P97857 · ATS1_MOUSE
- ProteinA disintegrin and metalloproteinase with thrombospondin motifs 1
- GeneAdamts1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids968 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 206 | Zn2+ (UniProtKB | ChEBI); catalytic; in inhibited form | ||||
Sequence: C | ||||||
Binding site | 262 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 262 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 345 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 345 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 352 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 402 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 403 | |||||
Sequence: E | ||||||
Binding site | 406 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 412 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 463 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 466 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 466 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | basement membrane | |
Cellular Component | cytoplasmic vesicle | |
Cellular Component | extracellular matrix | |
Cellular Component | extracellular region | |
Molecular Function | heparin binding | |
Molecular Function | metalloendopeptidase activity | |
Molecular Function | zinc ion binding | |
Biological Process | extracellular matrix organization | |
Biological Process | heart trabecula formation | |
Biological Process | kidney development | |
Biological Process | negative regulation of angiogenesis | |
Biological Process | ovulation from ovarian follicle | |
Biological Process | positive regulation of G1/S transition of mitotic cell cycle | |
Biological Process | positive regulation of vascular associated smooth muscle cell migration | |
Biological Process | positive regulation of vascular associated smooth muscle cell proliferation | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameA disintegrin and metalloproteinase with thrombospondin motifs 1
- EC number
- Short namesADAM-TS 1; ADAM-TS1; ADAMTS-1
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP97857
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 403 | Loss of activity. | ||||
Sequence: E → Q |
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.
PTM/Processing
Features
Showing features for signal, propeptide, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-48 | |||||
Sequence: MQPKVPLGSRKQKPCSDMGDVQRAARSRGSLSAHMLLLLLASITMLLC | ||||||
Propeptide | PRO_0000029152 | 49-253 | ||||
Sequence: ARGAHGRPTEEDEELVLPSLERAPGHDSTTTRLRLDAFGQQLHLKLQPDSGFLAPGFTLQTVGRSPGSEAQHLDPTGDLAHCFYSGTVNGDPGSAAALSLCEGVRGAFYLQGEEFFIQPAPGVATERLAPAVPEEESSARPQFHILRRRRRGSGGAKCGVMDDETLPTSDSRPESQNTRNQWPVRDPTPQDAGKPSGPGSIRKKR | ||||||
Chain | PRO_0000029153 | 254-968 | A disintegrin and metalloproteinase with thrombospondin motifs 1 | |||
Sequence: FVSSPRYVETMLVADQSMADFHGSGLKHYLLTLFSVAARFYKHPSIRNSISLVVVKILVIYEEQKGPEVTSNAALTLRNFCSWQKQHNSPSDRDPEHYDTAILFTRQDLCGSHTCDTLGMADVGTVCDPSRSCSVIEDDGLQAAFTTAHELGHVFNMPHDDAKHCASLNGVSGDSHLMASMLSSLDHSQPWSPCSAYMVTSFLDNGHGECLMDKPQNPIKLPSDLPGTLYDANRQCQFTFGEESKHCPDAASTCTTLWCTGTSGGLLVCQTKHFPWADGTSCGEGKWCVSGKCVNKTDMKHFATPVHGSWGPWGPWGDCSRTCGGGVQYTMRECDNPVPKNGGKYCEGKRVRYRSCNIEDCPDNNGKTFREEQCEAHNEFSKASFGNEPTVEWTPKYAGVSPKDRCKLTCEAKGIGYFFVLQPKVVDGTPCSPDSTSVCVQGQCVKAGCDRIIDSKKKFDKCGVCGGNGSTCKKMSGIVTSTRPGYHDIVTIPAGATNIEVKHRNQRGSRNNGSFLAIRAADGTYILNGNFTLSTLEQDLTYKGTVLRYSGSSAALERIRSFSPLKEPLTIQVLMVGHALRPKIKFTYFMKKKTESFNAIPTFSEWVIEEWGECSKTCGSGWQRRVVQCRDINGHPASECAKEVKPASTRPCADLPCPHWQVGDWSPCSKTCGKGYKKRTLKCVSHDGGVLSNESCDPLKKPKHYIDFCTLTQCS | ||||||
Disulfide bond | 334↔386 | |||||
Sequence: CSWQKQHNSPSDRDPEHYDTAILFTRQDLCGSHTCDTLGMADVGTVCDPSRSC | ||||||
Disulfide bond | 363↔368 | |||||
Sequence: CGSHTC | ||||||
Disulfide bond | 380↔463 | |||||
Sequence: CDPSRSCSVIEDDGLQAAFTTAHELGHVFNMPHDDAKHCASLNGVSGDSHLMASMLSSLDHSQPWSPCSAYMVTSFLDNGHGEC | ||||||
Disulfide bond | 418↔447 | |||||
Sequence: CASLNGVSGDSHLMASMLSSLDHSQPWSPC | ||||||
Disulfide bond | 489↔512 | |||||
Sequence: CQFTFGEESKHCPDAASTCTTLWC | ||||||
Disulfide bond | 500↔522 | |||||
Sequence: CPDAASTCTTLWCTGTSGGLLVC | ||||||
Disulfide bond | 507↔541 | |||||
Sequence: CTTLWCTGTSGGLLVCQTKHFPWADGTSCGEGKWC | ||||||
Disulfide bond | 535↔546 | |||||
Sequence: CGEGKWCVSGKC | ||||||
Glycosylation | 548 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 572↔609 | |||||
Sequence: CSRTCGGGVQYTMRECDNPVPKNGGKYCEGKRVRYRSC | ||||||
Disulfide bond | 576↔614 | |||||
Sequence: CGGGVQYTMRECDNPVPKNGGKYCEGKRVRYRSCNIEDC | ||||||
Disulfide bond | 587↔599 | |||||
Sequence: CDNPVPKNGGKYC | ||||||
Glycosylation | 721 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 765 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 783 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 946 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
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
- PTM
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).
