Q9QYV0 · ADA15_RAT

  • Protein
    Disintegrin and metalloproteinase domain-containing protein 15
  • Gene
    Adam15
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    5/5

Function

function

Active metalloproteinase with gelatinolytic and collagenolytic activity. Plays a role in the wound healing process. Mediates both heterotypic intraepithelial cell/T-cell interactions and homotypic T-cell aggregation. Inhibits beta-1 integrin-mediated cell adhesion and migration of airway smooth muscle cells. Suppresses cell motility on or towards fibronectin possibly by driving alpha-v/beta-1 integrin (ITAGV-ITGB1) cell surface expression via ERK1/2 inactivation. Cleaves E-cadherin in response to growth factor deprivation. Plays a role in glomerular cell migration. Plays a role in pathological neovascularization. May play a role in cartilage remodeling. May be proteolytically processed, during sperm epididymal maturation and the acrosome reaction. May play a role in sperm-egg binding through its disintegrin domain (By similarity).

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site, active site.

1864100200300400500600700800
Type
IDPosition(s)Description
Binding site180Zn2+ (UniProtKB | ChEBI); catalytic; in inhibited form
Binding site350Zn2+ (UniProtKB | ChEBI); catalytic
Active site351
Binding site354Zn2+ (UniProtKB | ChEBI); catalytic
Binding site360Zn2+ (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
Cellular Componentacrosomal vesicle
Cellular Componentadherens junction
Cellular Componentcell surface
Cellular Componentextracellular exosome
Cellular Componentextracellular space
Cellular Componentmembrane
Cellular Componentmotile cilium
Molecular Functionimmunoglobulin receptor binding
Molecular Functionintegrin binding
Molecular Functionmetal ion binding
Molecular Functionmetalloendopeptidase activity
Molecular Functionmetallopeptidase activity
Molecular FunctionSH3 domain binding
Biological Processangiogenesis
Biological Processcardiac epithelial to mesenchymal transition
Biological Processcell-cell adhesion
Biological Processcellular response to phorbol 13-acetate 12-myristate
Biological Processcollagen catabolic process
Biological Processimmune response to tumor cell
Biological Processinnate immune response
Biological Processintegrin-mediated signaling pathway
Biological Processmale gonad development
Biological Processnegative regulation of cell growth
Biological Processnegative regulation of cell migration
Biological Processnegative regulation of cell-matrix adhesion
Biological Processproteolysis
Biological Processresponse to hypobaric hypoxia
Biological Processtissue regeneration

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Disintegrin and metalloproteinase domain-containing protein 15
  • EC number
  • Short names
    ADAM 15
  • Alternative names
    • CRII-7
    • Metalloprotease RGD disintegrin protein
    • Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 15 (MDC-15)
    • Metargidin

Gene names

    • Name
      Adam15
    • Synonyms
      Mdc15

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    Q9QYV0
  • Secondary accessions
    • Q6P779

Proteomes

Organism-specific databases

Subcellular Location

Endomembrane system
; Single-pass type I membrane protein
Note: The majority of the protein is localized in a perinuclear compartment which may correspond to the trans-Golgi network or the late endosome. The pro-protein is the major detectable form on the cell surface, whereas the majority of the protein in the cell is processed (By similarity).

Features

Showing features for topological domain, transmembrane.

Type
IDPosition(s)Description
Topological domain209-698Extracellular
Transmembrane699-719Helical
Topological domain720-864Cytoplasmic

Keywords

Phenotypes & Variants

Variants

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

The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Chemistry

PTM/Processing

Features

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

Type
IDPosition(s)Description
Signal1-17
PropeptidePRO_000002908618-208
Glycosylation57N-linked (GlcNAc...) asparagine
ChainPRO_0000029087209-864Disintegrin and metalloproteinase domain-containing protein 15
Glycosylation239N-linked (GlcNAc...) asparagine
Disulfide bond325↔411
Disulfide bond367↔395
Disulfide bond369↔378
Glycosylation391N-linked (GlcNAc...) asparagine
Glycosylation394N-linked (GlcNAc...) asparagine
Disulfide bond482↔502
Glycosylation608N-linked (GlcNAc...) asparagine
Glycosylation613N-linked (GlcNAc...) asparagine
Disulfide bond659↔669
Disulfide bond663↔675
Disulfide bond677↔686
Modified residue717Phosphotyrosine; by HCK and LCK
Modified residue737Phosphotyrosine; by HCK and LCK

Post-translational modification

The precursor is cleaved by a furin endopeptidase.
Phosphorylation increases association with PTKs.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Predominantly expressed in brain, spinal cord, sciatic nerve and lung. Expressed at lower levels in all other tissues. In the peripheral nervous system, expressed predominantly by Schwann cells. In the central nervous system, preferentially expressed by neuronal cells.

