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Q9R001 (ATS5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 5

Short name=ADAM-TS 5
Short name=ADAM-TS5
Short name=ADAMTS-5
EC=3.4.24.-
Alternative name(s):
ADMP-2
Aggrecanase-2
Implantin
Gene names
Name:Adamts5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length930 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover. May play an important role in the destruction of aggrecan in arthritic diseases. May play a role in proteolytic processing mostly during the peri-implantation period.

Catalytic activity

Cleaves aggrecan at the 392-Glu-|-Ala-393 site.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Developmental stage

Expressed specifically in the peri-implantation period in embryo and trophoblast and at low or undetectable level thereafter.

Domain

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

The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

Post-translational modification

The precursor is cleaved by a furin endopeptidase By similarity.

C- and O-glycosylated By similarity. 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 can mediate the efficient secretion of ADAMTS family members. 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.

Sequence similarities

Contains 1 disintegrin domain.

Contains 1 peptidase M12B domain.

Contains 2 TSP type-1 domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Propeptide22 – 261240 Potential
PRO_0000029172
Chain262 – 930669A disintegrin and metalloproteinase with thrombospondin motifs 5
PRO_0000029173

Regions

Domain267 – 476210Peptidase M12B
Domain485 – 56682Disintegrin
Domain567 – 62256TSP type-1 1
Domain875 – 92955TSP type-1 2
Region732 – 874143Spacer
Motif207 – 2148Cysteine switch By similarity
Compositional bias41 – 466Poly-Ala
Compositional bias257 – 2615Poly-Arg
Compositional bias624 – 731108Cys-rich

Sites

Active site4111 By similarity
Metal binding2091Zinc; in inhibited form By similarity
Metal binding4101Zinc; catalytic By similarity
Metal binding4141Zinc; catalytic By similarity
Metal binding4201Zinc; catalytic By similarity

Amino acid modifications

Glycosylation4981N-linked (GlcNAc...) Potential
Glycosylation5701C-linked (Man) By similarity
Glycosylation5731C-linked (Man) By similarity
Glycosylation5821O-linked (Fuc...) By similarity
Glycosylation7281N-linked (GlcNAc...) Potential
Glycosylation8021N-linked (GlcNAc...) Potential
Glycosylation8071N-linked (GlcNAc...) Potential
Disulfide bond342 ↔ 394 By similarity
Disulfide bond371 ↔ 376 By similarity
Disulfide bond388 ↔ 471 By similarity
Disulfide bond426 ↔ 455 By similarity
Disulfide bond497 ↔ 519 By similarity
Disulfide bond508 ↔ 529 By similarity
Disulfide bond514 ↔ 548 By similarity
Disulfide bond542 ↔ 553 By similarity
Disulfide bond579 ↔ 616 By similarity
Disulfide bond583 ↔ 621 By similarity
Disulfide bond594 ↔ 606 By similarity

Experimental info

Sequence conflict71P → S in AAD56356. Ref.1
Sequence conflict761Q → H in AAD56356. Ref.1
Sequence conflict7721T → P in AAD56356. Ref.1
Sequence conflict8441D → G in AAD56356. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9R001 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 0CF1B264C782FF49

FASTA930101,844
        10         20         30         40         50         60 
MRLEWAPLLL LLLLLSASCL SLAADSPAAA PAQDKTRQPQ AAAAAAEPDQ PQGEETRERG 

        70         80         90        100        110        120 
HLQPLAGQRR SGGLVQNIDQ LYSGGGKVGY LVYAGGRRFL LDLERDDTVG AAGSIVTAGG 

       130        140        150        160        170        180 
GLSASSGHRG HCFYRGTVDG SPRSLAVFDL CGGLDGFFAV KHARYTLKPL LRGSWAEYER 

       190        200        210        220        230        240 
IYGDGSSRIL HVYNREGFSF EALPPRASCE TPASPSGPQE SPSVHSRSRR RSALAPQLLD 

       250        260        270        280        290        300 
HSAFSPSGNA GPQTWWRRRR RSISRARQVE LLLVADSSMA RMYGRGLQHY LLTLASIANR 

