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A disintegrin and metalloproteinase with thrombospondin motifs 5 (ADAM-TS 5) (ADAM-TS5) (ADAMTS-5) (EC 3.4.24.-) (ADMP-2) (Aggrecanase-2) (Implantin)

 ATS5_MOUSE              Reviewed;         930 AA.
Q9R001; B2RRX9;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
12-SEP-2018, entry version 155.
RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 5;
Short=ADAM-TS 5;
Short=ADAM-TS5;
Short=ADAMTS-5;
EC=3.4.24.-;
AltName: Full=ADMP-2;
AltName: Full=Aggrecanase-2;
AltName: Full=Implantin;
Flags: Precursor;
Name=Adamts5;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10464288; DOI=10.1074/jbc.274.36.25555;
Hurskainen T.L., Hirohata S., Seldin M.F., Apte S.S.;
"ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of
zinc metalloproteases.";
J. Biol. Chem. 274:25555-25563(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15800625; DOI=10.1038/nature03417;
Stanton H., Rogerson F.M., East C.J., Golub S.B., Lawlor K.E.,
Meeker C.T., Little C.B., Last K., Farmer P.J., Campbell I.K.,
Fourie A.M., Fosang A.J.;
"ADAMTS5 is the major aggrecanase in mouse cartilage in vivo and in
vitro.";
Nature 434:648-652(2005).
[4]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=27855162; DOI=10.1371/journal.pbio.1002580;
McMahon M., Ye S., Izzard L., Dlugolenski D., Tripp R.A., Bean A.G.,
McCulloch D.R., Stambas J.;
"ADAMTS5 is a critical regulator of virus-specific T cell immunity.";
PLoS Biol. 14:E1002580-E1002580(2016).
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=28702327; DOI=10.1016/j.molmet.2017.05.004;
Bauters D., Cobbaut M., Geys L., Van Lint J., Hemmeryckx B.,
Lijnen H.R.;
"Loss of ADAMTS5 enhances brown adipose tissue mass and promotes
browning of white adipose tissue via CREB signaling.";
Mol. Metab. 6:715-724(2017).
-!- FUNCTION: 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). {ECO:0000269|PubMed:15800625,
ECO:0000269|PubMed:27855162, ECO:0000269|PubMed:28702327}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:Q9UNA0};
Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9UNA0};
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000250|UniProtKB:Q9UNA0}.
-!- 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.
-!- DOMAIN: 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.
-!- PTM: The precursor is cleaved by furin and PCSK7 outside of the
cell. {ECO:0000250|UniProtKB:Q9UNA0}.
-!- PTM: 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. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: 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). {ECO:0000269|PubMed:15800625,
ECO:0000269|PubMed:27855162, ECO:0000269|PubMed:28702327}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AF140673; AAD56356.1; -; mRNA.
EMBL; BC138619; AAI38620.1; -; mRNA.
EMBL; BC138620; AAI38621.1; -; mRNA.
CCDS; CCDS28288.1; -.
RefSeq; NP_035912.2; NM_011782.2.
UniGene; Mm.112933; -.
UniGene; Mm.437478; -.
ProteinModelPortal; Q9R001; -.
SMR; Q9R001; -.
STRING; 10090.ENSMUSP00000023611; -.
MEROPS; M12.225; -.
PhosphoSitePlus; Q9R001; -.
MaxQB; Q9R001; -.
PaxDb; Q9R001; -.
PeptideAtlas; Q9R001; -.
PRIDE; Q9R001; -.
Ensembl; ENSMUST00000023611; ENSMUSP00000023611; ENSMUSG00000022894.
GeneID; 23794; -.
KEGG; mmu:23794; -.
UCSC; uc007ztw.1; mouse.
CTD; 11096; -.
MGI; MGI:1346321; Adamts5.
eggNOG; ENOG410IND8; Eukaryota.
eggNOG; ENOG410ZQPN; LUCA.
GeneTree; ENSGT00900000140774; -.
