P59384 · ATS15_MOUSE

  • Protein
    A disintegrin and metalloproteinase with thrombospondin motifs 15
  • Gene
    Adamts15
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Metalloprotease which has proteolytic activity against the proteoglycan VCAN, cleaving it at the 'Glu-1401-|-1402-Ala' site (PubMed:24220035).
Cleaves VCAN in the pericellular matrix surrounding myoblasts, facilitating myoblast contact and fusion which is required for skeletal muscle development and regeneration (PubMed:23233679).

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site, site, active site.

1950100200300400500600700800900
TypeIDPosition(s)Description
Binding site174Zn2+ (UniProtKB | ChEBI); catalytic; in inhibited form
Site212-213Cleavage; by furin
Binding site361Zn2+ (UniProtKB | ChEBI); catalytic
Active site362
Binding site365Zn2+ (UniProtKB | ChEBI); catalytic
Binding site371Zn2+ (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
Cellular Componentcell surface
Cellular Componentcollagen-containing extracellular matrix
Cellular Componentextracellular matrix
Cellular Componentextracellular space
Molecular Functionendopeptidase activity
Molecular Functionextracellular matrix binding
Molecular Functionheparin binding
Molecular Functionmetalloendopeptidase activity
Molecular Functionzinc ion binding
Biological Processextracellular matrix disassembly
Biological Processextracellular matrix organization
Biological Processmyoblast fusion
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    A disintegrin and metalloproteinase with thrombospondin motifs 15
  • EC number
  • Short names
    ADAM-TS 15; ADAM-TS15; ADAMTS-15

Gene names

    • Name
      Adamts15

Organism names

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

Accessions

  • Primary accession
    P59384
  • Secondary accessions
    • Q504Z2
    • Q91Z56

Proteomes

Organism-specific databases

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis141Reduced glycosylation.
Mutagenesis212Reduced propeptide cleavage.

Variants

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

The viewer provides 41 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

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

TypeIDPosition(s)Description
Signal1-18
PropeptidePRO_000027078719-212
Glycosylation141N-linked (GlcNAc...) asparagine
ChainPRO_0000078212213-950A disintegrin and metalloproteinase with thrombospondin motifs 15
Disulfide bond293↔345
Disulfide bond322↔327
Disulfide bond339↔422
Disulfide bond377↔406
Disulfide bond448↔470
Disulfide bond459↔480
Disulfide bond465↔499
Disulfide bond493↔504
Disulfide bond528↔565
Disulfide bond532↔570
Disulfide bond543↔555
Glycosylation591N-linked (GlcNAc...) asparagine
Glycosylation623N-linked (GlcNAc...) asparagine
Glycosylation679N-linked (GlcNAc...) asparagine

Post-translational modification

The precursor is cleaved by a furin endopeptidase.
Glycosylated (PubMed:24220035).
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 (By similarity).
Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL (By similarity).
Fucosylation mediates the efficient secretion of ADAMTS family members (By similarity).
Can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs (By similarity).
Also N-glycosylated (PubMed:24220035).
These other glycosylations can also facilitate secretion (By similarity).

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

In the adult colon, highly expressed in the muscularis externa (inner circular smooth muscle and outer longitudinal smooth muscle), muscularis mucosa, submucosal glands, crypt, villi epithelial cells, goblet cells and lamina propria (PubMed:24220035).
Expressed at perimuscular and peritendious areas in the developing limbs (PubMed:35962790).

Developmental stage

At 10.5 dpc, strongly and specifically expressed in the developing heart tubes (PubMed:24220035).
By 13.5 dpc, widely expressed including in the perichondrium in the developing autopod, brain, ear, whisker follicles, vertebral column and epidermis (PubMed:24220035).
Also localizes to the myocardium of the developing right atrium, the bulbous cordis and the airway epithelia of the main bronchiole in the lung bud at 11.5 dpc, the vertebral column and dorsal root ganglia at 14.5 dpc, and the developing hind limb at 15.5 dpc (PubMed:24220035).
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 the mesenchyme of developing limb, highest expression is observed between 13.0 dpc and 15.0 dpc; expression disappears almost completely by 15.5 dpc (PubMed:35962790).
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, domain, compositional bias.

TypeIDPosition(s)Description
Region144-172Disordered
Motif172-179Cysteine switch
Domain218-427Peptidase M12B
Domain428-515Disintegrin
Domain516-571TSP type-1 1
Region701-838Spacer
Region798-822Disordered
Compositional bias799-815Basic and acidic residues
Domain839-895TSP type-1 2
Domain896-949TSP 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
    950
  • Mass (Da)
    103,938
  • Last updated
    2007-01-09 v2
  • Checksum
    891926F281E92010
MLLLGISILALAWRPAGSSEPEWEVVVPIRRDPDINGRHYYRRGTEDSGDQGLIFQITAFQQDFYLHLTPDAQFLAPAFATEYLGVPLQRLTGSSLDLRRCFYSGYVNAEPDSFAAVSLCGGLRGAFGYRGAEYVISPLPNTSAPEAQRHSQGAHLLQRRGAPVGPSGDPTSRCGVASGWNPAILRALDPYKPRRTGAGESHNRRRSGRAKRFVSIPRYVETLVVADESMVKFHGADLEHYLLTLLATAARLYRHPSILNPINIVVVKVLLLGDRDTGPKVTGNAALTLRNFCAWQKKLNKVSDKHPEYWDTAILFTRQDLCGATTCDTLGMADVGTMCDPKRSCSVIEDDGLPSAFTTAHELGHVFNMPHDNVKVCEEVFGKLRANHMMSPTLIQIDRANPWSACSAAIITDFLDSGHGDCLLDQPSKPITLPEDLPGTSYSLSQQCELAFGVGSKPCPYMQYCTKLWCTGKAKGQMVCQTRHFPWADGTSCGEGKFCLKGACVERHNPNKYRVDGSWAKWEPYGSCSRTCGGGVQLARRQCSNPTPANGGKYCEGVRVKYRSCNLEPCPSSASGKSFREEQCEAFNGYNHSTNRLTLAVAWVPKYSGVSPRDKCKLICRANGTGYFYVLAPKVVDGTLCTPDSTSVCVQGKCIKAGCDGNLGSKKKFDKCGVCGGDNKSCKRVTGLFTKPMHGYNFVVAIPAGASSIDIRQRGYKGLIGDDNYLALKNSQGKYLLNGHFVVSAVERDLVVKGSVLRYSGTGTAVESLQASRPILEPLTVEVLSVGKMTPPRVRYSFYLPKEPREDKSTRPKDPRGSPVLRNSVLSLSNQVEQPDNRPPARWVAGSWGPCSVSCGSGLQKRAVDCRDSPGQQGASACDVDHRPLEKRACGEPCPTWELGNWSPCSKSCGRGFKRRPLKCVGHGGRLLARDQCDLRRKPQELDFCVLRPC

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A1L1SUC3A0A1L1SUC3_MOUSEAdamts1556

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict389-396in Ref. 1; AAH43308
Sequence conflict611-614in Ref. 1; AAH09667
Compositional bias799-815Basic and acidic residues
Sequence conflict819in Ref. 1; AAH09667

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BC009667
EMBL· GenBank· DDBJ
AAH09667.1
EMBL· GenBank· DDBJ
mRNA
BC043308
EMBL· GenBank· DDBJ
AAH43308.1
EMBL· GenBank· DDBJ
mRNA
BC094677
EMBL· GenBank· DDBJ
AAH94677.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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