       310        320        330        340        350        360 
LYSHASIENH IRLAVVKVVV LTDKDTSLEV SKNAATTLKN FCKWQHQHNQ LGDDHEEHYD 

       370        380        390        400        410        420 
AAILFTREDL CGHHSCDTLG MADVGTICSP ERSCAVIEDD GLHAAFTVAH EIGHLLGLSH 

       430        440        450        460        470        480 
DDSKFCEENF GTTEDKRLMS SILTSIDASK PWSKCTSATI TEFLDDGHGN CLLDLPRKQI 

       490        500        510        520        530        540 
LGPEELPGQT YDATQQCNLT FGPEYSVCPG MDVCARLWCA VVRQGQMVCL TKKLPAVEGT 

       550        560        570        580        590        600 
PCGKGRVCLQ GKCVDKTKKK YYSTSSHGNW GSWGPWGQCS RSCGGGVQFA YRHCNNPAPR 

       610        620        630        640        650        660 
NSGRYCTGKR AIYRSCSVTP CPPNGKSFRH EQCEAKNGYQ SDAKGVKTFV EWVPKYAGVL 

       670        680        690        700        710        720 
PADVCKLTCR AKGTGYYVVF SPKVTDGTEC RPYSNSVCVR GRCVRTGCDG IIGSKLQYDK 

       730        740        750        760        770        780 
CGVCGGDNSS CTKIIGTFNK KSKGYTDVVR IPEGATHIKV RQFKAKDQTR FTAYLALKKK 

       790        800        810        820        830        840 
TGEYLINGKY MISTSETIID INGTVMNYSG WSHRDDFLHG MGYSATKEIL IVQILATDPT 

       850        860        870        880        890        900 
KALDVRYSFF VPKKTTQKVN SVISHGSNKV GPHSTQLQWV TGPWLACSRT CDTGWHTRTV 

       910        920        930 
QCQDGNRKLA KGCLLSQRPS AFKQCLLKKC 

« Hide

References

« Hide 'large scale' references
[1]"ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases."
Hurskainen T.L., Hirohata S., Seldin M.F., Apte S.S.
J. Biol. Chem. 274:25555-25563(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF140673 mRNA. Translation: AAD56356.1.
BC138619 mRNA. Translation: AAI38620.1.
BC138620 mRNA. Translation: AAI38621.1.
RefSeqNP_035912.2. NM_011782.2.
UniGeneMm.112933.
Mm.437478.

3D structure databases

ProteinModelPortalQ9R001.
SMRQ9R001. Positions 264-854, 876-930.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000023611.

Protein family/group databases

MEROPSM12.225.

PTM databases

PhosphoSiteQ9R001.

Proteomic databases

PRIDEQ9R001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023611; ENSMUSP00000023611; ENSMUSG00000022894.
GeneID23794.
KEGGmmu:23794.
UCSCuc007ztw.1. mouse.

Organism-specific databases

CTD11096.
MGIMGI:1346321. Adamts5.

Phylogenomic databases

eggNOGNOG302522.
GeneTreeENSGT00650000092972.
HOGENOMHOG000004799.
HOVERGENHBG004313.
InParanoidB2RRX9.
KOK08620.
OMARASCETP.
OrthoDBEOG7WDN1M.
TreeFamTF331949.

Gene expression databases

ArrayExpressQ9R001.
BgeeQ9R001.
GenevestigatorQ9R001.

Family and domain databases

Gene3D3.40.390.10. 1 hit.
InterProIPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR013276. Pept_M12B_ADAM-TS5.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamPF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 2 hits.
[Graphical view]
PRINTSPR01860. ADAMTS5.
PR01857. ADAMTSFAMILY.
SMARTSM00209. TSP1. 2 hits.
[Graphical view]
SUPFAMSSF82895. SSF82895. 2 hits.
PROSITEPS50215. ADAM_MEPRO. 1 hit.
PS50092. TSP1. 2 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio303403.
PROQ9R001.
SOURCESearch...

Entry information

Entry nameATS5_MOUSE
AccessionPrimary (citable) accession number: Q9R001
Secondary accession number(s): B2RRX9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 27, 2011
Last modified: March 19, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot