LOCUS       NP_008969                930 aa            linear   PRI 27-APR-2025
DEFINITION  A disintegrin and metalloproteinase with thrombospondin motifs 5
            preproprotein [Homo sapiens].
ACCESSION   NP_008969
VERSION     NP_008969.2
DBSOURCE    REFSEQ: accession NM_007038.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 930)
  AUTHORS   Gao,S., Jia,M., Wang,J., Sun,Q., Liu,F., Yu,L., Guo,Y., Li,N. and
            Wei,L.
  TITLE     Association of ADAMTS-5 gene polymorphisms with the susceptibility
            to knee osteoarthritis in a Chinese Han population
  JOURNAL   J Orthop Surg Res 19 (1), 513 (2024)
   PUBMED   39192347
  REMARK    GeneRIF: Association of ADAMTS-5 gene polymorphisms with the
            susceptibility to knee osteoarthritis in a Chinese Han population.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 930)
  AUTHORS   Hao,X. and Wu,X.
  TITLE     SP1-mediated ADAMTS5 transcription promotes IL-1beta-induced
            chondrocyte injury via Wnt/beta-catenin pathway in osteoarthritis
  JOURNAL   Mol Med Rep 30 (2) (2024)
   PUBMED   38940327
  REMARK    GeneRIF: SP1-mediated ADAMTS5 transcription promotes
            IL-1beta-induced chondrocyte injury via Wnt/beta-catenin pathway in
            osteoarthritis.
REFERENCE   3  (residues 1 to 930)
  AUTHORS   Chen,Z., Du,F., Zhang,R., Wu,Q., Lu,Z., Zhang,R.L. and Wang,Q.
  TITLE     ADAMTS5 Promotes Permeability of the Blood-Brain Barrier during
            Treponema pallidum Subspecies pallidum Invading the Central Nervous
            System
  JOURNAL   ACS Infect Dis 10 (4), 1222-1231 (2024)
   PUBMED   38536197
  REMARK    GeneRIF: ADAMTS5 Promotes Permeability of the Blood-Brain Barrier
            during Treponema pallidum Subspecies pallidum Invading the Central
            Nervous System.
REFERENCE   4  (residues 1 to 930)
  AUTHORS   Su,J.Q., Lai,P.Y., Hu,P.H., Hu,J.M., Chang,P.K., Chen,C.Y.,
            Wu,J.J., Lin,Y.J., Sun,C.A., Yang,T., Hsu,C.H., Lin,H.C. and
            Chou,Y.C.
  TITLE     Differential DNA methylation analysis of SUMF2, ADAMTS5, and PXDN
            provides novel insights into colorectal cancer prognosis prediction
            in Taiwan
  JOURNAL   World J Gastroenterol 28 (8), 825-839 (2022)
   PUBMED   35317099
  REMARK    GeneRIF: Differential DNA methylation analysis of SUMF2, ADAMTS5,
            and PXDN provides novel insights into colorectal cancer prognosis
            prediction in Taiwan.
REFERENCE   5  (residues 1 to 930)
  AUTHORS   He,S., Li,J., Ma,D., Liu,Z. and Lv,N.
  TITLE     MicroRNA-148a targets ADAMTS5 to inhibit proliferation of
            endometriosis cells
  JOURNAL   Pak J Pharm Sci 35 (1(Special)), 335-341 (2022)
   PUBMED   35236644
  REMARK    GeneRIF: MicroRNA-148a targets ADAMTS5 to inhibit proliferation of
            endometriosis cells.
REFERENCE   6  (residues 1 to 930)
  AUTHORS   Tang,B.L.
  TITLE     ADAMTS: a novel family of extracellular matrix proteases
  JOURNAL   Int J Biochem Cell Biol 33 (1), 33-44 (2001)
   PUBMED   11167130
  REMARK    Review article
REFERENCE   7  (residues 1 to 930)
  AUTHORS   Mercuri,F.A., Maciewicz,R.A., Tart,J., Last,K. and Fosang,A.J.
  TITLE     Mutations in the interglobular domain of aggrecan alter matrix
            metalloproteinase and aggrecanase cleavage patterns. Evidence that
            matrix metalloproteinase cleavage interferes with aggrecanase
            activity
  JOURNAL   J Biol Chem 275 (42), 33038-33045 (2000)
   PUBMED   11032846
REFERENCE   8  (residues 1 to 930)
  AUTHORS   Hurskainen,T.L., Hirohata,S., Seldin,M.F. and Apte,S.S.
