Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

A disintegrin and metalloproteinase with thrombospondin motifs 5

Gene

Adamts5

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

Functioni

Metalloproteinase that plays an important role in connective tissue organization, development, inflammation, arthritis, and cell migration. ADAMTS5 is an extracellular matrix (ECM) degrading enzyme that show proteolytic activity toward the hyalectan group of chondroitin sulfate proteoglycans (CSPGs) including aggrecan, versican, brevican and neurocan. Cleavage within the hyalectans occurs at Glu-Xaa recognition motifs. Plays a role in embryonic development, including limb and cardiac morphogenesis, and skeletal muscle development through its versican remodeling properties. Participates in the development of brown adipose tissue and browning of white adipose tissue (PubMed:28702327). Plays an important role for T-lymphocyte migration from draining lymph nodes following viral infection (PubMed:27855162).3 Publications

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

Keywordsi

Molecular functionHydrolase, Metalloprotease, Protease
LigandMetal-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1346321 Adamts5

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Disruption phenotypei

ADAMTS5 deficiency is associated with a significant increased mass of brown adipose tissue (PubMed:28702327) although mice are viable and fertile (PubMed:15800625). During viral infection, ADAMTS5 absence leads to a delayed virus clearance and compromised T cell migration (PubMed:27855162).3 Publications

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...) asparagineSequence analysis1
Disulfide bondi508 ↔ 529By similarity
Disulfide bondi514 ↔ 548By similarity
Disulfide bondi542 ↔ 553By similarity
Glycosylationi570C-linked (Man) tryptophanBy similarity1
Glycosylationi573C-linked (Man) tryptophanBy similarity1
Disulfide bondi579 ↔ 616By similarity
Glycosylationi582O-linked (Fuc...) serineBy similarity1
Disulfide bondi583 ↔ 621By similarity
Disulfide bondi594 ↔ 606By similarity
Glycosylationi728N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi802N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi807N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

The precursor is cleaved by furin and PCSK7 outside of the cell.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-X2-(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

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.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IND8 Eukaryota
ENOG410ZQPN LUCA
GeneTreeiENSGT00900000140774
HOGENOMiHOG000004799
HOVERGENiHBG004313
InParanoidiQ9R001
KOiK08620
OMAiNYSGWSH
OrthoDBiEOG091G00AX
TreeFamiTF331949

Family and domain databases

Gene3Di2.20.100.10, 2 hits
3.40.390.10, 1 hit
InterProiView protein in InterPro
IPR006586 ADAM_Cys-rich
IPR010294 ADAM_spacer1
IPR024079 MetalloPept_cat_dom_sf
IPR013276 Pept_M12B_ADAM-TS5
IPR001590 Peptidase_M12B
IPR002870 Peptidase_M12B_N
IPR000884 TSP1_rpt
IPR036383 TSP1_rpt_sf
PfamiView protein in Pfam
PF05986 ADAM_spacer1, 1 hit
PF01562 Pep_M12B_propep, 1 hit
PF01421 Reprolysin, 1 hit
PF00090 TSP_1, 2 hits
PRINTSiPR01860 ADAMTS5
SMARTiView protein in SMART
SM00608 ACR, 1 hit
SM00209 TSP1, 2 hits
SUPFAMiSSF82895 SSF82895, 2 hits
PROSITEiView protein in PROSITE
PS50215 ADAM_MEPRO, 1 hit
PS50092 TSP1, 2 hits
PS00142 ZINC_PROTEASE, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiATS5_MOUSE
AccessioniPrimary (citable) accession number: Q9R001
Secondary accession number(s): B2RRX9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 27, 2011
Last modified: May 23, 2018
This is version 152 of the entry and version 2 of the sequence. See 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

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health