UniProtKB - Q9R001 (ATS5_MOUSE)
Protein
A disintegrin and metalloproteinase with thrombospondin motifs 5
Gene
Adamts5
Organism
Mus musculus (Mouse)
Status
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 209 | Zinc; in inhibited formBy similarity | 1 | |
Metal bindingi | 410 | Zinc; catalyticBy similarity | 1 | |
Active sitei | 411 | PROSITE-ProRule annotation | 1 | |
Metal bindingi | 414 | Zinc; catalyticBy similarity | 1 | |
Metal bindingi | 420 | Zinc; catalyticBy similarity | 1 |
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
- negative regulation of cold-induced thermogenesis Source: YuBioLab
- tooth eruption Source: Ensembl
Keywordsi
Molecular function | Hydrolase, Metalloprotease, Protease |
Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
BRENDAi | 3.4.24.B12 3474 |
Reactomei | R-MMU-1474228 Degradation of the extracellular matrix R-MMU-5173214 O-glycosylation of TSR domain-containing proteins |
Protein family/group databases
MEROPSi | M12.225 |
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 |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:1346321 Adamts5 |
Subcellular locationi
Extracellular region or secreted
- extracellular matrix By similarity
Extracellular region or secreted
- collagen-containing extracellular matrix Source: InterPro
- extracellular space Source: MGI
Keywords - Cellular componenti
Extracellular matrix, SecretedPathology & 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 21 | Sequence analysisAdd BLAST | 21 | |
PropeptideiPRO_0000029172 | 22 – 261 | Sequence analysisAdd BLAST | 240 | |
ChainiPRO_0000029173 | 262 – 930 | A disintegrin and metalloproteinase with thrombospondin motifs 5Add BLAST | 669 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 342 ↔ 394 | By similarity | ||
Disulfide bondi | 371 ↔ 376 | By similarity | ||
Disulfide bondi | 388 ↔ 471 | By similarity | ||
Disulfide bondi | 426 ↔ 455 | By similarity | ||
Disulfide bondi | 497 ↔ 519 | By similarity | ||
Glycosylationi | 498 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 508 ↔ 529 | By similarity | ||
Disulfide bondi | 514 ↔ 548 | By similarity | ||
Disulfide bondi | 542 ↔ 553 | By similarity | ||
Glycosylationi | 570 | C-linked (Man) tryptophanBy similarity | 1 | |
Glycosylationi | 573 | C-linked (Man) tryptophanBy similarity | 1 | |
Disulfide bondi | 579 ↔ 616 | By similarity | ||
Glycosylationi | 582 | O-linked (Fuc...) serineBy similarity | 1 | |
Disulfide bondi | 583 ↔ 621 | By similarity | ||
Disulfide bondi | 594 ↔ 606 | By similarity | ||
Glycosylationi | 728 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 802 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 807 | N-linked (GlcNAc...) asparagineSequence analysis | 1 |
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, ZymogenProteomic databases
MaxQBi | Q9R001 |
PaxDbi | Q9R001 |
PeptideAtlasi | Q9R001 |
PRIDEi | Q9R001 |
PTM databases
PhosphoSitePlusi | Q9R001 |
Expressioni
Developmental stagei
Expressed specifically in the peri-implantation period in embryo and trophoblast and at low or undetectable level thereafter.
