UniProt functional annotation for Q9UHI8



	UniProt functional annotation for Q9UHI8

UniProt code: Q9UHI8.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Cleaves aggrecan, a cartilage proteoglycan, at the '1938- Glu-|-Leu-1939' site (within the chondroitin sulfate attachment domain), and may be involved in its turnover (By similarity). Has angiogenic inhibitor activity. 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. {ECO:0000250, ECO:0000269|PubMed:10438512}.

Cofactor: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:17897672}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:17897672};

Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.

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

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. {ECO:0000250}.

Ptm: Glycosylated. 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}.

Sequence caution: Sequence=AAD48080.1; Type=Erroneous initiation; Evidence={ECO:0000305}; Sequence=BAA92584.1; Type=Erroneous initiation; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Cleaves aggrecan, a cartilage proteoglycan, at the '1938- Glu-\|-Leu-1939' site (within the chondroitin sulfate attachment domain), and may be involved in its turnover (By similarity). Has angiogenic inhibitor activity. 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. {ECO:0000250, ECO:0000269\|PubMed:10438512}.


Cofactor:		Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269\|PubMed:17897672}; Note=Binds 1 zinc ion per subunit. {ECO:0000269\|PubMed:17897672};
Subcellular location:		Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Domain:		The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.
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. {ECO:0000250}.
Ptm:		Glycosylated. 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}.
Sequence caution:		Sequence=AAD48080.1; Type=Erroneous initiation; Evidence={ECO:0000305}; Sequence=BAA92584.1; Type=Erroneous initiation; Evidence={ECO:0000305};