HOGENOM; HOG000004799; -.
HOVERGEN; HBG004313; -.
InParanoid; Q9R001; -.
KO; K08620; -.
OMA; NYSGWSH; -.
OrthoDB; EOG091G00AX; -.
TreeFam; TF331949; -.
BRENDA; 3.4.24.B12; 3474.
Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
Reactome; R-MMU-5173214; O-glycosylation of TSR domain-containing proteins.
PRO; PR:Q9R001; -.
Proteomes; UP000000589; Chromosome 16.
Bgee; ENSMUSG00000022894; Expressed in 275 organ(s), highest expression level in decidua.
Genevisible; Q9R001; MM.
GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0050840; F:extracellular matrix binding; IDA:MGI.
GO; GO:0008201; F:heparin binding; IDA:MGI.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
GO; GO:0008237; F:metallopeptidase activity; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0042742; P:defense response to bacterium; IGI:MGI.
GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IMP:YuBioLab.
GO; GO:0044691; P:tooth eruption; IEA:Ensembl.
Gene3D; 2.20.100.10; -; 2.
Gene3D; 3.40.390.10; -; 1.
InterPro; IPR006586; ADAM_Cys-rich.
InterPro; IPR010294; ADAM_spacer1.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR013276; Pept_M12B_ADAM-TS5.
InterPro; IPR001590; Peptidase_M12B.
InterPro; IPR002870; Peptidase_M12B_N.
InterPro; IPR000884; TSP1_rpt.
InterPro; IPR036383; TSP1_rpt_sf.
Pfam; PF05986; ADAM_spacer1; 1.
Pfam; PF01562; Pep_M12B_propep; 1.
Pfam; PF01421; Reprolysin; 1.
Pfam; PF00090; TSP_1; 2.
PRINTS; PR01860; ADAMTS5.
SMART; SM00608; ACR; 1.
SMART; SM00209; TSP1; 2.
SUPFAM; SSF82895; SSF82895; 2.
PROSITE; PS50215; ADAM_MEPRO; 1.
PROSITE; PS50092; TSP1; 2.
PROSITE; PS00142; ZINC_PROTEASE; 1.
2: Evidence at transcript level;
Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
Extracellular matrix; Glycoprotein; Hydrolase; Metal-binding;
Metalloprotease; Protease; Reference proteome; Repeat; Secreted;
Signal; Zinc; Zymogen.
SIGNAL 1 21 {ECO:0000255}.
PROPEP 22 261 {ECO:0000255}.
/FTId=PRO_0000029172.
CHAIN 262 930 A disintegrin and metalloproteinase with
thrombospondin motifs 5.
/FTId=PRO_0000029173.
DOMAIN 267 476 Peptidase M12B. {ECO:0000255|PROSITE-
ProRule:PRU00276}.
DOMAIN 485 566 Disintegrin.
DOMAIN 567 622 TSP type-1 1. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 875 929 TSP type-1 2. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
REGION 732 874 Spacer.
MOTIF 207 214 Cysteine switch. {ECO:0000250}.
COMPBIAS 41 46 Poly-Ala.
COMPBIAS 257 261 Poly-Arg.
COMPBIAS 624 731 Cys-rich.
ACT_SITE 411 411 {ECO:0000255|PROSITE-ProRule:PRU00276,
ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 209 209 Zinc; in inhibited form. {ECO:0000250}.
METAL 410 410 Zinc; catalytic.
{ECO:0000250|UniProtKB:Q9UNA0}.
METAL 414 414 Zinc; catalytic.
{ECO:0000250|UniProtKB:Q9UNA0}.
METAL 420 420 Zinc; catalytic.
{ECO:0000250|UniProtKB:Q9UNA0}.
CARBOHYD 498 498 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 570 570 C-linked (Man) tryptophan.
{ECO:0000250|UniProtKB:Q9UNA0}.
CARBOHYD 573 573 C-linked (Man) tryptophan.
