ADAMTS9
A disintegrin and metalloproteinase with thrombospondin motifs 9
Also known as: ATS9_HUMAN, KIAA1312
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q9P2N4
- Gene
- ADAMTS9
- Ensembl
- ENSG00000163638
- Chromosome
- 3
- Canonical length
- 1935 aa
- Protein class
- Cancer-related genes, Human disease related genes, Plasma proteins, Predicted intracellular proteins, Predicted secreted proteins
- Subcellular location
- Endoplasmic reticulum,Vesicles
- 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. Members of the family 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. Members of the ADAMTS family have been implicated in the cleavage of proteoglycans, the control of organ shape during development, and the inhibition of angiogenesis. This gene is localized to chromosome 3p14.3-p14.2, an area known to be lost in hereditary renal tumors. Alternative splicing results in multiple transcript variants encoding different isoforms that may undergo similar proteolytic processing. [provided by RefSeq, Jan 2016]
Canonical amino-acid sequenceUniProt
1935 residues, UniProt reviewed canonical sequence.
>Q9P2N4|ADAMTS9
1 MQFVSWATLL TLLVRDLAEM GSPDAAAAVR KDRLHPRQVK LLETLSEYEI VSPIRVNALG
61 EPFPTNVHFK RTRRSINSAT DPWPAFASSS SSSTSSQAHY RLSAFGQQFL FNLTANAGFI
121 APLFTVTLLG TPGVNQTKFY SEEEAELKHC FYKGYVNTNS EHTAVISLCS GMLGTFRSHD
181 GDYFIEPLQS MDEQEDEEEQ NKPHIIYRRS APQREPSTGR HACDTSEHKN RHSKDKKKTR
241 ARKWGERINL AGDVAALNSG LATEAFSAYG NKTDNTREKR THRRTKRFLS YPRFVEVLVV
301 ADNRMVSYHG ENLQHYILTL MSIVASIYKD PSIGNLINIV IVNLIVIHNE QDGPSISFNA
361 QTTLKNFCQW QHSKNSPGGI HHDTAVLLTR QDICRAHDKC DTLGLAELGT ICDPYRSCSI
421 SEDSGLSTAF TIAHELGHVF NMPHDDNNKC KEEGVKSPQH VMAPTLNFYT NPWMWSKCSR
481 KYITEFLDTG YGECLLNEPE SRPYPLPVQL PGILYNVNKQ CELIFGPGSQ VCPYMMQCRR
541 LWCNNVNGVH KGCRTQHTPW ADGTECEPGK HCKYGFCVPK EMDVPVTDGS WGSWSPFGTC
601 SRTCGGGIKT AIRECNRPEP KNGGKYCVGR RMKFKSCNTE PCLKQKRDFR DEQCAHFDGK
661 HFNINGLLPN VRWVPKYSGI LMKDRCKLFC RVAGNTAYYQ LRDRVIDGTP CGQDTNDICV
721 QGLCRQAGCD HVLNSKARRD KCGVCGGDNS SCKTVAGTFN TVHYGYNTVV RIPAGATNID
781 VRQHSFSGET DDDNYLALSS SKGEFLLNGN FVVTMAKREI RIGNAVVEYS GSETAVERIN
841 STDRIEQELL LQVLSVGKLY NPDVRYSFNI PIEDKPQQFY WNSHGPWQAC SKPCQGERKR
901 KLVCTRESDQ LTVSDQRCDR LPQPGHITEP CGTDCDLRWH VASRSECSAQ CGLGYRTLDI
961 YCAKYSRLDG KTEKVDDGFC SSHPKPSNRE KCSGECNTGG WRYSAWTECS KSCDGGTQRR
1021 RAICVNTRND VLDDSKCTHQ EKVTIQRCSE FPCPQWKSGD WSECLVTCGK GHKHRQVWCQ
1081 FGEDRLNDRM CDPETKPTSM QTCQQPECAS WQAGPWGQCS VTCGQGYQLR AVKCIIGTYM
1141 SVVDDNDCNA ATRPTDTQDC ELPSCHPPPA APETRRSTYS APRTQWRFGS WTPCSATCGK
1201 GTRMRYVSCR DENGSVADES ACATLPRPVA KEECSVTPCG QWKALDWSSC SVTCGQGRAT
1261 RQVMCVNYSD HVIDRSECDQ DYIPETDQDC SMSPCPQRTP DSGLAQHPFQ NEDYRPRSAS
1321 PSRTHVLGGN QWRTGPWGAC SSTCAGGSQR RVVVCQDENG YTANDCVERI KPDEQRACES
1381 GPCPQWAYGN WGECTKLCGG GIRTRLVVCQ RSNGERFPDL SCEILDKPPD REQCNTHACP
1441 HDAAWSTGPW SSCSVSCGRG HKQRNVYCMA KDGSHLESDY CKHLAKPHGH RKCRGGRCPK
1501 WKAGAWSQCS VSCGRGVQQR HVGCQIGTHK IARETECNPY TRPESERDCQ GPRCPLYTWR
