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Protein

A disintegrin and metalloproteinase with thrombospondin motifs 5

Gene

Adamts5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Metal bindingi209Zinc; in inhibited formBy similarity1
Metal bindingi410Zinc; catalyticBy similarity1
Active sitei411PROSITE-ProRule annotation1
Metal bindingi414Zinc; catalyticBy similarity1
Metal bindingi420Zinc; catalyticBy similarity1

GO - Molecular functioni

  • extracellular matrix binding Source: MGI
  • heparin binding Source: MGI
  • metalloendopeptidase activity Source: InterPro
  • metallopeptidase activity Source: MGI
  • zinc ion binding Source: InterPro

GO - Biological processi

  • defense response to bacterium Source: MGI
  • tooth eruption Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.24.B12. 3474.
ReactomeiR-MMU-1474228. Degradation of the extracellular matrix.
R-MMU-5173214. 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
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1346321. Adamts5.

Subcellular locationi

GO - Cellular componenti

  • extracellular space Source: MGI
  • proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
PropeptideiPRO_000002917222 – 261Sequence analysisAdd BLAST240
ChainiPRO_0000029173262 – 930A disintegrin and metalloproteinase with thrombospondin motifs 5Add BLAST669

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi342 ↔ 394By similarity
Disulfide bondi371 ↔ 376By similarity
Disulfide bondi388 ↔ 471By similarity
Disulfide bondi426 ↔ 455By similarity
Disulfide bondi497 ↔ 519By similarity
Glycosylationi498N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi508 ↔ 529By similarity
Disulfide bondi514 ↔ 548By similarity
Disulfide bondi542 ↔ 553By similarity
Glycosylationi570C-linked (Man)By similarity1
Glycosylationi573C-linked (Man)By similarity1
Disulfide bondi579 ↔ 616By similarity
Glycosylationi582O-linked (Fuc...)By similarity1
Disulfide bondi583 ↔ 621By similarity
Disulfide bondi594 ↔ 606By similarity
Glycosylationi728N-linked (GlcNAc...)Sequence analysis1
Glycosylationi802N-linked (GlcNAc...)Sequence analysis1
Glycosylationi807N-linked (GlcNAc...)Sequence analysis1

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

MaxQBiQ9R001.
PaxDbiQ9R001.
PeptideAtlasiQ9R001.
PRIDEiQ9R001.

PTM databases

PhosphoSitePlusiQ9R001.

Expressioni

Developmental stagei

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

Gene expression databases

BgeeiENSMUSG00000022894.
GenevisibleiQ9R001. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000023611.

Structurei

3D structure databases

ProteinModelPortaliQ9R001.
SMRiQ9R001.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini267 – 476Peptidase M12BPROSITE-ProRule annotationAdd BLAST210
Domaini485 – 566DisintegrinAdd BLAST82
Domaini567 – 622TSP type-1 1PROSITE-ProRule annotationAdd BLAST56
Domaini875 – 929TSP type-1 2PROSITE-ProRule annotationAdd BLAST55

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni732 – 874SpacerAdd BLAST143

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi207 – 214Cysteine switchBy similarity8

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi41 – 46Poly-Ala6
Compositional biasi257 – 261Poly-Arg5
Compositional biasi624 – 731Cys-richAdd BLAST108

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

eggNOGiENOG410IND8. Eukaryota.
ENOG410ZQPN. LUCA.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000004799.
HOVERGENiHBG004313.
InParanoidiQ9R001.
KOiK08620.
OMAiRASCETP.
OrthoDBiEOG091G00AX.
TreeFamiTF331949.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR006586. ADAM_Cys-rich.
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. TSP1_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.
SMARTiSM00608. ACR. 1 hit.
SM00209. 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)DescriptionActionsGraphical viewLength
Sequence conflicti7P → S in AAD56356 (PubMed:10464288).Curated1
Sequence conflicti76Q → H in AAD56356 (PubMed:10464288).Curated1
Sequence conflicti772T → P in AAD56356 (PubMed:10464288).Curated1
Sequence conflicti844D → G in AAD56356 (PubMed:10464288).Curated1

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.
CCDSiCCDS28288.1.
RefSeqiNP_035912.2. NM_011782.2.
UniGeneiMm.112933.
Mm.437478.

3D structure databases

ProteinModelPortaliQ9R001.
SMRiQ9R001.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000023611.

Protein family/group databases

MEROPSiM12.225.

PTM databases

PhosphoSitePlusiQ9R001.

Proteomic databases

MaxQBiQ9R001.
PaxDbiQ9R001.
PeptideAtlasiQ9R001.
PRIDEiQ9R001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi11096.
MGIiMGI:1346321. Adamts5.

Phylogenomic databases

eggNOGiENOG410IND8. Eukaryota.
ENOG410ZQPN. LUCA.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000004799.
HOVERGENiHBG004313.
InParanoidiQ9R001.
KOiK08620.
OMAiRASCETP.
OrthoDBiEOG091G00AX.
TreeFamiTF331949.

Enzyme and pathway databases

BRENDAi3.4.24.B12. 3474.
ReactomeiR-MMU-1474228. Degradation of the extracellular matrix.
R-MMU-5173214. O-glycosylation of TSR domain-containing proteins.

Miscellaneous databases

PROiQ9R001.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000022894.
GenevisibleiQ9R001. MM.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR006586. ADAM_Cys-rich.
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. TSP1_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.
SMARTiSM00608. ACR. 1 hit.
SM00209. 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]
ProtoNetiSearch...

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 2, 2016
This is version 144 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.