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Protein

Venom plasminogen activator TSV-PA

Gene
N/A
Organism
Trimeresurus stejnegeri (Chinese green tree viper) (Viridovipera stejnegeri)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Snake venom serine protease that activates plasminogen.1 Publication

Kineticsi

  1. KM=26.0 µM for S-22381 Publication
  2. KM=55 nM for plasminogen1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei65 – 651Charge relay system1 Publication
    Active sitei110 – 1101Charge relay system1 Publication
    Active sitei204 – 2041Charge relay system1 Publication

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Fibrinolytic toxin, Hemostasis impairing toxin, Hydrolase, Protease, Serine protease, Toxin

    Keywords - Biological processi

    Plasminogen activation

    Protein family/group databases

    MEROPSiS01.186.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Venom plasminogen activator TSV-PA (EC:3.4.21.-)
    Alternative name(s):
    Snake venom serine protease
    Short name:
    SVSP
    OrganismiTrimeresurus stejnegeri (Chinese green tree viper) (Viridovipera stejnegeri)
    Taxonomic identifieri39682 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeTrimeresurus

    Subcellular locationi

    • Secreted 1 Publication

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi44 – 463NSN → AKHRRSP: Is inhibited by plasma inhibitors. Is more inhibited by plasma inhibitors; when associated with G-202. 1 Publication
    Mutagenesisi44 – 441N → AAAAGG: Is inhibited by plasma inhibitors. Is more inhibited by plasma inhibitors; when associated with G-202. 1 Publication
    Mutagenesisi44 – 441N → RRHRGG: Is inhibited by plasma inhibitors. Is more inhibited by plasma inhibitors; when associated with G-202. 1 Publication
    Mutagenesisi104 – 1063DDE → NVI: Loss of plasminogenolytic and fibrinogenolytic activities. 1 Publication
    Mutagenesisi202 – 2021F → G: Is inhibited by plasma inhibitors. Is more inhibited by plasma inhibitors; when associated with 44-N--N-46 or N-44. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818By similarityAdd
    BLAST
    Propeptidei19 – 246PRO_0000028421
    Chaini25 – 258234Venom plasminogen activator TSV-PAPRO_0000028422Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi31 ↔ 163PROSITE-ProRule annotation1 Publication
    Disulfide bondi50 ↔ 66PROSITE-ProRule annotation1 Publication
    Disulfide bondi98 ↔ 256PROSITE-ProRule annotation1 Publication
    Disulfide bondi142 ↔ 210PROSITE-ProRule annotation1 Publication
    Disulfide bondi174 ↔ 189PROSITE-ProRule annotation1 Publication
    Glycosylationi185 – 1851N-linked (GlcNAc...)Sequence analysis
    Disulfide bondi200 ↔ 225PROSITE-ProRule annotation1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Expressioni

    Tissue specificityi

    Expressed by the venom gland.1 Publication

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Structurei

    Secondary structure

    1
    258
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni33 – 386Combined sources
    Beta strandi39 – 446Combined sources
    Beta strandi47 – 548Combined sources
    Beta strandi56 – 627Combined sources
    Helixi64 – 663Combined sources
    Beta strandi72 – 765Combined sources
    Beta strandi80 – 823Combined sources
    Beta strandi88 – 903Combined sources
    Beta strandi92 – 965Combined sources
    Turni106 – 1094Combined sources
    Beta strandi112 – 1187Combined sources
    Beta strandi141 – 1488Combined sources
    Beta strandi150 – 1545Combined sources
    Beta strandi162 – 1698Combined sources
    Helixi171 – 1777Combined sources
    Turni178 – 1803Combined sources
    Beta strandi185 – 1917Combined sources
    Beta strandi207 – 2104Combined sources
    Beta strandi213 – 2208Combined sources
    Beta strandi232 – 2365Combined sources
    Helixi237 – 2404Combined sources
    Helixi241 – 2499Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BQYX-ray2.50A/B25-258[»]
    ProteinModelPortaliQ91516.
    SMRiQ91516. Positions 25-258.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ91516.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 249225Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S1 family. Snake venom subfamily.PROSITE-ProRule annotation
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOVERGENiHBG013304.

