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O57413

- VM2T3_PROMU

UniProt

O57413 - VM2T3_PROMU

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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

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).2 Publications
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).2 Publications

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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi308 ↔ 3872 Publications
Disulfide bondi349 ↔ 3712 Publications
Disulfide bondi351 ↔ 3542 Publications
Disulfide bondi414 ↔ 429 By similarity
Disulfide bondi416 ↔ 424 By similarity
Disulfide bondi423 ↔ 446 By similarity
Disulfide bondi437 ↔ 443 By similarity
Disulfide bondi442 ↔ 467 By similarity
Disulfide bondi455 ↔ 474 By 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.

Miscellaneous databases

EvolutionaryTraceiO57413.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini197 – 392196Peptidase M12BAdd
BLAST
Domaini400 – 48182DisintegrinAdd
BLAST

Motif

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

Sequence similaritiesi

Contains 1 disintegrin domain.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31E → Q in CAA54364. 1 Publication
Sequence conflicti7 – 71V → M in CAA54364. 1 Publication
Sequence conflicti29 – 291N → D in CAA54364. 1 Publication
Sequence conflicti37 – 371R → A in CAA54364. 1 Publication
Sequence conflicti40 – 401S → T in CAA54364. 1 Publication
Sequence conflicti200 – 2001K → E1 Publication
Sequence conflicti200 – 2001K → E1 Publication
Sequence conflicti368 – 3681F → S in CAA54364. 1 Publication

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: May 14, 2014
This is version 87 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

Similar proteinsi