  TITLE     ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of
            zinc metalloproteases. General features and genomic distribution of
            the ADAM-TS family
  JOURNAL   J Biol Chem 274 (36), 25555-25563 (1999)
   PUBMED   10464288
REFERENCE   9  (residues 1 to 930)
  AUTHORS   Abbaszade,I., Liu,R.Q., Yang,F., Rosenfeld,S.A., Ross,O.H.,
            Link,J.R., Ellis,D.M., Tortorella,M.D., Pratta,M.A., Hollis,J.M.,
            Wynn,R., Duke,J.L., George,H.J., Hillman,M.C. Jr., Murphy,K.,
            Wiswall,B.H., Copeland,R.A., Decicco,C.P., Bruckner,R., Nagase,H.,
            Itoh,Y., Newton,R.C., Magolda,R.L., Trzaskos,J.M., Burn,T.C. et al.
  TITLE     Cloning and characterization of ADAMTS11, an aggrecanase from the
            ADAMTS family
  JOURNAL   J Biol Chem 274 (33), 23443-23450 (1999)
   PUBMED   10438522
REFERENCE   10 (residues 1 to 930)
  AUTHORS   Fosang,A.J., Last,K., Fujii,Y., Seiki,M. and Okada,Y.
  TITLE     Membrane-type 1 MMP (MMP-14) cleaves at three sites in the aggrecan
            interglobular domain
  JOURNAL   FEBS Lett 430 (3), 186-190 (1998)
   PUBMED   9688535
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK094057.1, AP001601.1,
            AF142099.1, AP001600.1 and CA313018.1.
            
            On Aug 2, 2008 this sequence version replaced NP_008969.1.
            
            Summary: This gene encodes a member of the ADAMTS (a disintegrin
            and metalloproteinase with thrombospondin motifs) protein family.
            Members of the family share several distinct protein modules,
            including a propeptide region, a metalloproteinase domain, a
            disintegrin-like domain, and a thrombospondin type 1 (TS) motif.
            Individual members of this family differ in the number of
            C-terminal TS motifs, and some have unique C-terminal domains. The
            encoded preproprotein is proteolytically processed to generate the
            mature enzyme. This enzyme contains two C-terminal TS motifs and
            functions as an aggrecanase that cleaves aggrecan, a major
            proteoglycan of cartilage, and may mediate cartilage destruction in
            osteoarthritis. [provided by RefSeq, Feb 2016].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF142099.1, SRR14038195.1319587.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000284987.6/ ENSP00000284987.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..930
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q21.3"
     Protein         1..930
                     /product="A disintegrin and metalloproteinase with
                     thrombospondin motifs 5 preproprotein"
                     /note="aggrecanase-2; a disintegrin-like and
                     metalloprotease (reprolysin type) with thrombospondin type
                     1 motif, 5 (aggrecanase-2); a disintegrin and
                     metalloproteinase with thrombospondin motifs 5; a
                     disintegrin and metalloproteinase with thrombospondin
                     motifs 11"
                     /calculated_mol_wt=99932
     sig_peptide     1..16
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UNA0.2)"
                     /calculated_mol_wt=1804
     Region          24..69
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNA0.2)"
     Region          66..178
                     /region_name="Pep_M12B_propep"
                     /note="Reprolysin family propeptide; pfam01562"
                     /db_xref="CDD:460254"
     Region          206..231
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNA0.2)"
     Region          207..214
                     /region_name="Cysteine switch. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNA0.2)"
     Site            261
                     /site_type="cleavage"
                     /note="Cleavage, by furin and PCSK7.
                     /evidence=ECO:0000269|PubMed:18992360; propagated from
                     UniProtKB/Swiss-Prot (Q9UNA0.2)"
     mat_peptide     262..930
                     /product="A disintegrin and metalloproteinase with
                     thrombospondin motifs 5. /id=PRO_0000029171"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNA0.2)"
                     /calculated_mol_wt=73709
     Region          269..473
                     /region_name="ZnMc_ADAMTS_like"
                     /note="Zinc-dependent metalloprotease, ADAMTS_like
                     subgroup. ADAMs (A Disintegrin And Metalloprotease) are
                     glycoproteins, which play roles in cell signaling, cell
                     fusion, and cell-cell interactions. This particular
                     subfamily represents domain architectures that...;
                     cd04273"
                     /db_xref="CDD:239801"
     Site            order(410..411,414,420)
                     /site_type="active"
                     /db_xref="CDD:239801"
     Region          487..554
                     /region_name="ADAMTS_CR_2"
                     /note="ADAMTS cysteine-rich domain 2; pfam17771"
                     /db_xref="CDD:465496"
     Site            498
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:18042673; propagated from
                     UniProtKB/Swiss-Prot (Q9UNA0.2)"
     Region          570..622
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Site            570
                     /site_type="glycosylation"
                     /note="C-linked (Man) tryptophan.
