Q7LZ61 · VM3CX_DABSI

Function

function

Catalytic subunit of blood coagulation factor X-activating enzyme. Activates coagulation factor X (F10) by cleaving the Arg-Ile bond and is also able to activate coagulation factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-Ile and Arg-Val bonds.

Catalytic activity

  • Specifically activates several components of the blood clotting system, including coagulation factor X, coagulation factor IX and protein C by cleavage of Arg-|-Xaa bonds. Has no action on insulin B chain.
    EC:3.4.24.58 (UniProtKB | ENZYME | Rhea)

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site, active site.

161950100150200250300350400450500550600
TypeIDPosition(s)Description
Binding site333Zn2+ (UniProtKB | ChEBI); catalytic
Active site334
Binding site337Zn2+ (UniProtKB | ChEBI); catalytic
Binding site343Zn2+ (UniProtKB | ChEBI); catalytic
Binding site403Ca2+ 1 (UniProtKB | ChEBI)
Binding site406Ca2+ 1 (UniProtKB | ChEBI)
Binding site408Ca2+ 1 (UniProtKB | ChEBI)
Binding site410Ca2+ 1 (UniProtKB | ChEBI)
Binding site413Ca2+ 1 (UniProtKB | ChEBI)
Binding site416Ca2+ 1 (UniProtKB | ChEBI)
Binding site467Ca2+ 2 (UniProtKB | ChEBI)
Binding site468Ca2+ 2 (UniProtKB | ChEBI)
Binding site470Ca2+ 2 (UniProtKB | ChEBI)
Binding site482Ca2+ 2 (UniProtKB | ChEBI)
Binding site483Ca2+ 2 (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
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
    Coagulation factor X-activating enzyme heavy chain
  • EC number
  • Alternative names
    • Coagulation factor X-activating enzyme chain alpha
    • RVV-X heavy chain
    • Russellysin
    • Snake venom metalloproteinase (SVMP)

Organism names

Accessions

  • Primary accession
    Q7LZ61
  • Secondary accessions
    • B4UT23

Subcellular Location

Keywords

PTM/Processing

Features

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

TypeIDPosition(s)Description
Signal1-20
PropeptidePRO_000035522621-188
ChainPRO_0000078204189-619Coagulation factor X-activating enzyme heavy chain
Disulfide bond215↔251
Glycosylation216N-linked (GlcNAc...) (complex) asparagine
Glycosylation257N-linked (GlcNAc...) (complex) asparagine
Disulfide bond308↔388
Disulfide bond348↔372
Disulfide bond350↔355
Glycosylation351N-linked (GlcNAc...) (complex) asparagine
Glycosylation371N-linked (GlcNAc...) (complex) asparagine
Disulfide bond404↔433
Disulfide bond415↔428
Disulfide bond417↔423
Disulfide bond427↔450
Disulfide bond441↔447
Disulfide bond446↔472
Disulfide bond459↔479
Disulfide bond466↔498
Disulfide bond491↔503
Disulfide bond510↔560
Disulfide bond525↔571
Disulfide bond538↔548
Disulfide bond555↔597
Disulfide bond577Interchain (with C-158 in coagulation factor X-activating enzyme light chain LC2)
Disulfide bond591↔603

Post-translational modification

N-glycosylated; probably required for conformation. Removal of easily accessible sugars does not change its functional capacity, but removal of the core sugars with N-glycanase causes a virtually complete loss of enzyme activity, apparently as a result of major conformational changes in the molecule. Not O-glycosylated.

Keywords

PTM databases

Expression

Tissue specificity

Expressed by the venom gland.

Interaction

Subunit

Heterotrimer; disulfide-linked. The heterotrimer consists of 1 heavy chain and 2 light chains (lectins): LC1 and LC2.

Family & Domains

Features

Showing features for domain, motif.

TypeIDPosition(s)Description
Domain199-393Peptidase M12B
Domain401-487Disintegrin
Motif465-467D/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
    619
  • Mass (Da)
    69,648
  • Last updated
    2008-11-25 v2
  • Checksum
    71084A3B46338797
MMQVLLVTISLAVFPYQGSSIILESGNVNDYEVVYPQKVTALPKGAVQQPEQKYEDTMQYEFEVNGEPVVLHLEKNKILFSEDYSETHYYPDGREITTNPPVEDHCYYHGRIQNDAHSSASISACNGLKGHFKLRGEMYFIEPLKLSNSEAHAVYKYENIEKEDEIPKMCGVTQTNWESDKPIKKASQLVSTSAQFNKIFIELVIIVDHSMAKKCNSTATNTKIYEIVNSANEIFNPLNIHVTLIGVEFWCDRDLINVTSSADETLNSFGEWRASDLMTRKSHDNALLFTDMRFDLNTLGITFLAGMCQAYRSVEIVQEQGNRNFKTAVIMAHELSHNLGMYHDGKNCICNDSSCVMSPVLSDQPSKLFSNCSIHDYQRYLTRYKPKCIFNPPLRKDIVSPPVCGNEIWEEGEECDCGSPANCQNPCCDAATCKLKPGAECGNGLCCYQCKIKTAGTVCRRARDECDVPEHCTGQSAECPRDQLQQNGKPCQNNRGYCYNGDCPIMRNQCISLFGSRANVAKDSCFQENLKGSYYGYCRKENGRKIPCAPQDVKCGRLFCLNNSPRNKNPCNMHYSCMDQHKGMVDPGTKCEDGKVCNNKRQCVDVNTAYQSTTGFSQI

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict191in Ref. 3; AA sequence

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DQ137799
EMBL· GenBank· DDBJ
AAZ39881.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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