Decreased levels in postnatal skeletal muscle (PubMed:23233679).
In myoblasts, up-regulated soon after induction of myoblast differentiation (PubMed:23233679).
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, motif, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-23 | Disordered | ||||
Sequence: MQPKVPLGSRKQKPCSDMGDVQR | ||||||
Region | 177-253 | Disordered | ||||
Sequence: APAVPEEESSARPQFHILRRRRRGSGGAKCGVMDDETLPTSDSRPESQNTRNQWPVRDPTPQDAGKPSGPGSIRKKR | ||||||
Motif | 204-211 | Cysteine switch | ||||
Sequence: AKCGVMDD | ||||||
Compositional bias | 218-233 | Polar residues | ||||
Sequence: DSRPESQNTRNQWPVR | ||||||
Domain | 259-468 | Peptidase M12B | ||||
Sequence: RYVETMLVADQSMADFHGSGLKHYLLTLFSVAARFYKHPSIRNSISLVVVKILVIYEEQKGPEVTSNAALTLRNFCSWQKQHNSPSDRDPEHYDTAILFTRQDLCGSHTCDTLGMADVGTVCDPSRSCSVIEDDGLQAAFTTAHELGHVFNMPHDDAKHCASLNGVSGDSHLMASMLSSLDHSQPWSPCSAYMVTSFLDNGHGECLMDKP | ||||||
Domain | 477-559 | Disintegrin | ||||
Sequence: DLPGTLYDANRQCQFTFGEESKHCPDAASTCTTLWCTGTSGGLLVCQTKHFPWADGTSCGEGKWCVSGKCVNKTDMKHFATPV | ||||||
Domain | 560-615 | TSP type-1 1 | ||||
Sequence: HGSWGPWGPWGDCSRTCGGGVQYTMRECDNPVPKNGGKYCEGKRVRYRSCNIEDCP | ||||||
Region | 726-850 | Spacer | ||||
Sequence: KKMSGIVTSTRPGYHDIVTIPAGATNIEVKHRNQRGSRNNGSFLAIRAADGTYILNGNFTLSTLEQDLTYKGTVLRYSGSSAALERIRSFSPLKEPLTIQVLMVGHALRPKIKFTYFMKKKTESF | ||||||
Domain | 855-911 | TSP type-1 2 | ||||
Sequence: TFSEWVIEEWGECSKTCGSGWQRRVVQCRDINGHPASECAKEVKPASTRPCADLPCP | ||||||
Domain | 912-968 | TSP type-1 3 | ||||
Sequence: HWQVGDWSPCSKTCGKGYKKRTLKCVSHDGGVLSNESCDPLKKPKHYIDFCTLTQCS |
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
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length968
- Mass (Da)105,801
- Last updated2011-07-27 v4
- Checksum90A44F7D5262B6C5
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E9PY08 | E9PY08_MOUSE | Adamts1 | 681 |
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 218-233 | Polar residues | ||||
Sequence: DSRPESQNTRNQWPVR | ||||||
Sequence conflict | 335 | in Ref. 1; BAA24501 and 4; AAH40382/AAH50834 | ||||
Sequence: S → N | ||||||
Sequence conflict | 425 | in Ref. 1; BAA24501 and 4; AAH40382/AAH50834 | ||||
Sequence: S → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |