Q2LD49 · VM3TM_TRIST
- ProteinZinc metalloproteinase-disintegrin-like TSV-DM
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids621 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
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 μM | NFF-2 (fluorogenic substrates with cleavage at Ala-Nva) |
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 336 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 337 | |||||
Sequence: E | ||||||
Binding site | 340 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 346 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 406 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 409 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 411 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 413 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 416 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 419 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 470 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 471 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 473 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 484 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 485 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | plasma membrane | |
Molecular Function | metal ion binding | |
Molecular Function | metalloendopeptidase activity | |
Molecular Function | toxin activity | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameZinc metalloproteinase-disintegrin-like TSV-DM
- EC number
- Alternative names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Lepidosauria > Squamata > Bifurcata > Unidentata > Episquamata > Toxicofera > Serpentes > Colubroidea > Viperidae > Crotalinae > Trimeresurus
Accessions
- Primary accessionQ2LD49
Subcellular Location
PTM/Processing
Features
Showing features for signal, propeptide, modified residue, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MIQVLLVTICLAVFPYQGSS | ||||||
Propeptide | PRO_0000340310 | 21-191 | ||||
Sequence: IILESGNVNDYEVVYPRKVTSLPKGAVQQKYEDAMQYELKVNGEPVVLHLEKNKGLFSKDYSETHYSPDGRKITTKPPVKDHCYYHGHIQNDADSTASISACNGLKGHFKLQGEMYLIEPLKLPDSEAHAVFKYENVEKEDEAPKMCGVTETNWESDEPIKEASQSNLTPE | ||||||
Modified residue | 192 | Pyrrolidone carboxylic acid | ||||
Sequence: Q | ||||||
Chain | PRO_0000340311 | 192-621 | Zinc metalloproteinase-disintegrin-like TSV-DM | |||
Sequence: QQSYLNAPKYVKFFLVADHIMYLKYGRNLTTLRTRIFDTVNVVYLILLRINIHVLLVGMEIWSHKDKIIVQSVPAVTLKLFATWREADLLKHKSHGCAHLLTGINFNGPTAGLAYLGAICNPMYSAGIVQDHNKIHHLVAIAMAHELGHNLGINHDKDTCTCRAKACVMAGTISCDASYLFSDCSRQEHREFLIKNMPQCILKKPLKTDVVSPPVCGNYFVEVGEDCDCGSPATCRDSCCNPTNCKLRQGAQCAEGLCCDQCRFKGAGTECRPASSECDMADLCTGRSAECTDRFQRNGQPCQNNNGYCYNGTCPSMTDQCIALFGPNAAVSQDACFQFNREGNHYGYCRKEQNTKIACEPENVKCGRLYCIDSSPANKNPCNIVYLPNDEEKGMVLAGTKCADGRACNSNGQCVGVNGAYKSTTGFSQI | ||||||
Glycosylation | 219 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 311↔391 | |||||
Sequence: CNPMYSAGIVQDHNKIHHLVAIAMAHELGHNLGINHDKDTCTCRAKACVMAGTISCDASYLFSDCSRQEHREFLIKNMPQC | ||||||
Disulfide bond | 351↔375 | |||||
Sequence: CTCRAKACVMAGTISCDASYLFSDC | ||||||
Disulfide bond | 353↔358 | |||||
Sequence: CRAKAC | ||||||
Disulfide bond | 366 | Interchain (with C-366) | ||||
Sequence: C | ||||||
Disulfide bond | 407↔436 | |||||
Sequence: CGNYFVEVGEDCDCGSPATCRDSCCNPTNC | ||||||
Disulfide bond | 418↔431 | |||||
Sequence: CDCGSPATCRDSCC | ||||||
Disulfide bond | 420↔426 | |||||
Sequence: CGSPATC | ||||||
Disulfide bond | 430↔453 | |||||
Sequence: CCNPTNCKLRQGAQCAEGLCCDQC | ||||||
Disulfide bond | 444↔450 | |||||
Sequence: CAEGLCC | ||||||
Disulfide bond | 449↔475 | |||||
Sequence: CCDQCRFKGAGTECRPASSECDMADLC | ||||||
Disulfide bond | 462↔482 | |||||
Sequence: CRPASSECDMADLCTGRSAEC | ||||||
Disulfide bond | 469↔500 | |||||
Sequence: CDMADLCTGRSAECTDRFQRNGQPCQNNNGYC | ||||||
Disulfide bond | 493↔505 | |||||
Sequence: CQNNNGYCYNGTC | ||||||
Glycosylation | 502 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 512↔562 | |||||
Sequence: CIALFGPNAAVSQDACFQFNREGNHYGYCRKEQNTKIACEPENVKCGRLYC | ||||||
Disulfide bond | 527↔573 | |||||
Sequence: CFQFNREGNHYGYCRKEQNTKIACEPENVKCGRLYCIDSSPANKNPC | ||||||
Disulfide bond | 540↔550 | |||||
Sequence: CRKEQNTKIAC | ||||||
Disulfide bond | 557↔599 | |||||
Sequence: CGRLYCIDSSPANKNPCNIVYLPNDEEKGMVLAGTKCADGRAC | ||||||
Disulfide bond | 593↔605 | |||||
Sequence: CADGRACNSNGQC |
Post-translational modification
The N-terminus is blocked.
Keywords
- PTM
Expression
Tissue specificity
Expressed by the venom gland.
Interaction
Subunit
Homodimer; disulfide-linked.
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 200-396 | Peptidase M12B | ||||
Sequence: KYVKFFLVADHIMYLKYGRNLTTLRTRIFDTVNVVYLILLRINIHVLLVGMEIWSHKDKIIVQSVPAVTLKLFATWREADLLKHKSHGCAHLLTGINFNGPTAGLAYLGAICNPMYSAGIVQDHNKIHHLVAIAMAHELGHNLGINHDKDTCTCRAKACVMAGTISCDASYLFSDCSRQEHREFLIKNMPQCILKKP | ||||||
Domain | 404-489 | Disintegrin | ||||
Sequence: PPVCGNYFVEVGEDCDCGSPATCRDSCCNPTNCKLRQGAQCAEGLCCDQCRFKGAGTECRPASSECDMADLCTGRSAECTDRFQRN | ||||||
Motif | 468-470 | D/ECD-tripeptide | ||||
Sequence: ECD |
Sequence similarities
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length621
- Mass (Da)68,718
- Last updated2006-02-21 v1
- ChecksumF8C31FECC7B33F0E
Keywords
- Technical term