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ATS5_BOVIN
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   03-AUG-2022, entry version 130.
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   PaxDb; Q9TT92; -.
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; IEA:InterPro.
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; 2.20.100.10; -; 1.
DR   Gene3D; 3.40.390.10; -; 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   Pfam; PF17771; ADAM_CR_2; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   Pfam; PF00090; TSP_1; 1.
DR   SMART; SM00608; ACR; 1.
DR   SUPFAM; SSF82895; SSF82895; 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
 
 
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