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MGP004449

UniProt Annotations

Entry Information
Gene NameADAM metallopeptidase with thrombospondin type 1 motif, 5
Protein EntryATS5_HUMAN
UniProt IDQ9UNA0
SpeciesHuman
Comments
Comment typeDescription
Catalytic ActivityCleaves aggrecan at the 392-Glu-|-Ala-393 site.
CofactorName=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:18042673}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:18042673};
DomainThe 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.
DomainThe spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.
FunctionCleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover. May play an important role in the destruction of aggrecan in arthritic diseases. May play a role in proteolytic processing mostly during the peri-implantation period.
InteractionP13608:ACAN (xeno); NbExp=2; IntAct=EBI-2808663, EBI-6259246;
PtmC- and O-glycosylated. O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)- (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 can mediate the efficient secretion of ADAMTS family members. Can 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). {ECO:0000250}.
PtmGlycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)- (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. Also can 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). {ECO:0000250}.
PtmThe precursor is cleaved by a furin endopeptidase. {ECO:0000250}.
SimilarityContains 1 disintegrin domain. {ECO:0000305}.
SimilarityContains 1 peptidase M12B domain. {ECO:0000255|PROSITE-ProRule:PRU00276}.
SimilarityContains 2 TSP type-1 domains. {ECO:0000255|PROSITE- ProRule:PRU00210}.
Subcellular LocationSecreted, extracellular space, extracellular matrix {ECO:0000250}.
Tissue SpecificityExpressed at low level in placenta primarily but also detected in heart and brain, cervix, uterus, bladder, esophagus, rib cartilage, chondroblastoma, fibrous tissue and a joint capsule from an arthritic patient.
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