Q499S5 · MMP11_RAT

Function

function

May play an important role in the progression of epithelial malignancies.

Cofactor

Protein has several cofactor binding sites:
Ca2+ (UniProtKB | Rhea| CHEBI:29108 )
Note: Binds 1 Ca2+ ion per subunit.
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )
Note: Binds 2 Zn2+ ions per subunit.

Features

Showing features for binding site, active site.

149150100150200250300350400450
TypeIDPosition(s)Description
Binding site84Zn2+ 2 (UniProtKB | ChEBI); catalytic; in inhibited form
Binding site168Zn2+ 1 (UniProtKB | ChEBI)
Binding site170Zn2+ 1 (UniProtKB | ChEBI)
Binding site175Ca2+ (UniProtKB | ChEBI)
Binding site176Ca2+ (UniProtKB | ChEBI)
Binding site178Ca2+ (UniProtKB | ChEBI)
Binding site180Ca2+ (UniProtKB | ChEBI)
Binding site183Zn2+ 1 (UniProtKB | ChEBI)
Binding site196Zn2+ 1 (UniProtKB | ChEBI)
Binding site218Zn2+ 2 (UniProtKB | ChEBI); catalytic
Active site219
Binding site222Zn2+ 2 (UniProtKB | ChEBI); catalytic
Binding site228Zn2+ 2 (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 space
Molecular Functionmetalloendopeptidase activity
Molecular Functionmetallopeptidase activity
Molecular Functionzinc ion binding
Biological Processbasement membrane organization
Biological Processcollagen catabolic process
Biological Processcollagen fibril organization
Biological Processextracellular matrix organization
Biological Processnegative regulation of fat cell differentiation
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Stromelysin-3
  • EC number
  • Short names
    SL-3; ST3
  • Alternative names
    • Matrix metalloproteinase-11 (MMP-11)

Gene names

    • Name
      Mmp11

Organism names

  • Taxonomic identifier
  • Strain
    • Wistar
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    Q499S5
  • Secondary accessions
    • P97568

Proteomes

Organism-specific databases

PTM/Processing

Features

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

TypeIDPosition(s)Description
Signal1-35
PropeptidePRO_000004264936-101Activation peptide
ChainPRO_0000042650102-491Stromelysin-3
Disulfide bond297↔483

Post-translational modification

The precursor is cleaved by a furin endopeptidase.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Highly expressed in ovary and uterus.

Induction

In skin fibroblasts of superficial dermis upon skin lesion with highest level between days 5-10.

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for motif, region, compositional bias, repeat.

TypeIDPosition(s)Description
Motif82-89Cysteine switch
Region260-279Disordered
Compositional bias262-279Polar residues
Repeat298-342Hemopexin 1
Repeat343-385Hemopexin 2
Repeat387-435Hemopexin 3
Repeat436-483Hemopexin 4

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
    491
  • Mass (Da)
    55,511
  • Last updated
    2005-09-13 v1
  • Checksum
    B0C5B191A623FD41
MARAACLLRAISRALLLPLPLLLLLLLLLPPQLMARARPPENHRHRPVKRVPQLLPAALPNSLPSVPASHWVPGPASSSRPLRCGVPDPPDVLNARNRQKRFVLSGGRWEKTDLTYRILRFPWQLVREQVRQTVAEALRVWSEVTPLTFTEVHEGRADIMIDFTRYWHGDNLPFDGPGGILAHAFFPKTHREGDVHFDYDETWTIGDKGTDLLQVAAHEFGHVLGLQHTTAAKALMSPFYTFRYPLSLSPDDRRGIQHLYGRPQLTPTSPTPTLSSQAGTDTNEIALQEPEVPPEVCETSFDAVSTIRGELFFFKAGFVWRLRSGQLQPGYPALASRHWQGLPSPVDAAFEDAQGQIWFFQGAQYWVYDGEKPVLGPAPLSKLGLQGSPVHAALVWGPEKNKIYFFRGGDYWRFHPRTQRVDNPVPRRTTDWRGVPSEIDAAFQDAEGYAYFLRGHLYWKFDPVKVKVLESFPRPIGPDFFDCAEPANTFR

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A8L2R8J4A0A8L2R8J4_RATMmp11488

Sequence caution

The sequence AAC53061.1 differs from that shown. Reason: Erroneous initiation
The sequence AAH99781.2 differs from that shown. Reason: Erroneous initiation

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias262-279Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U46034
EMBL· GenBank· DDBJ
AAC53061.1
EMBL· GenBank· DDBJ
mRNA Different initiation
BC099781
EMBL· GenBank· DDBJ
AAH99781.2
EMBL· GenBank· DDBJ
mRNA Different initiation

Genome annotation databases

Similar Proteins

Disclaimer

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