Q196W5 · 095L_IIV3

Function

function

Probable endopeptidase.

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site, active site.

136350100150200250300350
TypeIDPosition(s)Description
Binding site119Zn2+ (UniProtKB | ChEBI); catalytic; in inhibited form
Binding site275Zn2+ (UniProtKB | ChEBI); catalytic
Active site276
Binding site279Zn2+ (UniProtKB | ChEBI); catalytic
Binding site285Zn2+ (UniProtKB | ChEBI); catalytic

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 matrix
Cellular Componentextracellular region
Molecular Functionmetalloendopeptidase activity
Molecular Functionzinc ion binding
Biological Processcollagen catabolic process
Biological Processextracellular matrix organization
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Probable matrix metalloproteinase 095L
  • EC number

Gene names

    • ORF names
      IIV3-095L

Organism names

Accessions

  • Primary accession
    Q196W5

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, propeptide, chain.

TypeIDPosition(s)Description
Signal1-25
PropeptidePRO_000037751226-126Activation peptide
ChainPRO_0000377513127-363Probable matrix metalloproteinase 095L

Keywords

PTM databases

Structure

3D structure databases

Family & Domains

Features

Showing features for motif.

TypeIDPosition(s)Description
Motif117-124Cysteine switch

Domain

The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

Sequence similarities

Belongs to the peptidase M10A family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    363
  • Mass (Da)
    40,667
  • Last updated
    2006-07-11 v1
  • Checksum
    BFE243A6AF604F1A
MSVDSFTSRLAVVMTAVVLVWWAQALPVPSPRRGESDCDAACRKFLLQYGYLDLGEENCTEVDSNRKLCSVDDELVGVPRPLARVDLAAGVSHLQTMAGLEPTGRIDASTARLFTSPRCGVPDVSKYIVAAGRRRRTRRESVIVCTTRWTTTKSNSNETLVKWWLDQSSMQWLNSTLNWVSLTNVLHHSFWKWSKESMLAFQQVSLERDAQIVVRFENGSHGDGWDFDGPGNVLAHAFQPGQSLGGDIHLDAAEPWTIYDIDGHDGNSILHVVLHEIGHALGLEHSRDPTSIMYAWYTPFKYDLGPEDVSAVAGLYGAKPASSVAAWNPKIQKFYWDRHVRNDLLPLLERDLDAEEEDSDEVR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DQ643392
EMBL· GenBank· DDBJ
ABF82125.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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