Induction

In response to sciatic nerve injury.

Gene expression databases

Interaction

Subunit

Interacts with ITAGV-ITGB3 (vitronectin receptor). Interacts with SH3GL2 and SNX9; this interaction occurs preferentially with ADAM15 precursor, rather than the processed form, suggesting it occurs in a secretory pathway compartment prior to the medial Golgi (By similarity).
Interacts with ITAG9-ITGB1. Interacts specifically with Src family protein-tyrosine kinases (PTKs). Interacts with SH3PXD2A. Interacts with ITAGV-ITGB1. Interacts with GRB2, HCK, ITSN1, ITSN2, LYN, MAPK1, MAPK3, NCF1, NCK1, nephrocystin, PTK6, SNX33, LCK and SRC (By similarity).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias, motif, domain.

Type
IDPosition(s)Description
Region17-49Disordered
Compositional bias27-49Polar residues
Motif178-185Cysteine switch
Domain215-416Peptidase M12B
Domain423-510Disintegrin
Domain659-687EGF-like
Region738-864Disordered
Compositional bias796-834Pro residues
Motif816-822SH3-binding
Compositional bias849-864Pro residues
Motif851-857SH3-binding

Domain

The cytoplasmic domain is required for SH3GL2- and SNX9-binding.
Disintegrin domain binds to integrin alphaV-beta3.
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 & Isoform

Align isoforms (2)
  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 2 isoforms produced by Alternative splicing.

Q9QYV0-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    864
  • Mass (Da)
    93,308
  • Last updated
    2010-07-13 v2
  • Checksum
    5D46466922A89196
MRLALLWALGLLGAGSPRPSPPLPNIGGTEEEQQASPERTQSRSLENQVVQDSPPINLTEVLQTGLPETLRIGLELDGENHILELQQNRDLVPGRPTLVWYQPDGTRMVSEGHSLENCCYRGRVQGRPSSWVSLCACSGIRGLVVLSPERSYTLELGPGDLQRPLIVSRIQDLLLPGHTCAPSWHAFVPTEAAPDLLLEQHHLRRLKRDVVTETKIVELVIVADNSEVRKYPDFQQLLNRTLEVALLLDTFFQPLNVRVALVGLEAWTQRDLIEMSSNPAVLLDNFLRWRRTDLLPRLPHDSAQLVTVTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDSPGNSCPCPGPAPAKSCIMEASTDFLPGLNFSNCSRWALEKALLDGMGSCLFEWPPSRAPMSSLCGNMFVDPGEQCDCGFPDECTDPCCDYFTCQLRPGAQCASDGPCCQNCKLQPAGWQCRLPTDDCDLPEFCLGDSSQCPPDIRLGDGEPCASGEAVCMHGRCASYTRQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRSPSGSYMPCNLRDAICGQLQCQWGRNQPLLGSVQDQLSEVLEANGTQLNCSWVDLDLGNDVAQPLLALPGTACGPGLVCIGHRCQPVDLLGAQECRSKCHGHGVCDSSRHCHCDEGWAPPDCMTQLRATSSLTTGLLLSLLLLLVLVLLGASYWYRARLHQRLCQLKGSSCQYRAAQSGPPERPGPPQRAQQMPGTKQANVSFPVPPSRPLPPNPVPKKLQAELADRSNPPTRPLPADPVVWRPKPQGPTKPPPPRKPLPANPQGRPPLGDLPGPGDGSLQLVVPSRPAPPPPAASSLYL

Q9QYV0-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A8I6AF83A0A8I6AF83_RATAdam15840

Features

Showing features for compositional bias, sequence conflict, alternative sequence.

Type
IDPosition(s)Description
Compositional bias27-49Polar residues
Sequence conflict202in Ref. 2; AAH61796
Alternative sequenceVSP_039534762-809in isoform 2
Compositional bias796-834Pro residues
Compositional bias849-864Pro residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ251198
EMBL· GenBank· DDBJ
CAB61762.1
EMBL· GenBank· DDBJ
mRNA
BC061796
EMBL· GenBank· DDBJ
AAH61796.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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