Q2LD49 · VM3TM_TRIST

Function

function

Snake venom zinc metalloprotease that hydrolyzes the alpha-chain (FGA) and more slowly the beta-chain (FGB) of fibrinogen. Inhibits cell proliferation and induces cell morphologic changes transiently on human umbilical vein endothelial cells.

Miscellaneous

Negative results: does not affect gamma-chain of fibrinogen (FGG). Does not show apoptosis effects (PubMed:16487560).

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Activity regulation

Inhibited by EDTA and DTT, and partially inhibited by EGTA, but not inhibited by PMSF and NEM.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
25 μMNFF-2 (fluorogenic substrates with cleavage at Ala-Nva)

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site336Zn2+ (UniProtKB | ChEBI); catalytic
Active site337
Binding site340Zn2+ (UniProtKB | ChEBI); catalytic
Binding site346Zn2+ (UniProtKB | ChEBI); catalytic
Binding site406Ca2+ 1 (UniProtKB | ChEBI)
Binding site409Ca2+ 1 (UniProtKB | ChEBI)
Binding site411Ca2+ 1 (UniProtKB | ChEBI)
Binding site413Ca2+ 1 (UniProtKB | ChEBI)
Binding site416Ca2+ 1 (UniProtKB | ChEBI)
Binding site419Ca2+ 1 (UniProtKB | ChEBI)
Binding site470Ca2+ 2 (UniProtKB | ChEBI)
Binding site471Ca2+ 2 (UniProtKB | ChEBI)
Binding site473Ca2+ 2 (UniProtKB | ChEBI)
Binding site484Ca2+ 2 (UniProtKB | ChEBI)
Binding site485Ca2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentextracellular region
Cellular Componentplasma membrane
Molecular Functionmetal ion binding
Molecular Functionmetalloendopeptidase activity
Molecular Functiontoxin activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Zinc metalloproteinase-disintegrin-like TSV-DM
  • EC number
  • Alternative names
    • Snake venom metalloproteinase (SVMP)

Organism names

Accessions

  • Primary accession
    Q2LD49

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, propeptide, modified residue, chain, glycosylation, disulfide bond.

TypeIDPosition(s)Description
Signal1-20
PropeptidePRO_000034031021-191
Modified residue192Pyrrolidone carboxylic acid
ChainPRO_0000340311192-621Zinc metalloproteinase-disintegrin-like TSV-DM
Glycosylation219N-linked (GlcNAc...) asparagine
Disulfide bond311↔391
Disulfide bond351↔375
Disulfide bond353↔358
Disulfide bond366Interchain (with C-366)
Disulfide bond407↔436
Disulfide bond418↔431
Disulfide bond420↔426
Disulfide bond430↔453
Disulfide bond444↔450
Disulfide bond449↔475
Disulfide bond462↔482
Disulfide bond469↔500
Disulfide bond493↔505
Glycosylation502N-linked (GlcNAc...) asparagine
Disulfide bond512↔562
Disulfide bond527↔573
Disulfide bond540↔550
Disulfide bond557↔599
Disulfide bond593↔605

Post-translational modification

The N-terminus is blocked.

Keywords

Expression

Tissue specificity

Expressed by the venom gland.

Interaction

Subunit

Homodimer; disulfide-linked.

Structure

Family & Domains

Features

Showing features for domain, motif.

TypeIDPosition(s)Description
Domain200-396Peptidase M12B
Domain404-489Disintegrin
Motif468-470D/ECD-tripeptide

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    621
  • Mass (Da)
    68,718
  • Last updated
    2006-02-21 v1
  • Checksum
    F8C31FECC7B33F0E
MIQVLLVTICLAVFPYQGSSIILESGNVNDYEVVYPRKVTSLPKGAVQQKYEDAMQYELKVNGEPVVLHLEKNKGLFSKDYSETHYSPDGRKITTKPPVKDHCYYHGHIQNDADSTASISACNGLKGHFKLQGEMYLIEPLKLPDSEAHAVFKYENVEKEDEAPKMCGVTETNWESDEPIKEASQSNLTPEQQSYLNAPKYVKFFLVADHIMYLKYGRNLTTLRTRIFDTVNVVYLILLRINIHVLLVGMEIWSHKDKIIVQSVPAVTLKLFATWREADLLKHKSHGCAHLLTGINFNGPTAGLAYLGAICNPMYSAGIVQDHNKIHHLVAIAMAHELGHNLGINHDKDTCTCRAKACVMAGTISCDASYLFSDCSRQEHREFLIKNMPQCILKKPLKTDVVSPPVCGNYFVEVGEDCDCGSPATCRDSCCNPTNCKLRQGAQCAEGLCCDQCRFKGAGTECRPASSECDMADLCTGRSAECTDRFQRNGQPCQNNNGYCYNGTCPSMTDQCIALFGPNAAVSQDACFQFNREGNHYGYCRKEQNTKIACEPENVKCGRLYCIDSSPANKNPCNIVYLPNDEEKGMVLAGTKCADGRACNSNGQCVGVNGAYKSTTGFSQI

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DQ335449
EMBL· GenBank· DDBJ
ABC73079.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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