                     /evidence=ECO:0000269|PubMed:19671700; propagated from
                     UniProtKB/Swiss-Prot (Q9UNA0.2)"
     Site            573
                     /site_type="glycosylation"
                     /note="C-linked (Man) tryptophan.
                     /evidence=ECO:0000269|PubMed:19671700; propagated from
                     UniProtKB/Swiss-Prot (Q9UNA0.2)"
     Site            582
                     /site_type="glycosylation"
                     /note="O-linked (Fuc...) serine.
                     /evidence=ECO:0000269|PubMed:19671700; propagated from
                     UniProtKB/Swiss-Prot (Q9UNA0.2)"
     Region          628..731
                     /region_name="ADAMTS_CR_3"
                     /note="ADAMTS cysteine-rich domain; pfam19236"
                     /db_xref="CDD:437068"
     Site            728
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UNA0.2)"
     Region          732..874
                     /region_name="Spacer"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNA0.2)"
     Region          733..852
                     /region_name="ADAMTS_spacer1"
                     /note="ADAM-TS Spacer 1; pfam05986"
                     /db_xref="CDD:461796"
     Site            802
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UNA0.2)"
     Site            807
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UNA0.2)"
     Region          879..930
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     CDS             1..930
                     /gene="ADAMTS5"
                     /gene_synonym="ADAM-TS 11; ADAM-TS 5; ADAM-TS5; ADAMTS-11;
                     ADAMTS-5; ADAMTS11; ADMP-2"
                     /coded_by="NM_007038.5:698..3490"
                     /db_xref="CCDS:CCDS13579.1"
                     /db_xref="GeneID:11096"
                     /db_xref="HGNC:HGNC:221"
                     /db_xref="MIM:605007"
ORIGIN      
        1 mllgwaslll cafrlplaav gpaatpaqdk agqpptaaaa aqprrrqgee vqeraeppgh
       61 phplaqrrrs kglvqnidql ysgggkvgyl vyaggrrfll dlerdgsvgi agfvpagggt
      121 sapwrhrshc fyrgtvdgsp rslavfdlcg gldgffavkh arytlkpllr gpwaeeekgr
      181 vygdgsaril hvytregfsf ealpprasce tpastpeahe hapahsnpsg raalasqlld
      241 qsalspaggs gpqtwwrrrr rsisrarqve lllvadasma rlygrglqhy lltlasianr
      301 lyshasienh irlavvkvvv lgdkdkslev sknaattlkn fckwqhqhnq lgddheehyd
      361 aailftredl cghhscdtlg madvgticsp erscaviedd glhaaftvah eighllglsh
      421 ddskfceetf gstedkrlms siltsidask pwskctsati teflddghgn clldlprkqi
      481 lgpeelpgqt ydatqqcnlt fgpeysvcpg mdvcarlwca vvrqgqmvcl tkklpavegt
      541 pcgkgriclq gkcvdktkkk yystsshgnw gswgswgqcs rscgggvqfa yrhcnnpapr
      601 nngryctgkr aiyrscslmp cppngksfrh eqceakngyq sdakgvktfv ewvpkyagvl
      661 padvckltcr akgtgyyvvf spkvtdgtec rlysnsvcvr gkcvrtgcdg iigsklqydk
      721 cgvcggdnss ctkivgtfnk kskgytdvvr ipegathikv rqfkakdqtr ftaylalkkk
      781 ngeylingky mistsetiid ingtvmnysg wshrddflhg mgysatkeil ivqilatdpt
      841 kpldvrysff vpkkstpkvn svtshgsnkv gshtsqpqwv tgpwlacsrt cdtgwhtrtv
      901 qcqdgnrkla kgcplsqrps afkqcllkkc
//
