ID ATS5_BOVIN Reviewed; 207 AA.
AC Q9TT92;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 08-NOV-2023, entry version 133.
DE RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 5;
DE Short=ADAM-TS 5;
DE Short=ADAM-TS5;
DE Short=ADAMTS-5;
DE EC=3.4.24.-;
DE AltName: Full=ADMP-2;
DE AltName: Full=Aggrecanase-2;
DE Flags: Fragment;
GN Name=ADAMTS5;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10403768; DOI=10.1006/bbrc.1999.0909;
RA Flannery C.R., Little C.B., Hughes C.E., Caterson B.;
RT "Expression of ADAMTS homologues in articular cartilage.";
RL Biochem. Biophys. Res. Commun. 260:318-322(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10625599; DOI=10.1074/jbc.275.2.721;
RA Curtis C.L., Hughes C.E., Flannery C.R., Little C.B., Harwood J.L.,
RA Caterson B.;
RT "n-3 fatty acids specifically modulate catabolic factors involved in
RT articular cartilage degradation.";
RL J. Biol. Chem. 275:721-724(2000).
CC -!- FUNCTION: Metalloproteinase that plays an important role in connective
CC tissue organization, development, inflammation and cell migration.
CC Extracellular matrix (ECM) degrading enzyme that shows proteolytic
CC activity toward the hyalectan group of chondroitin sulfate
CC proteoglycans (CSPGs) including ACAN, VCAN, BCAN and NCAN. Cleavage
CC within the hyalectans occurs at Glu-Xaa recognition motifs. Plays a
CC role in embryonic development, including limb and cardiac
CC morphogenesis, and skeletal muscle development through its VCAN
CC remodeling properties. Cleaves VCAN in the pericellular matrix
CC surrounding myoblasts, facilitating myoblast contact and fusion which
CC is required for skeletal muscle development and regeneration.
CC Participates in the development of brown adipose tissue and browning of
CC white adipose tissue. Plays an important role for T-lymphocyte
CC migration from draining lymph nodes following viral infection.
CC {ECO:0000250|UniProtKB:Q9R001}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9UNA0};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9UNA0};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:Q9UNA0}.
CC -!- DOMAIN: The spacer domain and the TSP type-1 domains are important for
CC a tight interaction with the extracellular matrix.
CC -!- PTM: The precursor is cleaved by furin and PCSK7 outside of the cell.
CC {ECO:0000250|UniProtKB:Q9UNA0}.
CC -!- PTM: Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a
CC threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-
CC G of the TSP type-1 repeat domains where C1 and C2 are the first and
CC second cysteine residue of the repeat, respectively. Fucosylated
CC repeats can then be further glycosylated by the addition of a beta-1,3-
CC glucose residue by the glucosyltransferase, B3GALTL. Fucosylation
CC mediates the efficient secretion of ADAMTS family members. Can also be
CC C-glycosylated with one or two mannose molecules on tryptophan residues
CC within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated.
CC These other glycosylations can also facilitate secretion (By
CC similarity). {ECO:0000250}.
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DR EMBL; AF192771; AAF07177.1; -; mRNA.
DR AlphaFoldDB; Q9TT92; -.
DR SMR; Q9TT92; -.
DR STRING; 9913.ENSBTAP00000000849; -.
DR BindingDB; Q9TT92; -.
DR ChEMBL; CHEMBL2673; -.
DR MEROPS; M12.225; -.
DR GlyCosmos; Q9TT92; 4 sites, No reported glycans.
DR PaxDb; 9913-ENSBTAP00000000849; -.
DR eggNOG; KOG3538; Eukaryota.
DR InParanoid; Q9TT92; -.
DR BRENDA; 3.4.24.B12; 908.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004175; F:endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISS:UniProtKB.
DR GO; GO:0008237; F:metallopeptidase activity; IDA:UniProtKB.
DR GO; GO:0022617; P:extracellular matrix disassembly; ISS:UniProtKB.
DR GO; GO:0007520; P:myoblast fusion; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1620.60; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF37; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 5; 1.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR Pfam; PF17771; ADAMTS_CR_2; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF00090; TSP_1; 1.
DR SMART; SM00608; ACR; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50092; TSP1; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Extracellular matrix; Glycoprotein; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Secreted;
KW Zinc.
FT CHAIN <1..>207
FT /note="A disintegrin and metalloproteinase with
FT thrombospondin motifs 5"
FT /id="PRO_0000078210"
FT DOMAIN <1..74
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 83..164
FT /note="Disintegrin"
FT DOMAIN 165..205
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT ACT_SITE 9
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 8
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9UNA0"
FT BINDING 12
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9UNA0"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9UNA0"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:Q9UNA0"
FT CARBOHYD 171
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:Q9UNA0"
FT CARBOHYD 180
FT /note="O-linked (Fuc...) serine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNA0"
FT DISULFID 24..53
FT /evidence="ECO:0000250|UniProtKB:Q9UNA0"
FT DISULFID 95..117
FT /evidence="ECO:0000250|UniProtKB:Q9UNA0"
FT DISULFID 106..127
FT /evidence="ECO:0000250|UniProtKB:Q9UNA0"
FT DISULFID 112..146
FT /evidence="ECO:0000250|UniProtKB:Q9UNA0"
FT DISULFID 140..151
FT /evidence="ECO:0000250|UniProtKB:Q9UNA0"
FT NON_TER 1
FT NON_TER 207
SQ SEQUENCE 207 AA; 22576 MW; E648BEA73A3F86EE CRC64;
HAAFTVAHEI GHLLGLSHDD SKFCEENFGS TEDKRLMSSI LTSIDASKPW SKCTSATITE
FLDDGHGNCL LDLPRKQIPG PEELPGQTYD ASQQCNLTFG PEYSVCPGMD VCARLWCAVV
RQGQMVCLTK KLPAVEGTPC GKGRICLQGK CVDKTKKKYY STSSHGNWGS WGSWGQCSRS
CGGGVQFAYR HCNNPAPKNN GRYCTGK
//
