhibited by plasma inhibitors. Is
FT more inhibited by plasma inhibitors; when associated with
FT G-202."
FT /evidence="ECO:0000269|PubMed:12081498"
FT MUTAGEN 104..106
FT /note="DDE->NVI: Loss of plasminogenolytic and
FT fibrinogenolytic activities."
FT /evidence="ECO:0000269|PubMed:9252366"
FT MUTAGEN 202
FT /note="F->G: Is inhibited by plasma inhibitors. Is more
FT inhibited by plasma inhibitors; when associated with 44-N--
FT N-46 or N-44."
FT /evidence="ECO:0000269|PubMed:12081498"
FT TURN 33..38
FT /evidence="ECO:0007829|PDB:1BQY"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:1BQY"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:1BQY"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:1BQY"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:1BQY"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:1BQY"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:1BQY"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:1BQY"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:1BQY"
FT TURN 106..109
FT /evidence="ECO:0007829|PDB:1BQY"
FT STRAND 112..118
FT /evidence="ECO:0007829|PDB:1BQY"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:1BQY"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:1BQY"
FT STRAND 162..169
FT /evidence="ECO:0007829|PDB:1BQY"
FT HELIX 171..177
FT /evidence="ECO:0007829|PDB:1BQY"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:1BQY"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:1BQY"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:1BQY"
FT STRAND 213..220
FT /evidence="ECO:0007829|PDB:1BQY"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:1BQY"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:1BQY"
FT HELIX 241..249
FT /evidence="ECO:0007829|PDB:1BQY"
SQ 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
//
