ADAMTS17

Protein identityUniProt · HPA

UniProt accession

Q8TE56

Gene

ADAMTS17

Ensembl

ENSG00000140470

Chromosome

15

Canonical length

1095 aa

Protein class

Disease related genes, Human disease related genes, Predicted intracellular proteins, Predicted secreted proteins

Subcellular location

Nucleoplasm

Secretome location

Secreted to extracellular matrix

OverviewNCBI Gene

This gene encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) protein family. ADAMTS family members share several distinct protein modules, including a propeptide region, a metalloproteinase domain, a disintegrin-like domain, and a thrombospondin type 1 (TS) motif. Individual members of this family differ in the number of C-terminal TS motifs, and some have unique C-terminal domains. The encoded preproprotein is proteolytically processed to generate the mature protein, which may promote breast cancer cell growth and survival. Mutations in this gene are associated with a Weill-Marchesani-like syndrome, which is characterized by lenticular myopia, ectopia lentis, glaucoma, spherophakia, and short stature. [provided by RefSeq, May 2016]

Canonical amino-acid sequenceUniProt

1095 residues, UniProt reviewed canonical sequence.

>Q8TE56|ADAMTS17
     1  MCDGALLPPL VLPVLLLLVW GLDPGTAVGD AAADVEVVLP WRVRPDDVHL PPLPAAPGPR
    61  RRRRPRTPPA APRARPGERA LLLHLPAFGR DLYLQLRRDL RFLSRGFEVE EAGAARRRGR
   121  PAELCFYSGR VLGHPGSLVS LSACGAAGGL VGLIQLGQEQ VLIQPLNNSQ GPFSGREHLI
   181  RRKWSLTPSP SAEAQRPEQL CKVLTEKKKP TWGRPSRDWR ERRNAIRLTS EHTVETLVVA
   241  DADMVQYHGA EAAQRFILTV MNMVYNMFQH QSLGIKINIQ VTKLVLLRQR PAKLSIGHHG
   301  ERSLESFCHW QNEEYGGARY LGNNQVPGGK DDPPLVDAAV FVTRTDFCVH KDEPCDTVGI
   361  AYLGGVCSAK RKCVLAEDNG LNLAFTIAHE LGHNLGMNHD DDHSSCAGRS HIMSGEWVKG
   421  RNPSDLSWSS CSRDDLENFL KSKVSTCLLV TDPRSQHTVR LPHKLPGMHY SANEQCQILF
   481  GMNATFCRNM EHLMCAGLWC LVEGDTSCKT KLDPPLDGTE CGADKWCRAG ECVSKTPIPE
   541  HVDGDWSPWG AWSMCSRTCG TGARFRQRKC DNPPPGPGGT HCPGASVEHA VCENLPCPKG
   601  LPSFRDQQCQ AHDRLSPKKK GLLTAVVVDD KPCELYCSPL GKESPLLVAD RVLDGTPCGP
   661  YETDLCVHGK CQKIGCDGII GSAAKEDRCG VCSGDGKTCH LVKGDFSHAR GTALKDSGKG
   721  SINSDWKIEL PGEFQIAGTT VRYVRRGLWE KISAKGPTKL PLHLMVLLFH DQDYGIHYEY
   781  TVPVNRTAEN QSEPEKPQDS LFIWTHSGWE GCSVQCGGGE RRTIVSCTRI VNKTTTLVND
   841  SDCPQASRPE PQVRRCNLHP CQSRWVAGPW SPCSATCEKG FQHREVTCVY QLQNGTHVAT
   901  RPLYCPGPRP AAVQSCEGQD CLSIWEASEW SQCSASCGKG VWKRTVACTN SQGKCDASTR
   961  PRAEEACEDY SGCYEWKTGD WSTCSSTCGK GLQSRVVQCM HKVTGRHGSE CPALSKPAPY
  1021  RQCYQEVCND RINANTITSP RLAALTYKCT RDQWTVYCRV IREKNLCQDM RWYQRCCQTC
  1081  RDFYANKMRQ PPPNS

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against ADAMTS17 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)

0.36

Highest tissue expression

9.9 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about ADAMTS17.

Disease | AllUniProt

Conditions ADAMTS17 is implicated in, by any mechanism.

• Weill-Marchesani syndrome 4 (WMS4) MIM:613195

Disease | GeneticClinVar

70 pathogenic / likely-pathogenic of 1,495 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Weill-Marchesani 4 syndrome, recessive
• Ovarian serous cystadenocarcinoma
• Anterior segment dysgenesis
• ADAMTS17-related disorder

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)

0.73

gnomAD pLI

0

gnomAD missense Z

-1.39

DepMap mean gene effect

0.02

DepMap dependency class

selective

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 5% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• extracellular matrix organization
• proteolysis

Molecular functions

• metal ion binding
• metalloendopeptidase activity

Cellular components

• extracellular matrix

Protein domainsUniProt · Pfam · InterPro

• Thrombospondin type-1 (TSP1) repeat
• Peptidase M12B, ADAM/reprolysin
• Peptidase M12B, propeptide
• ADAM, cysteine-rich domain
• ADAMTS/ADAMTS-like, Spacer 1
• PLAC
• Zinc finger C2H2-type
• 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
• A disintegrin and metalloproteinase with thrombospondin motifs 17/19, C-terminal helical domain
• Thrombospondin type 1 domain
• Reprolysin (M12B) family zinc metalloprotease
• Reprolysin family propeptide
• ADAM-TS Spacer 1
• ADAMTS cysteine-rich domain 2
• Thrombospondin type 1 domain
• ADAMTS cysteine-rich domain
• ADAMTS C-terminal helical domain

KeywordsUniProt

• Cleavage on pair of basic residues
• Deafness
• Disulfide bond
• Dwarfism
• Extracellular matrix
• Glycoprotein
• Hydrolase
• Metal-binding
• Metalloprotease
• Protease
• Repeat
• Secreted
• Signal
• Zinc
• Zymogen