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O57413

- VM2T3_PROMU

UniProt

O57413 - VM2T3_PROMU

Protein

Zinc metalloproteinase/disintegrin

Gene
N/A
Organism
Protobothrops mucrosquamatus (Taiwan habu) (Trimeresurus mucrosquamatus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
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    Functioni

    Snake venom metalloproteinase TM-3: fibrin(ogen)olytic protease which cleaves the Aalpha chain of fibrinogen (FGA) first followed by the Bbeta chain (FGB) and shows relatively low activity on the gamma chain (FGG).
    Disintegrin trimucrin: inhibits platelet aggregation induced by ADP, thrombin, platelet-activating factor and collagen. Acts by inhibiting fibrinogen interaction with platelet receptors GPIIb/GPIIIa (ITGA2B/ITGB3).

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Enzyme regulationi

    Inhibited by EDTA and 1,10-phenanthroline.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi333 – 3331Zinc; catalytic
    Active sitei334 – 3341
    Metal bindingi337 – 3371Zinc; catalytic
    Metal bindingi343 – 3431Zinc; catalytic

    GO - Molecular functioni

    1. metalloendopeptidase activity Source: InterPro
    2. zinc ion binding Source: InterPro

    Keywords - Molecular functioni

    Cell adhesion impairing toxin, Fibrinogenolytic toxin, Fibrinolytic toxin, Hemostasis impairing toxin, Hydrolase, Metalloprotease, Platelet aggregation inhibiting toxin, Protease, Toxin

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM12.157.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Zinc metalloproteinase/disintegrin
    Cleaved into the following 2 chains:
    Alternative name(s):
    Fibrinlysin
    Trimutase
    OrganismiProtobothrops mucrosquamatus (Taiwan habu) (Trimeresurus mucrosquamatus)
    Taxonomic identifieri103944 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeProtobothrops

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Propeptidei21 – 189169PRO_0000322612Add
    BLAST
    Chaini190 – 392203Snake venom metalloproteinase TM-3PRO_5000053304Add
    BLAST
    Propeptidei393 – 40816By similarityPRO_0000322613Add
    BLAST
    Chaini409 – 48173Disintegrin trimucrinBy similarityPRO_0000322614Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi308 ↔ 387
    Disulfide bondi349 ↔ 371
    Disulfide bondi351 ↔ 354
    Disulfide bondi414 ↔ 429By similarity
    Disulfide bondi416 ↔ 424By similarity
    Disulfide bondi423 ↔ 446By similarity
    Disulfide bondi437 ↔ 443By similarity
    Disulfide bondi442 ↔ 467By similarity
    Disulfide bondi455 ↔ 474By similarity

    Keywords - PTMi

    Disulfide bond, Zymogen

    Expressioni

    Tissue specificityi

    Expressed by the venom gland.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    Secondary structure

    1
    481
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi197 – 2059
    Helixi207 – 2126
    Turni213 – 2153
    Helixi217 – 23519
    Helixi236 – 2383
    Beta strandi240 – 24910
    Helixi262 – 27514
    Helixi277 – 2804
    Beta strandi284 – 2907
    Helixi295 – 2973
    Beta strandi300 – 3023
    Turni310 – 3123
    Beta strandi313 – 3186
    Helixi324 – 33815
    Turni346 – 3483
    Beta strandi352 – 3543
    Helixi370 – 38213
    Helixi386 – 3894

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KUFX-ray1.35A190-392[»]
    1KUGX-ray1.37A190-392[»]
    1KUIX-ray1.50A190-392[»]
    1KUKX-ray1.45A190-392[»]
    ProteinModelPortaliO57413.
    SMRiO57413. Positions 192-392, 411-476.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO57413.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini197 – 392196Peptidase M12BPROSITE-ProRule annotationAdd
    BLAST
    Domaini400 – 48182DisintegrinPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi459 – 4613Cell attachment site

    Sequence similaritiesi

    Contains 1 disintegrin domain.PROSITE-ProRule annotation
    Contains 1 peptidase M12B domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOVERGENiHBG006978.

