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Q9R001

- ATS5_MOUSE

UniProt

Q9R001 - ATS5_MOUSE

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Protein

A disintegrin and metalloproteinase with thrombospondin motifs 5

Gene

Adamts5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

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 activityi

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

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi209 – 2091Zinc; in inhibited formBy similarity
Metal bindingi410 – 4101Zinc; catalyticBy similarity
Active sitei411 – 4111PROSITE-ProRule annotation
Metal bindingi414 – 4141Zinc; catalyticBy similarity
Metal bindingi420 – 4201Zinc; catalyticBy similarity

GO - Molecular functioni

  1. metalloendopeptidase activity Source: InterPro
  2. metallopeptidase activity Source: MGI
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. defense response to bacterium Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_199052. Degradation of the extracellular matrix.
REACT_211817. O-glycosylation of TSR domain-containing proteins.

Protein family/group databases

MEROPSiM12.225.

Names & Taxonomyi

Protein namesi
Recommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 5 (EC:3.4.24.-)
Short name:
ADAM-TS 5
Short name:
ADAM-TS5
Short name:
ADAMTS-5
Alternative name(s):
ADMP-2
Aggrecanase-2
Implantin
Gene namesi
Name:Adamts5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 16

Organism-specific databases

MGIiMGI:1346321. Adamts5.

Subcellular locationi

GO - Cellular componenti

  1. proteinaceous extracellular matrix Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Propeptidei22 – 261240Sequence AnalysisPRO_0000029172Add
BLAST
Chaini262 – 930669A disintegrin and metalloproteinase with thrombospondin motifs 5PRO_0000029173Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi342 ↔ 394By similarity
Disulfide bondi371 ↔ 376By similarity
Disulfide bondi388 ↔ 471By similarity
Disulfide bondi426 ↔ 455By similarity
Disulfide bondi497 ↔ 519By similarity
Glycosylationi498 – 4981N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi508 ↔ 529By similarity
Disulfide bondi514 ↔ 548By similarity
Disulfide bondi542 ↔ 553By similarity
Glycosylationi570 – 5701C-linked (Man)By similarity
Glycosylationi573 – 5731C-linked (Man)By similarity
Disulfide bondi579 ↔ 616By similarity
Glycosylationi582 – 5821O-linked (Fuc...)By similarity
Disulfide bondi583 ↔ 621By similarity
Disulfide bondi594 ↔ 606By similarity
Glycosylationi728 – 7281N-linked (GlcNAc...)Sequence Analysis
Glycosylationi802 – 8021N-linked (GlcNAc...)Sequence Analysis
Glycosylationi807 – 8071N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

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).By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PRIDEiQ9R001.

PTM databases

PhosphoSiteiQ9R001.

Expressioni

Developmental stagei

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

Gene expression databases

BgeeiQ9R001.
ExpressionAtlasiQ9R001. baseline and differential.
GenevestigatoriQ9R001.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000023611.

Structurei

3D structure databases

ProteinModelPortaliQ9R001.
SMRiQ9R001. Positions 264-797.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini267 – 476210Peptidase M12BPROSITE-ProRule annotationAdd
BLAST
Domaini485 – 56682DisintegrinAdd
BLAST
Domaini567 – 62256TSP type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini875 – 92955TSP type-1 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni732 – 874143SpacerAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi207 – 2148Cysteine switchBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi41 – 466Poly-Ala
Compositional biasi257 – 2615Poly-Arg
Compositional biasi624 – 731108Cys-richAdd
BLAST

Domaini

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.

Sequence similaritiesi

Contains 1 disintegrin domain.Curated
Contains 1 peptidase M12B domain.PROSITE-ProRule annotation
Contains 2 TSP type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG302522.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000004799.
HOVERGENiHBG004313.
InParanoidiQ9R001.
KOiK08620.
OMAiRASCETP.
OrthoDBiEOG7WDN1M.
TreeFamiTF331949.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR010294. 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]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 2 hits.
[Graphical view]
PRINTSiPR01860. ADAMTS5.
PR01857. ADAMTSFAMILY.
SMARTiSM00209. TSP1. 2 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 2 hits.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50092. TSP1. 2 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9R001-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRLEWAPLLL LLLLLSASCL SLAADSPAAA PAQDKTRQPQ AAAAAAEPDQ
60 70 80 90 100
PQGEETRERG HLQPLAGQRR SGGLVQNIDQ LYSGGGKVGY LVYAGGRRFL
110 120 130 140 150
LDLERDDTVG AAGSIVTAGG GLSASSGHRG HCFYRGTVDG SPRSLAVFDL
160 170 180 190 200
CGGLDGFFAV KHARYTLKPL LRGSWAEYER IYGDGSSRIL HVYNREGFSF
210 220 230 240 250
EALPPRASCE TPASPSGPQE SPSVHSRSRR RSALAPQLLD HSAFSPSGNA
260 270 280 290 300
GPQTWWRRRR RSISRARQVE LLLVADSSMA RMYGRGLQHY LLTLASIANR
310 320 330 340 350
LYSHASIENH IRLAVVKVVV LTDKDTSLEV SKNAATTLKN FCKWQHQHNQ
360 370 380 390 400
LGDDHEEHYD AAILFTREDL CGHHSCDTLG MADVGTICSP ERSCAVIEDD
410 420 430 440 450
GLHAAFTVAH EIGHLLGLSH DDSKFCEENF GTTEDKRLMS SILTSIDASK
460 470 480 490 500
PWSKCTSATI TEFLDDGHGN CLLDLPRKQI LGPEELPGQT YDATQQCNLT
510 520 530 540 550
FGPEYSVCPG MDVCARLWCA VVRQGQMVCL TKKLPAVEGT PCGKGRVCLQ
560 570 580 590 600
GKCVDKTKKK YYSTSSHGNW GSWGPWGQCS RSCGGGVQFA YRHCNNPAPR
610 620 630 640 650
NSGRYCTGKR AIYRSCSVTP CPPNGKSFRH EQCEAKNGYQ SDAKGVKTFV
660 670 680 690 700
EWVPKYAGVL PADVCKLTCR AKGTGYYVVF SPKVTDGTEC RPYSNSVCVR
710 720 730 740 750
GRCVRTGCDG IIGSKLQYDK CGVCGGDNSS CTKIIGTFNK KSKGYTDVVR
760 770 780 790 800
IPEGATHIKV RQFKAKDQTR FTAYLALKKK TGEYLINGKY MISTSETIID
810 820 830 840 850
INGTVMNYSG WSHRDDFLHG MGYSATKEIL IVQILATDPT KALDVRYSFF
860 870 880 890 900
VPKKTTQKVN SVISHGSNKV GPHSTQLQWV TGPWLACSRT CDTGWHTRTV
910 920 930
QCQDGNRKLA KGCLLSQRPS AFKQCLLKKC
Length:930
Mass (Da):101,844
Last modified:July 27, 2011 - v2
Checksum:i0CF1B264C782FF49
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71P → S in AAD56356. (PubMed:10464288)Curated
Sequence conflicti76 – 761Q → H in AAD56356. (PubMed:10464288)Curated
Sequence conflicti772 – 7721T → P in AAD56356. (PubMed:10464288)Curated
Sequence conflicti844 – 8441D → G in AAD56356. (PubMed:10464288)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF140673 mRNA. Translation: AAD56356.1.
BC138619 mRNA. Translation: AAI38620.1.
BC138620 mRNA. Translation: AAI38621.1.
CCDSiCCDS28288.1.
RefSeqiNP_035912.2. NM_011782.2.
UniGeneiMm.112933.
Mm.437478.

Genome annotation databases

EnsembliENSMUST00000023611; ENSMUSP00000023611; ENSMUSG00000022894.
GeneIDi23794.
KEGGimmu:23794.
UCSCiuc007ztw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF140673 mRNA. Translation: AAD56356.1 .
BC138619 mRNA. Translation: AAI38620.1 .
BC138620 mRNA. Translation: AAI38621.1 .
CCDSi CCDS28288.1.
RefSeqi NP_035912.2. NM_011782.2.
UniGenei Mm.112933.
Mm.437478.

3D structure databases

ProteinModelPortali Q9R001.
SMRi Q9R001. Positions 264-797.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000023611.

Protein family/group databases

MEROPSi M12.225.

PTM databases

PhosphoSitei Q9R001.

Proteomic databases

PRIDEi Q9R001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000023611 ; ENSMUSP00000023611 ; ENSMUSG00000022894 .
GeneIDi 23794.
KEGGi mmu:23794.
UCSCi uc007ztw.1. mouse.

Organism-specific databases

CTDi 11096.
MGIi MGI:1346321. Adamts5.

Phylogenomic databases

eggNOGi NOG302522.
GeneTreei ENSGT00760000118880.
HOGENOMi HOG000004799.
HOVERGENi HBG004313.
InParanoidi Q9R001.
KOi K08620.
OMAi RASCETP.
OrthoDBi EOG7WDN1M.
TreeFami TF331949.

Enzyme and pathway databases

Reactomei REACT_199052. Degradation of the extracellular matrix.
REACT_211817. O-glycosylation of TSR domain-containing proteins.

Miscellaneous databases

NextBioi 303403.
PROi Q9R001.
SOURCEi Search...

Gene expression databases

Bgeei Q9R001.
ExpressionAtlasi Q9R001. baseline and differential.
Genevestigatori Q9R001.

Family and domain databases

Gene3Di 3.40.390.10. 1 hit.
InterProi IPR010294. 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 ]
Pfami PF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 2 hits.
[Graphical view ]
PRINTSi PR01860. ADAMTS5.
PR01857. ADAMTSFAMILY.
SMARTi SM00209. TSP1. 2 hits.
[Graphical view ]
SUPFAMi SSF82895. SSF82895. 2 hits.
PROSITEi PS50215. ADAM_MEPRO. 1 hit.
PS50092. TSP1. 2 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiATS5_MOUSE
AccessioniPrimary (citable) accession number: Q9R001
Secondary accession number(s): B2RRX9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3