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Q9H324 (ATS10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 10

Short name=ADAM-TS 10
Short name=ADAM-TS10
Short name=ADAMTS-10
EC=3.4.24.-
Gene names
Name:ADAMTS10
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1103 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Metalloprotease that participate in microfibrils assembly. Microfibrils are extracellular matrix components occurring independently or along with elastin in the formation of elastic tissues. Ref.4

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Interacts with FBN1; this interaction promotes microfibrils assembly. Ref.4

Subcellular location

Secretedextracellular spaceextracellular matrix Ref.4.

Tissue specificity

Widely expressed in adult tissues. Ref.2

Domain

The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix By similarity.

Post-translational modification

Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion By similarity.

Involvement in disease

Weill-Marchesani syndrome 1 (WMS1) [MIM:277600]: A rare connective tissue disorder characterized by short stature, brachydactyly, joint stiffness, and eye abnormalities including microspherophakia, ectopia lentis, severe myopia and glaucoma.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.5

Sequence similarities

Contains 1 disintegrin domain.

Contains 1 peptidase M12B domain.

Contains 1 PLAC domain.

Contains 5 TSP type-1 domains.

Ontologies

Keywords
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Dwarfism
   DomainRepeat
Signal
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular matrix

Inferred from direct assay Ref.4. Source: UniProtKB

microfibril

Inferred from direct assay Ref.4. Source: UniProtKB

   Molecular_functionmetalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Propeptide26 – 233208 By similarity
PRO_0000029184
Chain234 – 1103870A disintegrin and metalloproteinase with thrombospondin motifs 10
PRO_0000029185

Regions

Domain239 – 457219Peptidase M12B
Domain460 – 54687Disintegrin
Domain547 – 60256TSP type-1 1
Domain825 – 88359TSP type-1 2
Domain884 – 94562TSP type-1 3
Domain947 – 100155TSP type-1 4
Domain1003 – 105856TSP type-1 5
Domain1065 – 110339PLAC
Region706 – 828123Spacer
Compositional bias58 – 614Poly-Pro
Compositional bias568 – 5714Poly-Ser
Compositional bias604 – 705102Cys-rich

Sites

Active site3931 By similarity
Metal binding3921Zinc; catalytic By similarity
Metal binding3961Zinc; catalytic By similarity
Metal binding4021Zinc; catalytic By similarity

Amino acid modifications

Glycosylation901N-linked (GlcNAc...) Potential
Glycosylation2221N-linked (GlcNAc...) Potential
Glycosylation3231N-linked (GlcNAc...) Potential
Glycosylation7401N-linked (GlcNAc...) Potential
Glycosylation7951N-linked (GlcNAc...) Potential
Glycosylation8921N-linked (GlcNAc...) Potential
Disulfide bond315 ↔ 376 By similarity
Disulfide bond351 ↔ 358 By similarity
Disulfide bond370 ↔ 452 By similarity
Disulfide bond409 ↔ 436 By similarity
Disulfide bond479 ↔ 501 By similarity
Disulfide bond490 ↔ 508 By similarity
Disulfide bond496 ↔ 531 By similarity
Disulfide bond521 ↔ 536 By similarity
Disulfide bond559 ↔ 596 By similarity
Disulfide bond563 ↔ 601 By similarity
Disulfide bond574 ↔ 586 By similarity

Natural variations

Natural variant251A → T in WMS1; shows consistent and significantly diminished protein secretion. Ref.5
VAR_054439
Natural variant1191R → Q.
Corresponds to variant rs3814291 [ dbSNP | Ensembl ].
VAR_054440
Natural variant1341T → S. Ref.2
Corresponds to variant rs7255721 [ dbSNP | Ensembl ].
VAR_054441

Experimental info

Sequence conflict385 – 3862AT → PQ in AAG35563. Ref.2
Sequence conflict4371S → N in AAG35563. Ref.2
Sequence conflict6431C → S in AAG35563. Ref.2
Sequence conflict11011H → Q in AAG35563. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9H324 [UniParc].

Last modified June 12, 2007. Version 2.
Checksum: D7558271C303A87C

FASTA1,103120,874
        10         20         30         40         50         60 
MAPACQILRW ALALGLGLMF EVTHAFRSQD EFLSSLESYE IAFPTRVDHN GALLAFSPPP 

        70         80         90        100        110        120 
PRRQRRGTGA TAESRLFYKV ASPSTHFLLN LTRSSRLLAG HVSVEYWTRE GLAWQRAARP 

       130        140        150        160        170        180 
HCLYAGHLQG QASTSHVAIS TCGGLHGLIV ADEEEYLIEP LHGGPKGSRS PEESGPHVVY 

       190        200        210        220        230        240 
KRSSLRHPHL DTACGVRDEK PWKGRPWWLR TLKPPPARPL GNETERGQPG LKRSVSRERY 

       250        260        270        280        290        300 
VETLVVADKM MVAYHGRRDV EQYVLAIMNI VAKLFQDSSL GSTVNILVTR LILLTEDQPT 

       310        320        330        340        350        360 
LEITHHAGKS LDSFCKWQKS IVNHSGHGNA IPENGVANHD TAVLITRYDI CIYKNKPCGT 

       370        380        390        400        410        420 
LGLAPVGGMC ERERSCSVNE DIGLATAFTI AHEIGHTFGM NHDGVGNSCG ARGQDPAKLM 

       430        440        450        460        470        480 
AAHITMKTNP FVWSSCSRDY ITSFLDSGLG LCLNNRPPRQ DFVYPTVAPG QAYDADEQCR 

       490        500        510        520        530        540 
FQHGVKSRQC KYGEVCSELW CLSKSNRCIT NSIPAAEGTL CQTHTIDKGW CYKRVCVPFG 

       550        560        570        580        590        600 
SRPEGVDGAW GPWTPWGDCS RTCGGGVSSS SRHCDSPRPT IGGKYCLGER RRHRSCNTDD 

       610        620        630        640        650        660 
CPPGSQDFRE VQCSEFDSIP FRGKFYKWKT YRGGGVKACS LTCLAEGFNF YTERAAAVVD 

       670        680        690        700        710        720 
GTPCRPDTVD ICVSGECKHV GCDRVLGSDL REDKCRVCGG DGSACETIEG VFSPASPGAG 

       730        740        750        760        770        780 
YEDVVWIPKG SVHIFIQDLN LSLSHLALKG DQESLLLEGL PGTPQPHRLP LAGTTFQLRQ 

       790        800        810        820        830        840 
GPDQVQSLEA LGPINASLIV MVLARTELPA LRYRFNAPIA RDSLPPYSWH YAPWTKCSAQ 

       850        860        870        880        890        900 
CAGGSQVQAV ECRNQLDSSA VAPHYCSAHS KLPKRQRACN TEPCPPDWVV GNWSLCSRSC 

       910        920        930        940        950        960 
DAGVRSRSVV CQRRVSAAEE KALDDSACPQ PRPPVLEACH GPTCPPEWAA LDWSECTPSC 

       970        980        990       1000       1010       1020 
GPGLRHRVVL CKSADHRATL PPAHCSPAAK PPATMRCNLR RCPPARWVAG EWGECSAQCG 

      1030       1040       1050       1060       1070       1080 
VGQRQRSVRC TSHTGQASHE CTEALRPPTT QQCEAKCDSP TPGDGPEECK DVNKVAYCPL 

      1090       1100 
VLKFQFCSRA YFRQMCCKTC HGH 

« Hide

References

« Hide 'large scale' references
[1]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Discovery and characterization of a novel, widely expressed metalloprotease, ADAMTS10, and its proteolytic activation."
Somerville R.P.T., Jungers K.A., Apte S.S.
J. Biol. Chem. 279:51208-51217(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 27-1103, TISSUE SPECIFICITY, VARIANT SER-134.
[3]"ADAMTS10 mutations in autosomal recessive Weill-Marchesani syndrome."
Dagoneau N., Benoist-Lasselin C., Huber C., Faivre L., Megarbane A., Alswaid A., Dollfus H., Alembik Y., Munnich A., Legeai-Mallet L., Cormier-Daire V.
Am. J. Hum. Genet. 75:801-806(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN WMS1.
[4]"ADAMTS10 protein interacts with fibrillin-1 and promotes its deposition in extracellular matrix of cultured fibroblasts."
Kutz W.E., Wang L.W., Bader H.L., Majors A.K., Iwata K., Traboulsi E.I., Sakai L.Y., Keene D.R., Apte S.S.
J. Biol. Chem. 286:17156-17167(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FBN1.
[5]"Functional analysis of an ADAMTS10 signal peptide mutation in Weill-Marchesani syndrome demonstrates a long-range effect on secretion of the full-length enzyme."
Kutz W.E., Wang L.W., Dagoneau N., Odrcic K.J., Cormier-Daire V., Traboulsi E.I., Apte S.S.
Hum. Mutat. 29:1425-1434(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT WMS1 THR-25, CHARACTERIZATION OF VARIANT WMS1 THR-25.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC092315 Genomic DNA. No translation available.
AC130469 Genomic DNA. No translation available.
AF163762 mRNA. Translation: AAG35563.1.
RefSeqNP_001269281.1. NM_001282352.1.
NP_112219.3. NM_030957.3.
UniGeneHs.657508.

3D structure databases

ProteinModelPortalQ9H324.
SMRQ9H324. Positions 236-805.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123586. 7 interactions.
IntActQ9H324. 7 interactions.
MINTMINT-8247349.
STRING9606.ENSP00000270328.

Protein family/group databases

MEROPSM12.235.

PTM databases

PhosphoSiteQ9H324.

Polymorphism databases

DMDM148887344.

Proteomic databases

PaxDbQ9H324.
PRIDEQ9H324.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000270328; ENSP00000270328; ENSG00000142303.
ENST00000597188; ENSP00000471851; ENSG00000142303.
GeneID81794.
KEGGhsa:81794.
UCSCuc002mkj.1. human.

Organism-specific databases

CTD81794.
GeneCardsGC19M008645.
HGNCHGNC:13201. ADAMTS10.
HPAHPA040223.
MIM277600. phenotype.
608990. gene.
neXtProtNX_Q9H324.
Orphanet3449. Weill-Marchesani syndrome.
PharmGKBPA24537.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG288089.
HOGENOMHOG000004800.
HOVERGENHBG004315.
InParanoidQ9H324.
KOK08625.
OMALENYEIA.
PhylomeDBQ9H324.
TreeFamTF313537.

Gene expression databases

ArrayExpressQ9H324.
BgeeQ9H324.
CleanExHS_ADAMTS10.
GenevestigatorQ9H324.

Family and domain databases

Gene3D3.40.390.10. 1 hit.
InterProIPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR010909. PLAC.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamPF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF08686. PLAC. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 5 hits.
[Graphical view]
PRINTSPR01857. ADAMTSFAMILY.
SMARTSM00209. TSP1. 5 hits.
[Graphical view]
SUPFAMSSF82895. SSF82895. 5 hits.
PROSITEPS50215. ADAM_MEPRO. 1 hit.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 5 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiADAMTS10.
GenomeRNAi81794.
NextBio72110.
PROQ9H324.
SOURCESearch...

Entry information

Entry nameATS10_HUMAN
AccessionPrimary (citable) accession number: Q9H324
Entry history
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: June 12, 2007
Last modified: April 16, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM