ADAMTS10
A disintegrin and metalloproteinase with thrombospondin motifs 10
Also known as: ADAM-TS10, ATS10_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q9H324
- Gene
- ADAMTS10
- Ensembl
- ENSG00000142303
- Chromosome
- 19
- Canonical length
- 1103 aa
- Protein class
- Disease related genes, Human disease related genes, Predicted intracellular proteins, Predicted secreted proteins
- Secretome location
- Secreted to extracellular matrix
OverviewNCBI Gene
This gene belongs to the ADAMTS (a disintegrin and metalloproteinase domain with thrombospondin type-1 motifs) family of zinc-dependent proteases. ADAMTS proteases are complex secreted enzymes containing a prometalloprotease domain of the reprolysin type attached to an ancillary domain with a highly conserved structure that includes at least one thrombospondin type 1 repeat. They have been demonstrated to have important roles in connective tissue organization, coagulation, inflammation, arthritis, angiogenesis and cell migration. The product of this gene plays a major role in growth and in skin, lens, and heart development. It is also a candidate gene for autosomal recessive Weill-Marchesani syndrome. [provided by RefSeq, Jul 2008]
Canonical amino-acid sequenceUniProt
1103 residues, UniProt reviewed canonical sequence.
>Q9H324|ADAMTS10
1 MAPACQILRW ALALGLGLMF EVTHAFRSQD EFLSSLESYE IAFPTRVDHN GALLAFSPPP
61 PRRQRRGTGA TAESRLFYKV ASPSTHFLLN LTRSSRLLAG HVSVEYWTRE GLAWQRAARP
121 HCLYAGHLQG QASTSHVAIS TCGGLHGLIV ADEEEYLIEP LHGGPKGSRS PEESGPHVVY
181 KRSSLRHPHL DTACGVRDEK PWKGRPWWLR TLKPPPARPL GNETERGQPG LKRSVSRERY
241 VETLVVADKM MVAYHGRRDV EQYVLAIMNI VAKLFQDSSL GSTVNILVTR LILLTEDQPT
301 LEITHHAGKS LDSFCKWQKS IVNHSGHGNA IPENGVANHD TAVLITRYDI CIYKNKPCGT
361 LGLAPVGGMC ERERSCSVNE DIGLATAFTI AHEIGHTFGM NHDGVGNSCG ARGQDPAKLM
421 AAHITMKTNP FVWSSCSRDY ITSFLDSGLG LCLNNRPPRQ DFVYPTVAPG QAYDADEQCR
481 FQHGVKSRQC KYGEVCSELW CLSKSNRCIT NSIPAAEGTL CQTHTIDKGW CYKRVCVPFG
541 SRPEGVDGAW GPWTPWGDCS RTCGGGVSSS SRHCDSPRPT IGGKYCLGER RRHRSCNTDD
601 CPPGSQDFRE VQCSEFDSIP FRGKFYKWKT YRGGGVKACS LTCLAEGFNF YTERAAAVVD
661 GTPCRPDTVD ICVSGECKHV GCDRVLGSDL REDKCRVCGG DGSACETIEG VFSPASPGAG
721 YEDVVWIPKG SVHIFIQDLN LSLSHLALKG DQESLLLEGL PGTPQPHRLP LAGTTFQLRQ
781 GPDQVQSLEA LGPINASLIV MVLARTELPA LRYRFNAPIA RDSLPPYSWH YAPWTKCSAQ
841 CAGGSQVQAV ECRNQLDSSA VAPHYCSAHS KLPKRQRACN TEPCPPDWVV GNWSLCSRSC
901 DAGVRSRSVV CQRRVSAAEE KALDDSACPQ PRPPVLEACH GPTCPPEWAA LDWSECTPSC
961 GPGLRHRVVL CKSADHRATL PPAHCSPAAK PPATMRCNLR RCPPARWVAG EWGECSAQCG
1021 VGQRQRSVRC TSHTGQASHE CTEALRPPTT QQCEAKCDSP TPGDGPEECK DVNKVAYCPL
1081 VLKFQFCSRA YFRQMCCKTC HGHLocalizationUniProt · AlphaFold · HPA
Whether an antibody against ADAMTS10 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
- Secreted
- Secreted
- Yes
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.34
- Highest tissue expression
- 20 nTPM
Expression across tissuesHPA
Tissue
- blood vessel: 20 nTPM
- adipose tissue: 14 nTPM
- cervix: 11 nTPM
- cerebral cortex: 11 nTPM
- endometrium: 10 nTPM
- fallopian tube: 9.3 nTPM
Single-cell type
- myosatellite cells: 186 nCPM
- microglia: 69 nCPM
- adipocytes: 56 nCPM
- hepatic stellate cells: 45 nCPM
- vascular smooth muscle cells: 45 nCPM
- fibro-adipogenic progenitors: 42 nCPM
Immune cell
- basophil: 0 nTPM
- classical monocyte: 0 nTPM
- eosinophil: 0 nTPM
- gdT-cell: 0 nTPM
- intermediate monocyte: 0 nTPM
- MAIT T-cell: 0 nTPM
Brain region
- cerebral cortex: 14 nTPM
- hypothalamus: 12 nTPM
- medulla oblongata: 8.3 nTPM
- basal ganglia: 8.2 nTPM
- amygdala: 8.1 nTPM
- midbrain: 7.7 nTPM
DiseaseUniProt · ClinVar · IEDB · PubMed
Four sources answering four different questions about ADAMTS10.
Disease | AllUniProt
Conditions ADAMTS10 is implicated in, by any mechanism.
- Weill-Marchesani syndrome 1 (WMS1) MIM:277600
Disease | GeneticClinVar
37 pathogenic / likely-pathogenic of 1,096 ClinVar records.
Conditions with pathogenic or likely-pathogenic variants.
- Weill-Marchesani syndrome 1
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)
- 0.33
- gnomAD pLI
- 0.84
- gnomAD missense Z
- 3.63
- DepMap mean gene effect
- -0.12
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
Molecular functions
Cellular components
Protein domainsUniProt · Pfam · InterPro
- Thrombospondin type-1 (TSP1) repeat
- Peptidase M12B, ADAM/reprolysin
- Peptidase M12B, propeptide
- ADAMTS/ADAMTS-like, Spacer 1
- PLAC
- ADAMTS/ADAMTS-like
- Metallopeptidase, catalytic domain superfamily
- Thrombospondin type-1 repeat superfamily
- ADAMTS, cysteine-rich domain 2
- ADAMTS/ADAMTS-like, cysteine-rich domain 3
- ADAMTS and ADAMTS-like
- Thrombospondin type 1 domain
- Reprolysin (M12B) family zinc metalloprotease
- Reprolysin family propeptide
- ADAM-TS Spacer 1
- PLAC (protease and lacunin) domain
- ADAMTS cysteine-rich domain 2
- Thrombospondin type 1 domain
- ADAMTS cysteine-rich domain
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of ADAMTS10 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 ADAMTS10 as an antibody target. Whether an autoantibody or antibody against ADAMTS10 could matter depends on whether native ADAMTS10 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
ADAMTS10 is annotated as secreted, so native ADAMTS10 circulates and is directly accessible to antibodies. Secreted and cell-surface proteins are the autoantibody targets most likely to act like drugs, blocking or depleting the native protein.
Annotation status
The present source text does not explicitly label ADAMTS10 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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