{ECO:0000250|UniProtKB:Q9UNA0}.
CARBOHYD 582 582 O-linked (Fuc...) serine.
{ECO:0000250|UniProtKB:Q9UNA0}.
CARBOHYD 728 728 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 802 802 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 807 807 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 342 394 {ECO:0000250|UniProtKB:Q9UNA0}.
DISULFID 371 376 {ECO:0000250|UniProtKB:Q9UNA0}.
DISULFID 388 471 {ECO:0000250|UniProtKB:Q9UNA0}.
DISULFID 426 455 {ECO:0000250|UniProtKB:Q9UNA0}.
DISULFID 497 519 {ECO:0000250|UniProtKB:Q9UNA0}.
DISULFID 508 529 {ECO:0000250|UniProtKB:Q9UNA0}.
DISULFID 514 548 {ECO:0000250|UniProtKB:Q9UNA0}.
DISULFID 542 553 {ECO:0000250|UniProtKB:Q9UNA0}.
DISULFID 579 616 {ECO:0000250}.
DISULFID 583 621 {ECO:0000250}.
DISULFID 594 606 {ECO:0000250}.
CONFLICT 7 7 P -> S (in Ref. 1; AAD56356).
{ECO:0000305}.
CONFLICT 76 76 Q -> H (in Ref. 1; AAD56356).
{ECO:0000305}.
CONFLICT 772 772 T -> P (in Ref. 1; AAD56356).
{ECO:0000305}.
CONFLICT 844 844 D -> G (in Ref. 1; AAD56356).
{ECO:0000305}.
SEQUENCE 930 AA; 101844 MW; 0CF1B264C782FF49 CRC64;
MRLEWAPLLL LLLLLSASCL SLAADSPAAA PAQDKTRQPQ AAAAAAEPDQ PQGEETRERG
HLQPLAGQRR SGGLVQNIDQ LYSGGGKVGY LVYAGGRRFL LDLERDDTVG AAGSIVTAGG
GLSASSGHRG HCFYRGTVDG SPRSLAVFDL CGGLDGFFAV KHARYTLKPL LRGSWAEYER
IYGDGSSRIL HVYNREGFSF EALPPRASCE TPASPSGPQE SPSVHSRSRR RSALAPQLLD
HSAFSPSGNA GPQTWWRRRR RSISRARQVE LLLVADSSMA RMYGRGLQHY LLTLASIANR
LYSHASIENH IRLAVVKVVV LTDKDTSLEV SKNAATTLKN FCKWQHQHNQ LGDDHEEHYD
AAILFTREDL CGHHSCDTLG MADVGTICSP ERSCAVIEDD GLHAAFTVAH EIGHLLGLSH
DDSKFCEENF GTTEDKRLMS SILTSIDASK PWSKCTSATI TEFLDDGHGN CLLDLPRKQI
LGPEELPGQT YDATQQCNLT FGPEYSVCPG MDVCARLWCA VVRQGQMVCL TKKLPAVEGT
PCGKGRVCLQ GKCVDKTKKK YYSTSSHGNW GSWGPWGQCS RSCGGGVQFA YRHCNNPAPR
NSGRYCTGKR AIYRSCSVTP CPPNGKSFRH EQCEAKNGYQ SDAKGVKTFV EWVPKYAGVL
PADVCKLTCR AKGTGYYVVF SPKVTDGTEC RPYSNSVCVR GRCVRTGCDG IIGSKLQYDK
CGVCGGDNSS CTKIIGTFNK KSKGYTDVVR IPEGATHIKV RQFKAKDQTR FTAYLALKKK
TGEYLINGKY MISTSETIID INGTVMNYSG WSHRDDFLHG MGYSATKEIL IVQILATDPT
KALDVRYSFF VPKKTTQKVN SVISHGSNKV GPHSTQLQWV TGPWLACSRT CDTGWHTRTV
QCQDGNRKLA KGCLLSQRPS AFKQCLLKKC


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