    Family and domain databases

    InterProiIPR009003. Peptidase_S1_PA.
    IPR001314. Peptidase_S1A.
    IPR001254. Trypsin_dom.
    IPR018114. TRYPSIN_HIS.
    [Graphical view]
    PfamiPF00089. Trypsin. 1 hit.
    [Graphical view]
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiSM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q91516-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MELIRVLANL LILQLSYAQK SSELVFGGDE CNINEHRSLV VLFNSNGFLC
    60 70 80 90 100
    GGTLINQDWV VTAAHCDSNN FQLLFGVHSK KILNEDEQTR DPKEKFFCPN
    110 120 130 140 150
    RKKDDEVDKD IMLIKLDSSV SNSEHIAPLS LPSSPPSVGS VCRIMGWGKT
    160 170 180 190 200
    IPTKEIYPDV PHCANINILD HAVCRTAYSW RQVANTTLCA GILQGGRDTC
    210 220 230 240 250
    HFDSGGPLIC NGIFQGIVSW GGHPCGQPGE PGVYTKVFDY LDWIKSIIAG

    NKDATCPP
    Length:258
    Mass (Da):28,334
    Last modified:November 1, 1996 - v1
    Checksum:iAB1ACF6461C98A24
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U21903 mRNA. Translation: AAC59686.1.
    PIRiA57290.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U21903 mRNA. Translation: AAC59686.1.
    PIRiA57290.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BQYX-ray2.50A/B25-258[»]
    ProteinModelPortaliQ91516.
    SMRiQ91516. Positions 25-258.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    MEROPSiS01.186.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Phylogenomic databases

    HOVERGENiHBG013304.

    Miscellaneous databases

    EvolutionaryTraceiQ91516.

    Family and domain databases

    InterProiIPR009003. Peptidase_S1_PA.
    IPR001314. Peptidase_S1A.
    IPR001254. Trypsin_dom.
    IPR018114. TRYPSIN_HIS.
    [Graphical view]
    PfamiPF00089. Trypsin. 1 hit.
    [Graphical view]
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiSM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "A novel plasminogen activator from snake venom. Purification, characterization, and molecular cloning."
      Zhang Y., Wisner A., Xiong Y.L., Bon C.
      J. Biol. Chem. 270:10246-10255(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Venom and Venom gland.
    2. "Trimeresurus stejnegeri snake venom plasminogen activator. Site-directed mutagenesis and molecular modeling."
      Zhang Y., Wisner A., Maroun R.C., Choumet V., Xiong Y., Bon C.
      J. Biol. Chem. 272:20531-20537(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF 104-ASP--GLU-106.
    3. "The stratagem utilized by the plasminogen activator from the snake Trimeresurus stejnegeri to escape serpins."
      Braud S., Le Bonniec B.F., Bon C., Wisner A.
      Biochemistry 41:8478-8484(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASN-44; 44-ASN--ASN-46 AND PHE-202, BIOPHYSICOCHEMICAL PROPERTIES.
    4. "The crystal structure of the novel snake venom plasminogen activator TSV-PA: a prototype structure for snake venom serine proteinases."
      Parry M.A., Jacob U., Huber R., Wisner A., Bon C., Bode W.
      Structure 6:1195-1206(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 25-258, ACTIVE SITES, DISULFIDE BONDS.

    Entry informationi

    Entry nameiVSPPA_TRIST
    AccessioniPrimary (citable) accession number: Q91516
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 4, 2001
    Last sequence update: November 1, 1996
    Last modified: March 16, 2016
    This is version 93 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    Annotation programAnimal Toxin Annotation Program

    Miscellaneousi

    Miscellaneous

    Does not activate nor degrade prothrombin (F2), factor X (F10), or protein C (PROC) and does not clot fibrinogen.1 Publication

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.