Gene expression databases
Bgeei | ENSMUSG00000022894 Expressed in 275 organ(s), highest expression level in decidua |
Genevisiblei | Q9R001 MM |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 267 – 476 | Peptidase M12BPROSITE-ProRule annotationAdd BLAST | 210 | |
Domaini | 485 – 566 | DisintegrinAdd BLAST | 82 | |
Domaini | 567 – 622 | TSP type-1 1PROSITE-ProRule annotationAdd BLAST | 56 | |
Domaini | 875 – 929 | TSP type-1 2PROSITE-ProRule annotationAdd BLAST | 55 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 732 – 874 | SpacerAdd BLAST | 143 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 207 – 214 | Cysteine switchBy similarity | 8 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 41 – 46 | Poly-Ala | 6 | |
Compositional biasi | 257 – 261 | Poly-Arg | 5 | |
Compositional biasi | 624 – 731 | Cys-richAdd BLAST | 108 |
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, SignalPhylogenomic databases
eggNOGi | ENOG410IND8 Eukaryota ENOG410ZQPN LUCA |
GeneTreei | ENSGT00940000159090 |
HOGENOMi | HOG000004799 |
InParanoidi | Q9R001 |
KOi | K08620 |
OMAi | SFRQEQC |
OrthoDBi | 125522at2759 |
TreeFami | TF331949 |
Family and domain databases
Gene3Di | 2.20.100.10, 2 hits 3.40.390.10, 1 hit |
InterProi | View protein in InterPro IPR041645 ADAM_CR_2 IPR006586 ADAM_Cys-rich IPR010294 ADAM_spacer1 IPR013273 ADAMTS/ADAMTS-like IPR024079 MetalloPept_cat_dom_sf IPR013276 Pept_M12B_ADAM-TS5 IPR001590 Peptidase_M12B IPR002870 Peptidase_M12B_N IPR000884 TSP1_rpt IPR036383 TSP1_rpt_sf |
Pfami | View protein in Pfam PF17771 ADAM_CR_2, 1 hit PF05986 ADAM_spacer1, 1 hit PF01562 Pep_M12B_propep, 1 hit PF01421 Reprolysin, 1 hit PF00090 TSP_1, 2 hits |
PRINTSi | PR01860 ADAMTS5 PR01857 ADAMTSFAMILY |
SMARTi | View protein in SMART SM00608 ACR, 1 hit SM00209 TSP1, 2 hits |
SUPFAMi | SSF82895 SSF82895, 2 hits |
PROSITEi | View protein in PROSITE PS50215 ADAM_MEPRO, 1 hit PS50092 TSP1, 2 hits PS00142 ZINC_PROTEASE, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
Q9R001-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 7 | P → S in AAD56356 (PubMed:10464288).Curated | 1 | |
Sequence conflicti | 76 | Q → H in AAD56356 (PubMed:10464288).Curated | 1 | |
Sequence conflicti | 772 | T → P in AAD56356 (PubMed:10464288).Curated | 1 | |
Sequence conflicti | 844 | D → G in AAD56356 (PubMed:10464288).Curated | 1 |
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 |
Genome annotation databases
Ensembli | ENSMUST00000023611; ENSMUSP00000023611; ENSMUSG00000022894 |
GeneIDi | 23794 |
KEGGi | mmu:23794 |
UCSCi | uc007ztw.1 mouse |
Similar proteinsi
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 |
3D structure databases
SMRi | Q9R001 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 10090.ENSMUSP00000023611 |
Protein family/group databases
MEROPSi | M12.225 |
PTM databases
PhosphoSitePlusi | Q9R001 |
Proteomic databases
MaxQBi | Q9R001 |
PaxDbi | Q9R001 |
PeptideAtlasi | Q9R001 |
PRIDEi | Q9R001 |
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 | ENOG410IND8 Eukaryota ENOG410ZQPN LUCA |
GeneTreei | ENSGT00940000159090 |
HOGENOMi | HOG000004799 |
InParanoidi | Q9R001 |
KOi | K08620 |
OMAi | SFRQEQC |
OrthoDBi | 125522at2759 |
TreeFami | TF331949 |
Enzyme and pathway databases
BRENDAi | 3.4.24.B12 3474 |
Reactomei | R-MMU-1474228 Degradation of the extracellular matrix R-MMU-5173214 O-glycosylation of TSR domain-containing proteins |
Miscellaneous databases
ChiTaRSi | Adamts5 mouse |
PROi | PR:Q9R001 |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000022894 Expressed in 275 organ(s), highest expression level in decidua |
Genevisiblei | Q9R001 MM |
Family and domain databases
Gene3Di | 2.20.100.10, 2 hits 3.40.390.10, 1 hit |
InterProi | View protein in InterPro IPR041645 ADAM_CR_2 IPR006586 ADAM_Cys-rich IPR010294 ADAM_spacer1 IPR013273 ADAMTS/ADAMTS-like IPR024079 MetalloPept_cat_dom_sf IPR013276 Pept_M12B_ADAM-TS5 IPR001590 Peptidase_M12B IPR002870 Peptidase_M12B_N IPR000884 TSP1_rpt IPR036383 TSP1_rpt_sf |
Pfami | View protein in Pfam PF17771 ADAM_CR_2, 1 hit PF05986 ADAM_spacer1, 1 hit PF01562 Pep_M12B_propep, 1 hit PF01421 Reprolysin, 1 hit PF00090 TSP_1, 2 hits |
PRINTSi | PR01860 ADAMTS5 PR01857 ADAMTSFAMILY |
SMARTi | View protein in SMART SM00608 ACR, 1 hit SM00209 TSP1, 2 hits |
SUPFAMi | SSF82895 SSF82895, 2 hits |
PROSITEi | View protein in PROSITE PS50215 ADAM_MEPRO, 1 hit PS50092 TSP1, 2 hits PS00142 ZINC_PROTEASE, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | ATS5_MOUSE | |
Accessioni | Q9R001Primary (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: | October 16, 2019 | |
This is version 160 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Complete proteome, Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot