P97857 · ATS1_MOUSE

  • Protein
    A disintegrin and metalloproteinase with thrombospondin motifs 1
  • Gene
    Adamts1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Cleaves aggrecan, a cartilage proteoglycan, at the '1691-Glu-|-Leu-1692' site (within the chondroitin sulfate attachment domain), and may be involved in its turnover. Has angiogenic inhibitor activity (By similarity).
Active metalloprotease, which may be associated with various inflammatory processes as well as development of cancer cachexia. May play a critical role in follicular rupture (By similarity).

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site, active site.

1968100200300400500600700800900
TypeIDPosition(s)Description
Binding site206Zn2+ (UniProtKB | ChEBI); catalytic; in inhibited form
Binding site262Ca2+ 1 (UniProtKB | ChEBI)
Binding site262Ca2+ 2 (UniProtKB | ChEBI)
Binding site345Ca2+ 1 (UniProtKB | ChEBI)
Binding site345Ca2+ 2 (UniProtKB | ChEBI)
Binding site352Ca2+ 1 (UniProtKB | ChEBI)
Binding site402Zn2+ (UniProtKB | ChEBI); catalytic
Active site403
Binding site406Zn2+ (UniProtKB | ChEBI); catalytic
Binding site412Zn2+ (UniProtKB | ChEBI); catalytic
Binding site463Ca2+ 1 (UniProtKB | ChEBI)
Binding site466Ca2+ 1 (UniProtKB | ChEBI)
Binding site466Ca2+ 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 Componentbasement membrane
Cellular Componentcollagen-containing extracellular matrix
Cellular Componentcytoplasmic vesicle
Cellular Componentextracellular matrix
Cellular Componentextracellular region
Molecular Functionheparin binding
Molecular Functionmetalloendopeptidase activity
Molecular Functionzinc ion binding
Biological Processextracellular matrix organization
Biological Processheart trabecula formation
Biological Processkidney development
Biological Processnegative regulation of angiogenesis
Biological Processovulation from ovarian follicle
Biological Processpositive regulation of G1/S transition of mitotic cell cycle
Biological Processpositive regulation of neuron projection development
Biological Processpositive regulation of vascular associated smooth muscle cell migration
Biological Processpositive regulation of vascular associated smooth muscle cell proliferation
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    A disintegrin and metalloproteinase with thrombospondin motifs 1
  • EC number
  • Short names
    ADAM-TS 1; ADAM-TS1; ADAMTS-1

Gene names

    • Name
      Adamts1

Organism names

  • Taxonomic identifier
  • Strains
    • 129/SvJ
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P97857
  • Secondary accessions
    • E9QMN9
    • O54768

Proteomes

Organism-specific databases

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis403Loss of activity.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 66 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

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

TypeIDPosition(s)Description
Signal1-48
PropeptidePRO_000002915249-253
ChainPRO_0000029153254-968A disintegrin and metalloproteinase with thrombospondin motifs 1
Disulfide bond334↔386
Disulfide bond363↔368
Disulfide bond380↔463
Disulfide bond418↔447
Disulfide bond489↔512
Disulfide bond500↔522
Disulfide bond507↔541
Disulfide bond535↔546
Glycosylation548N-linked (GlcNAc...) asparagine
Disulfide bond572↔609
Disulfide bond576↔614
Disulfide bond587↔599
Glycosylation721N-linked (GlcNAc...) asparagine
Glycosylation765N-linked (GlcNAc...) asparagine
Glycosylation783N-linked (GlcNAc...) asparagine
Glycosylation946N-linked (GlcNAc...) asparagine

Post-translational modification

The precursor is cleaved by a furin endopeptidase.
Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X2-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Can also be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity).

Keywords

Proteomic databases

PTM databases

Expression

Induction

Induced in vitro in colon adenocarcinoma cells by interleukin-1, or in vivo in kidney and heart by lipopolysaccharide. Also induced by LH stimulation in granulosa cells of preovulatory follicles.

