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O57413 (VM2T3_PROMU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Zinc metalloproteinase/disintegrin

Cleaved into the following 2 chains:

  1. Snake venom metalloproteinase TM-3
    Short name=SVMP
    EC=3.4.24.-
    Alternative name(s):
    Fibrinlysin
    Trimutase
  2. Disintegrin trimucrin
OrganismProtobothrops mucrosquamatus (Taiwan habu) (Trimeresurus mucrosquamatus)
Taxonomic identifier103944 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeProtobothrops

Protein attributes

Sequence length481 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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). Ref.2 Ref.4

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). Ref.2 Ref.4

Cofactor

Binds 1 zinc ion per subunit By similarity.

Enzyme regulation

Inhibited by EDTA and 1,10-phenanthroline. Ref.4

Subunit structure

Monomer. Ref.4

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

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.

Sequence similarities

Belongs to the venom metalloproteinase (M12B) family. P-II subfamily. P-IIa sub-subfamily.

Contains 1 disintegrin domain.

Contains 1 peptidase M12B domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Propeptide21 – 189169
PRO_0000322612
Chain190 – 392203Snake venom metalloproteinase TM-3
PRO_5000053304
Propeptide393 – 40816 By similarity
PRO_0000322613
Chain409 – 48173Disintegrin trimucrin By similarity
PRO_0000322614

Regions

Domain197 – 392196Peptidase M12B
Domain400 – 48182Disintegrin
Motif459 – 4613Cell attachment site

Sites

Active site3341
Metal binding3331Zinc; catalytic
Metal binding3371Zinc; catalytic
Metal binding3431Zinc; catalytic

Amino acid modifications

Disulfide bond308 ↔ 387 Ref.5 Ref.6
Disulfide bond349 ↔ 371 Ref.5 Ref.6
Disulfide bond351 ↔ 354 Ref.5 Ref.6
Disulfide bond414 ↔ 429 By similarity
Disulfide bond416 ↔ 424 By similarity
Disulfide bond423 ↔ 446 By similarity
Disulfide bond437 ↔ 443 By similarity
Disulfide bond442 ↔ 467 By similarity
Disulfide bond455 ↔ 474 By similarity

Experimental info

Sequence conflict31E → Q in CAA54364. Ref.2
Sequence conflict71V → M in CAA54364. Ref.2
Sequence conflict291N → D in CAA54364. Ref.2
Sequence conflict371R → A in CAA54364. Ref.2
Sequence conflict401S → T in CAA54364. Ref.2
Sequence conflict2001K → E Ref.5
Sequence conflict2001K → E Ref.6
Sequence conflict3681F → S in CAA54364. Ref.2

Secondary structure

.................................. 481
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O57413 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: C38714924F6091DF

FASTA48154,178
        10         20         30         40         50         60 
MIEVLLVTIC LAVFPYQGSS IILESGNVND YEVVYPRKVS ALPKGAVQPK YEDAMQYEFK 

        70         80         90        100        110        120 
VNGEAVVLHL EKNKGLFSED YSETHYSPDG REITTYPSVE DHCYYHGRIH NDADSTASIS 

       130        140        150        160        170        180 
ACDGLKGYFK LQGETYPIEP LELSDSEAHA VFKYENVEKE DEAPKMCGVT QNWESDESIK 

       190        200        210        220        230        240 
KASQLYLTPE QQRFPQRYIK LAIVVDHGMY TKYSSNFKKI RKRVHQMVSN INEMCRPLNI 

       250        260        270        280        290        300 
AITLALLDVW SEKDFITVQA DAPTTAGLFG DWRERVLLKK KNHDHAQLLT DTNFARNTIG 

       310        320        330        340        350        360 
WAYVGRMCDE KYSVAVVKDH SSKVFMVAVT MTHELGHNLG MEHDDKDKCK CDTCIMSAVI 

       370        380        390        400        410        420 
SDKQSKLFSD CSKDYYQTFL TNDNPQCILN APLRTDTVST PVSGNEFLEA GEECDCGSPE 

       430        440        450        460        470        480 
NPCCDAATCK LRPGAQCAEG LCCDQCRFKK KRTICRRARG DNPDDRCTGQ SADCPRNGLY 


G 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF011909 mRNA. Translation: AAB94016.1.
X77089 mRNA. Translation: CAA54364.1.
AF519177 mRNA. Translation: AAP80728.1.
PIRS43125. S47570.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KUFX-ray1.35A190-392[»]
1KUGX-ray1.37A190-392[»]
1KUIX-ray1.50A190-392[»]
1KUKX-ray1.45A190-392[»]
ProteinModelPortalO57413.
SMRO57413. Positions 192-392, 411-476.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM12.157.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG006978.

Family and domain databases

Gene3D3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProIPR001762. Blood-coag_inhib_Disintegrin.
IPR018358. Disintegrin_CS.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view]
PfamPF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]
PRINTSPR00289. DISINTEGRIN.
SMARTSM00050. DISIN. 1 hit.
[Graphical view]
SUPFAMSSF57552. SSF57552. 1 hit.
PROSITEPS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO57413.

Entry information

Entry nameVM2T3_PROMU
AccessionPrimary (citable) accession number: O57413
Secondary accession number(s): Q7T1S1, Q91505
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references