ADAM15
Disintegrin and metalloproteinase domain-containing protein 15
Also known as: ADA15_HUMAN, MDC15
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q13444
- Gene
- ADAM15
- Ensembl
- ENSG00000143537
- Chromosome
- 1
- Canonical length
- 863 aa
- Protein class
- Predicted intracellular proteins, Predicted membrane proteins
- Subcellular location
- Vesicles
OverviewNCBI Gene
The protein encoded by this gene is a member of the ADAM (a disintegrin and metalloproteinase) protein family. ADAM family members are type I transmembrane glycoproteins known to be involved in cell adhesion and proteolytic ectodomain processing of cytokines and adhesion molecules. This protein contains multiple functional domains including a zinc-binding metalloprotease domain, a disintegrin-like domain, as well as a EGF-like domain. Through its disintegrin-like domain, this protein specifically interacts with the integrin beta chain, beta 3. It also interacts with Src family protein-tyrosine kinases in a phosphorylation-dependent manner, suggesting that this protein may function in cell-cell adhesion as well as in cellular signaling. Multiple alternatively spliced transcript variants encoding distinct isoforms have been observed. [provided by RefSeq, Jul 2008]
Canonical amino-acid sequenceUniProt
863 residues, UniProt reviewed canonical sequence.
>Q13444|ADAM15
1 MRLALLWALG LLGAGSPLPS WPLPNIGGTE EQQAESEKAP REPLEPQVLQ DDLPISLKKV
61 LQTSLPEPLR IKLELDGDSH ILELLQNREL VPGRPTLVWY QPDGTRVVSE GHTLENCCYQ
121 GRVRGYAGSW VSICTCSGLR GLVVLTPERS YTLEQGPGDL QGPPIISRIQ DLHLPGHTCA
181 LSWRESVHTQ KPPEHPLGQR HIRRRRDVVT ETKTVELVIV ADHSEAQKYR DFQHLLNRTL
241 EVALLLDTFF RPLNVRVALV GLEAWTQRDL VEISPNPAVT LENFLHWRRA HLLPRLPHDS
301 AQLVTGTSFS GPTVGMAIQN SICSPDFSGG VNMDHSTSIL GVASSIAHEL GHSLGLDHDL
361 PGNSCPCPGP APAKTCIMEA STDFLPGLNF SNCSRRALEK ALLDGMGSCL FERLPSLPPM
421 AAFCGNMFVE PGEQCDCGFL DDCVDPCCDS LTCQLRPGAQ CASDGPCCQN CQLRPSGWQC
481 RPTRGDCDLP EFCPGDSSQC PPDVSLGDGE PCAGGQAVCM HGRCASYAQQ CQSLWGPGAQ
541 PAAPLCLQTA NTRGNAFGSC GRNPSGSYVS CTPRDAICGQ LQCQTGRTQP LLGSIRDLLW
601 ETIDVNGTEL NCSWVHLDLG SDVAQPLLTL PGTACGPGLV CIDHRCQRVD LLGAQECRSK
661 CHGHGVCDSN RHCYCEEGWA PPDCTTQLKA TSSLTTGLLL SLLVLLVLVM LGASYWYRAR
721 LHQRLCQLKG PTCQYRAAQS GPSERPGPPQ RALLARGTKQ ASALSFPAPP SRPLPPDPVS
781 KRLQAELADR PNPPTRPLPA DPVVRSPKSQ GPAKPPPPRK PLPADPQGRC PSGDLPGPGA
841 GIPPLVVPSR PAPPPPTVSS LYLLocalizationUniProt · AlphaFold · HPA
Whether an antibody against ADAM15 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Cell surface
- Secreted
- No
- Transmembrane segments
- 1
- Mean surface accessibility (rSASA)
- 0.37
- Highest tissue expression
- 104 nTPM
Expression across tissuesHPA
Tissue
- skin: 104 nTPM
- esophagus: 77 nTPM
- adipose tissue: 67 nTPM
- breast: 62 nTPM
- heart muscle: 62 nTPM
- vagina: 54 nTPM
Single-cell type
- extravillous trophoblasts: 263 nCPM
- vascular endothelial cells: 172 nCPM
- esophageal suprabasal cells: 136 nCPM
- respiratory deuterosomal cells: 129 nCPM
- foveolar cells: 120 nCPM
- esophageal basal cells: 104 nCPM
Immune cell
- myeloid DC: 64 nTPM
- classical monocyte: 39 nTPM
- intermediate monocyte: 27 nTPM
- total PBMC: 23 nTPM
- gdT-cell: 9.5 nTPM
- T-reg: 9 nTPM
Brain region
- medulla oblongata: 36 nTPM
- thalamus: 31 nTPM
- white matter: 30 nTPM
- spinal cord: 30 nTPM
- pons: 29 nTPM
- cerebellum: 29 nTPM
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 0.86
- gnomAD pLI
- 0
- gnomAD missense Z
- 1.07
- DepMap mean gene effect
- -0.07
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 8% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- angiogenesis
- cardiac epithelial to mesenchymal transition
- cell-matrix adhesion
- cellular response to phorbol 13-acetate 12-myristate
- collagen catabolic process
- extracellular matrix disassembly
- immune response to tumor cell
- innate immune response
- integrin-mediated signaling pathway
- male gonad development
- negative regulation of cell growth
- negative regulation of cell migration
- negative regulation of cell-matrix adhesion
- proteolysis
- response to hypobaric hypoxia
- tissue regeneration
Molecular functions
- immunoglobulin receptor binding
- integrin binding
- metal ion binding
- metalloendopeptidase activity
- metallopeptidase activity
- SH3 domain binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
- EGF-like domain
- Peptidase M12B, ADAM/reprolysin
- Disintegrin domain
- Peptidase M12B, propeptide
- ADAM, cysteine-rich domain
- Metallopeptidase, catalytic domain superfamily
- Reprolysin domain, adamalysin-type
- Disintegrin domain superfamily
- Disintegrin
- Reprolysin (M12B) family zinc metalloprotease
- Reprolysin family propeptide
- ADAM cysteine-rich
KeywordsUniProt
- Angiogenesis
- Cell adhesion
- Cell junction
- Cell projection
- Cilium
- Cleavage on pair of basic residues
- Collagen degradation
- Cytoplasmic vesicle
- Disulfide bond
- EGF-like domain
- Flagellum
- Glycoprotein
- Hydrolase
- Membrane
- Metal-binding
- Metalloprotease
- Phosphoprotein
- Protease
- SH3-binding
- Signal
- Transmembrane
- Transmembrane helix
- Zinc
- Zymogen
InteractionsUniProt · HPA
Protein binding partners of ADAM15 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads ADAM15 as an antibody target. Whether an autoantibody or antibody against ADAM15 could matter depends on whether native ADAM15 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
ADAM15 is annotated at the cell surface, where native ADAM15 is exposed to circulating antibodies and is a prime autoantibody target that could block, deplete, or overstimulate it.
Annotation status
The present source text does not explicitly label ADAM15 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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