Developmental stage

In embryonic skeletal muscle, significantly increased levels between 13.5 dpc and 15.5 dpc with maximal expression observed at 15.5 dpc (PubMed:23233679).
Decreased levels in postnatal skeletal muscle (PubMed:23233679).
In myoblasts, up-regulated soon after induction of myoblast differentiation (PubMed:23233679).

Gene expression databases

Interaction

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

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

TypeIDPosition(s)Description
Region1-23Disordered
Region177-253Disordered
Motif204-211Cysteine switch
Compositional bias218-233Polar residues
Domain259-468Peptidase M12B
Domain477-559Disintegrin
Domain560-615TSP type-1 1
Region726-850Spacer
Domain855-911TSP type-1 2
Domain912-968TSP type-1 3

Domain

The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.
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.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    968
  • Mass (Da)
    105,801
  • Last updated
    2011-07-27 v4
  • Checksum
    90A44F7D5262B6C5
MQPKVPLGSRKQKPCSDMGDVQRAARSRGSLSAHMLLLLLASITMLLCARGAHGRPTEEDEELVLPSLERAPGHDSTTTRLRLDAFGQQLHLKLQPDSGFLAPGFTLQTVGRSPGSEAQHLDPTGDLAHCFYSGTVNGDPGSAAALSLCEGVRGAFYLQGEEFFIQPAPGVATERLAPAVPEEESSARPQFHILRRRRRGSGGAKCGVMDDETLPTSDSRPESQNTRNQWPVRDPTPQDAGKPSGPGSIRKKRFVSSPRYVETMLVADQSMADFHGSGLKHYLLTLFSVAARFYKHPSIRNSISLVVVKILVIYEEQKGPEVTSNAALTLRNFCSWQKQHNSPSDRDPEHYDTAILFTRQDLCGSHTCDTLGMADVGTVCDPSRSCSVIEDDGLQAAFTTAHELGHVFNMPHDDAKHCASLNGVSGDSHLMASMLSSLDHSQPWSPCSAYMVTSFLDNGHGECLMDKPQNPIKLPSDLPGTLYDANRQCQFTFGEESKHCPDAASTCTTLWCTGTSGGLLVCQTKHFPWADGTSCGEGKWCVSGKCVNKTDMKHFATPVHGSWGPWGPWGDCSRTCGGGVQYTMRECDNPVPKNGGKYCEGKRVRYRSCNIEDCPDNNGKTFREEQCEAHNEFSKASFGNEPTVEWTPKYAGVSPKDRCKLTCEAKGIGYFFVLQPKVVDGTPCSPDSTSVCVQGQCVKAGCDRIIDSKKKFDKCGVCGGNGSTCKKMSGIVTSTRPGYHDIVTIPAGATNIEVKHRNQRGSRNNGSFLAIRAADGTYILNGNFTLSTLEQDLTYKGTVLRYSGSSAALERIRSFSPLKEPLTIQVLMVGHALRPKIKFTYFMKKKTESFNAIPTFSEWVIEEWGECSKTCGSGWQRRVVQCRDINGHPASECAKEVKPASTRPCADLPCPHWQVGDWSPCSKTCGKGYKKRTLKCVSHDGGVLSNESCDPLKKPKHYIDFCTLTQCS

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
E9PY08E9PY08_MOUSEAdamts1681

Sequence caution

The sequence BAA11088.1 differs from that shown. Reason: Frameshift
The sequence BAA24501.1 differs from that shown. Reason: Erroneous initiation

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias218-233Polar residues
Sequence conflict335in Ref. 1; BAA24501 and 4; AAH40382/AAH50834
Sequence conflict425in Ref. 1; BAA24501 and 4; AAH40382/AAH50834

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB001735
EMBL· GenBank· DDBJ
BAA24501.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation
D67076
EMBL· GenBank· DDBJ
BAA11088.1
EMBL· GenBank· DDBJ
mRNA Frameshift
AC126936
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC040382
EMBL· GenBank· DDBJ
AAH40382.1
EMBL· GenBank· DDBJ
mRNA
BC050834
EMBL· GenBank· DDBJ
AAH50834.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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