1561 AEEWQECTKT CGEGSRYRKV VCVDDNKNEV HGARCDVSKR PVDRESCSLQ PCEYVWITGE
1621 WSECSVTCGK GYKQRLVSCS EIYTGKENYE YSYQTTINCP GTQPPSVHPC YLRDCPVSAT
1681 WRVGNWGSCS VSCGVGVMQR SVQCLTNEDQ PSHLCHTDLK PEERKTCRNV YNCELPQNCK
1741 EVKRLKGASE DGEYFLMIRG KLLKIFCAGM HSDHPKEYVT LVHGDSENFS EVYGHRLHNP
1801 TECPYNGSRR DDCQCRKDYT AAGFSSFQKI RIDLTSMQII TTDLQFARTS EGHPVPFATA
1861 GDCYSAAKCP QGRFSINLYG TGLSLTESAR WISQGNYAVS DIKKSPDGTR VVGKCGGYCG
1921 KCTPSSGTGL EVRVLLocalizationUniProt · AlphaFold · HPA
Whether an antibody against ADAMTS9 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)
- 0.35
- Highest tissue expression
- 39 nTPM
Expression across tissuesHPA
Tissue
- adipose tissue: 39 nTPM
- placenta: 30 nTPM
- urinary bladder: 21 nTPM
- breast: 19 nTPM
- blood vessel: 18 nTPM
- heart muscle: 14 nTPM
Single-cell type
- vascular endothelial cells: 1,366 nCPM
- podocytes: 1,243 nCPM
- epicardial cells: 892 nCPM
- endometrial stromal cells: 775 nCPM
- vascular smooth muscle cells: 774 nCPM
- pericytes: 752 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
- medulla oblongata: 26 nTPM
- pons: 22 nTPM
- thalamus: 22 nTPM
- spinal cord: 21 nTPM
- choroid plexus: 20 nTPM
- cerebral cortex: 19 nTPM
DiseaseUniProt · ClinVar · IEDB · PubMed
Four sources answering four different questions about ADAMTS9.
Disease | GeneticClinVar
1 pathogenic / likely-pathogenic of 564 ClinVar records.
Conditions with pathogenic or likely-pathogenic variants.
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)
- 0.39
- gnomAD pLI
- 0
- gnomAD missense Z
- 0.95
- DepMap mean gene effect
- -0.12
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 3% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- aorta morphogenesis
- camera-type eye morphogenesis
- cornea development in camera-type eye
- endothelial cell-matrix adhesion
- extracellular matrix organization
- heart valve morphogenesis
- lens development in camera-type eye
- melanocyte differentiation
- negative regulation of endothelial cell migration
- negative regulation of sprouting angiogenesis
- positive regulation of melanocyte differentiation
- protein transport
- proteolysis
- response to bacterium
- ventricular cardiac muscle tissue development
- vesicle-mediated transport
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
- Peptidase M12B, GON-ADAMTSs
- 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
- GON domain
- ADAMTS cysteine-rich domain 2
- Thrombospondin type 1 domain
- ADAMTS cysteine-rich domain
KeywordsUniProt
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads ADAMTS9 as an antibody target. Whether an autoantibody or antibody against ADAMTS9 could matter depends on whether native ADAMTS9 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
ADAMTS9 is annotated as secreted, so native ADAMTS9 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 ADAMTS9 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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