Mouse Gene Adamts4 (ENSMUST00000111315.8) from GENCODE VM23 Comprehensive Transcript Set (only Basic displayed by default)
Description: Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover. May play an important role in the destruction of aggrecan in arthritic diseases. Cleaves aggrecan at the '392-Glu-|-Ala-393' site (By similarity). (from UniProt Q8BNJ2) RefSeq Summary (NM_172845): This gene encodes a member of 'a disintegrin and metalloproteinase with thrombospondin motifs' (ADAMTS) family of multi-domain matrix-associated metalloendopeptidases that have diverse roles in tissue morphogenesis and pathophysiological remodeling, in inflammation and in vascular biology. The encoded preproprotein undergoes proteolytic processing to generate an active zinc-dependent aggrecanase enzyme that degrades cartilage. [provided by RefSeq, Jul 2016]. Sequence Note: The RefSeq transcript and protein were derived from genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments. Gencode Transcript: ENSMUST00000111315.8 Gencode Gene: ENSMUSG00000006403.13 Transcript (Including UTRs) Position: mm10 chr1:171,250,421-171,260,637 Size: 10,217 Total Exon Count: 9 Strand: + Coding Region Position: mm10 chr1:171,250,849-171,259,178 Size: 8,330 Coding Exon Count: 9
ID:ATS4_MOUSE DESCRIPTION: RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 4; Short=ADAM-TS 4; Short=ADAM-TS4; Short=ADAMTS-4; EC=3.4.24.82; AltName: Full=Aggrecanase-1; Flags: Precursor; FUNCTION: Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover. May play an important role in the destruction of aggrecan in arthritic diseases. Cleaves aggrecan at the '392-Glu-|-Ala-393' site (By similarity). CATALYTIC ACTIVITY: Glutamyl endopeptidase; bonds cleaved include 370-Thr-Glu-Gly-Glu-|-Ala-Arg-Gly-Ser-377 in the interglobular domain of mammalian aggrecan. COFACTOR: Binds 1 zinc ion per subunit (By similarity). SUBUNIT: Interacts with SRPX2 (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix (By similarity). DOMAIN: The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix (By similarity). 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. PTM: The precursor is cleaved by a furin endopeptidase (By similarity). SIMILARITY: Contains 1 disintegrin domain. SIMILARITY: Contains 1 peptidase M12B domain. SIMILARITY: Contains 1 TSP type-1 domain. SEQUENCE CAUTION: Sequence=BAC38944.1; Type=Erroneous initiation;
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q8BNJ2
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Protein Q8BNJ2 (Reactome details) participates in the following event(s):
R-MMU-5173005 B3GALTL transfers glucose to O-fucosyl-proteins R-MMU-5173192 POFUT2 transfers fucose to TSR domain-containing proteins R-MMU-3788075 Brevican degradation by ADAMTS4, ADAMTS5 R-MMU-5173214 O-glycosylation of TSR domain-containing proteins R-MMU-1474228 Degradation of the extracellular matrix R-MMU-5173105 O-linked glycosylation R-MMU-1474244 Extracellular matrix organization R-MMU-597592 Post-translational protein modification R-MMU-392499 Metabolism of proteins