    Family and domain databases

    Gene3Di3.40.390.10. 1 hit.
    4.10.70.10. 1 hit.
    InterProiIPR001762. Blood-coag_inhib_Disintegrin.
    IPR018358. Disintegrin_CS.
    IPR024079. MetalloPept_cat_dom.
    IPR001590. Peptidase_M12B.
    IPR002870. Peptidase_M12B_N.
    [Graphical view]
    PfamiPF00200. Disintegrin. 1 hit.
    PF01562. Pep_M12B_propep. 1 hit.
    PF01421. Reprolysin. 1 hit.
    [Graphical view]
    PRINTSiPR00289. DISINTEGRIN.
    SMARTiSM00050. DISIN. 1 hit.
    [Graphical view]
    SUPFAMiSSF57552. SSF57552. 1 hit.
    PROSITEiPS50215. ADAM_MEPRO. 1 hit.
    PS00427. DISINTEGRIN_1. 1 hit.
    PS50214. DISINTEGRIN_2. 1 hit.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    O57413-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIEVLLVTIC LAVFPYQGSS IILESGNVND YEVVYPRKVS ALPKGAVQPK    50
    YEDAMQYEFK VNGEAVVLHL EKNKGLFSED YSETHYSPDG REITTYPSVE 100
    DHCYYHGRIH NDADSTASIS ACDGLKGYFK LQGETYPIEP LELSDSEAHA 150
    VFKYENVEKE DEAPKMCGVT QNWESDESIK KASQLYLTPE QQRFPQRYIK 200
    LAIVVDHGMY TKYSSNFKKI RKRVHQMVSN INEMCRPLNI AITLALLDVW 250
    SEKDFITVQA DAPTTAGLFG DWRERVLLKK KNHDHAQLLT DTNFARNTIG 300
    WAYVGRMCDE KYSVAVVKDH SSKVFMVAVT MTHELGHNLG MEHDDKDKCK 350
    CDTCIMSAVI SDKQSKLFSD CSKDYYQTFL TNDNPQCILN APLRTDTVST 400
    PVSGNEFLEA GEECDCGSPE NPCCDAATCK LRPGAQCAEG LCCDQCRFKK 450
    KRTICRRARG DNPDDRCTGQ SADCPRNGLY G 481
    Length:481
    Mass (Da):54,178
    Last modified:June 1, 1998 - v1
    Checksum:iC38714924F6091DF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31E → Q in CAA54364. (PubMed:8068721)Curated
    Sequence conflicti7 – 71V → M in CAA54364. (PubMed:8068721)Curated
    Sequence conflicti29 – 291N → D in CAA54364. (PubMed:8068721)Curated
    Sequence conflicti37 – 371R → A in CAA54364. (PubMed:8068721)Curated
    Sequence conflicti40 – 401S → T in CAA54364. (PubMed:8068721)Curated
    Sequence conflicti200 – 2001K → E(PubMed:12077431)Curated
    Sequence conflicti200 – 2001K → E(PubMed:12071970)Curated
    Sequence conflicti368 – 3681F → S in CAA54364. (PubMed:8068721)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF011909 mRNA. Translation: AAB94016.1.
    X77089 mRNA. Translation: CAA54364.1.
    AF519177 mRNA. Translation: AAP80728.1.
    PIRiS47570. S43125.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF011909 mRNA. Translation: AAB94016.1 .
    X77089 mRNA. Translation: CAA54364.1 .
    AF519177 mRNA. Translation: AAP80728.1 .
    PIRi S47570. S43125.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KUF X-ray 1.35 A 190-392 [» ]
    1KUG X-ray 1.37 A 190-392 [» ]
    1KUI X-ray 1.50 A 190-392 [» ]
    1KUK X-ray 1.45 A 190-392 [» ]
    ProteinModelPortali O57413.
    SMRi O57413. Positions 192-392, 411-476.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi M12.157.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG006978.

    Miscellaneous databases

    EvolutionaryTracei O57413.

    Family and domain databases

    Gene3Di 3.40.390.10. 1 hit.
    4.10.70.10. 1 hit.
    InterProi IPR001762. Blood-coag_inhib_Disintegrin.
    IPR018358. Disintegrin_CS.
    IPR024079. MetalloPept_cat_dom.
    IPR001590. Peptidase_M12B.
    IPR002870. Peptidase_M12B_N.
    [Graphical view ]
    Pfami PF00200. Disintegrin. 1 hit.
    PF01562. Pep_M12B_propep. 1 hit.
    PF01421. Reprolysin. 1 hit.
    [Graphical view ]
    PRINTSi PR00289. DISINTEGRIN.
    SMARTi SM00050. DISIN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57552. SSF57552. 1 hit.
    PROSITEi PS50215. ADAM_MEPRO. 1 hit.
    PS00427. DISINTEGRIN_1. 1 hit.
    PS50214. DISINTEGRIN_2. 1 hit.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of a trimutase gene from Taiwan habu (Trimeresurus mucrosquamatus)."
      Guo Y., Chang T., Lai C.
      Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Venom gland.
    2. "Characterization of a cDNA encoding the precursor of platelet aggregation inhibition and metalloproteinase from Trimeresurus mucrosquamatus venom."
      Tsai I.H., Wang Y.M., Lee Y.H.
      Biochim. Biophys. Acta 1200:337-340(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
      Tissue: Venom gland.
    3. "Cloning and functional expression of a non-hemorrhagic thrombolytic enzyme from Taiwan habu."
      Guo Y.-W., Ho P.-H.
      Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 190-392.
    4. "Characterization of three fibrinogenolytic proteases isolated from the venom of Taiwan habu (Trimeresurus mucrosquamatus)."
      Huang K.-F., Hung C.C., Chiou S.-H.
      Biochem. Mol. Biol. Int. 31:1041-1050(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, SUBUNIT.
      Tissue: Venom.
    5. "The 1.35 A structure of cadmium-substituted TM-3, a snake-venom metalloproteinase from Taiwan habu: elucidation of a TNFalpha-converting enzyme-like active-site structure with a distorted octahedral geometry of cadmium."
      Huang K.-F., Chiou S.-H., Ko T.-P., Yuann J.M., Wang A.H.-J.
      Acta Crystallogr. D 58:1118-1128(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 190-392, METAL-BINDING SITES, DISULFIDE BONDS.
    6. "Determinants of the inhibition of a Taiwan habu venom metalloproteinase by its endogenous inhibitors revealed by X-ray crystallography and synthetic inhibitor analogues."
      Huang K.-F., Chiou S.-H., Ko T.-P., Wang A.H.-J.
      Eur. J. Biochem. 269:3047-3056(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.37 ANGSTROMS) OF 190-392, METAL-BINDING SITES, DISULFIDE BONDS.

    Entry informationi

    Entry nameiVM2T3_PROMU
    AccessioniPrimary (citable) accession number: O57413
    Secondary accession number(s): Q7T1S1, Q91505
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 26, 2008
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 88 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programAnimal Toxin Annotation Program
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    This disintegrin is 100% identical to the disintegrin of AC E9NW27, another disintegrin of the P-II subfamily of Protobothrops mucrosquamatus.
    The disintegrin belongs to the medium disintegrin subfamily.

    Keywords - Technical termi

    3D-structure

    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

    External Data

    Dasty 3