LOCUS       NP_001313280            1657 aa            linear   ROD 18-MAR-2025
DEFINITION  A disintegrin and metalloproteinase with thrombospondin motifs 7
            isoform 4 preproprotein [Mus musculus].
ACCESSION   NP_001313280 XP_006510821
VERSION     NP_001313280.1
DBSOURCE    REFSEQ: accession NM_001326351.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1657)
  AUTHORS   Wang,M., Liu,H., Zhang,M., Niu,X., Sun,M., Wang,F., Ni,Y., Hong,T.,
            Zhang,W. and Dang,S.
  TITLE     The secreted protease ADAMTS18 links early isoform transformation
            and maturation of glomerular basement membrane macromolecules to
            the integrity of the glomerular filtration barrier
  JOURNAL   Biochem Biophys Res Commun 750, 151386 (2025)
   PUBMED   39879696
REFERENCE   2  (residues 1 to 1657)
  AUTHORS   Sharifi,M.A., Wierer,M., Dang,T.A., Milic,J., Moggio,A., Sachs,N.,
            von Scheidt,M., Hinterdobler,J., Muller,P., Werner,J., Stiller,B.,
            Aherrahrou,Z., Erdmann,J., Zaliani,A., Graettinger,M.,
            Reinshagen,J., Gul,S., Gribbon,P., Maegdefessel,L., Bernhagen,J.,
            Sager,H.B., Mann,M., Schunkert,H. and Kessler,T.
  TITLE     ADAMTS-7 Modulates Atherosclerotic Plaque Formation by Degradation
            of TIMP-1
  JOURNAL   Circ Res 133 (8), 674-686 (2023)
   PUBMED   37675562
  REMARK    GeneRIF: ADAMTS-7 Modulates Atherosclerotic Plaque Formation by
            Degradation of TIMP-1.
REFERENCE   3  (residues 1 to 1657)
  AUTHORS   Gong,Z., Huang,J., Wang,D., Yang,S., Ma,Z., Fu,Y., Ma,Q. and
            Kong,W.
  TITLE     ADAMTS-7 deficiency attenuates thoracic aortic aneurysm and
            dissection in mice
  JOURNAL   J Mol Med (Berl) 101 (3), 237-248 (2023)
   PUBMED   36662289
  REMARK    GeneRIF: ADAMTS-7 deficiency attenuates thoracic aortic aneurysm
            and dissection in mice.
REFERENCE   4  (residues 1 to 1657)
  AUTHORS   Ma,Z., Mao,C., Jia,Y., Yu,F., Xu,P., Tan,Y., Zou,Q.H., Zhou,X.J.,
            Kong,W. and Fu,Y.
  TITLE     ADAMTS7-Mediated Complement Factor H Degradation Potentiates
            Complement Activation to Contributing to Renal Injuries
  JOURNAL   J Am Soc Nephrol 34 (2), 291-308 (2023)
   PUBMED   36735376
  REMARK    GeneRIF: ADAMTS7-Mediated Complement Factor H Degradation
            Potentiates Complement Activation to Contributing to Renal
            Injuries.
REFERENCE   5  (residues 1 to 1657)
  AUTHORS   Jaiswal,A.K. and Mishra,A.
  TITLE     ADAMTS7 Attenuates House Dust Mite-Induced Airway Inflammation and
            Th2 Immune Responses
  JOURNAL   Lung 200 (3), 305-313 (2022)
   PUBMED   35503474
  REMARK    GeneRIF: ADAMTS7 Attenuates House Dust Mite-Induced Airway
            Inflammation and Th2 Immune Responses.
REFERENCE   6  (residues 1 to 1657)
  AUTHORS   Lai,Y., Bai,X., Zhao,Y., Tian,Q., Liu,B., Lin,E.A., Chen,Y.,
            Lee,B., Appleton,C.T., Beier,F., Yu,X.P. and Liu,C.J.
  TITLE     ADAMTS-7 forms a positive feedback loop with TNF-alpha in the
            pathogenesis of osteoarthritis
  JOURNAL   Ann Rheum Dis 73 (8), 1575-1584 (2014)
   PUBMED   23928557
  REMARK    GeneRIF: ADAMTS-7 and TNF-alpha form a positive feedback loop in
            the regulation of cartilage degradation and osteoarthritis
            progression.
REFERENCE   7  (residues 1 to 1657)
  AUTHORS   Du,J., Takeuchi,H., Leonhard-Melief,C., Shroyer,K.R., Dlugosz,M.,
            Haltiwanger,R.S. and Holdener,B.C.
  TITLE     O-fucosylation of thrombospondin type 1 repeats restricts
            epithelial to mesenchymal transition (EMT) and maintains epiblast
            pluripotency during mouse gastrulation
  JOURNAL   Dev Biol 346 (1), 25-38 (2010)
   PUBMED   20637190
REFERENCE   8  (residues 1 to 1657)
  AUTHORS   Bai,X.H., Wang,D.W., Kong,L., Zhang,Y., Luan,Y., Kobayashi,T.,
            Kronenberg,H.M., Yu,X.P. and Liu,C.J.
  TITLE     ADAMTS-7, a direct target of PTHrP, adversely regulates
            endochondral bone growth by associating with and inactivating GEP
            growth factor
  JOURNAL   Mol Cell Biol 29 (15), 4201-4219 (2009)
   PUBMED   19487464
  REMARK    GeneRIF: Findings demonstrate that ADAMTS-7, a direct target of
            PTHrP signaling, negatively regulates endochondral bone formation
            by associating with and inactivating GEP chondrogenic growth
            factor.
REFERENCE   9  (residues 1 to 1657)
  AUTHORS   Somerville,R.P., Longpre,J.M., Apel,E.D., Lewis,R.M., Wang,L.W.,
            Sanes,J.R., Leduc,R. and Apte,S.S.
  TITLE     ADAMTS7B, the full-length product of the ADAMTS7 gene, is a
            chondroitin sulfate proteoglycan containing a mucin domain
  JOURNAL   J Biol Chem 279 (34), 35159-35175 (2004)
   PUBMED   15192113
  REMARK    GeneRIF: ADAMTS7B has a domain organization with a total of eight
            thrombospondin type 1 repeats in its ancillary domain. Of these,
            seven are arranged in two distinct clusters that are separated by a
            mucin domain
REFERENCE   10 (residues 1 to 1657)
  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
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BY347798.1, BC076575.1,
            CB246893.1, AC140392.3 and BC058991.1.
            
            On May 15, 2016 this sequence version replaced XP_006510821.1.
            
            Summary: This gene encodes a member of 'a disintegrin and
            metalloproteinase with thrombospondin motifs' (ADAMTS) family of
            multi-domain matrix-associated metalloendopeptidases that have
            diverse roles in tissue morphogenesis and pathophysiological
            remodeling, in inflammation and in vascular biology. The encoded
            preproprotein undergoes proteolytic processing to generate an
            active, zinc-dependent enzyme that degrades cartilage oligomeric
            matrix protein. The deficiency of the encoded protein decreases
            atherosclerosis in genetically hyperlipidemic mice and in response
            to vascular injury. Alternative splicing results in multiple
            transcript variants encoding different isoforms, some of which may
            undergo similar processing. [provided by RefSeq, May 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 the transcript AY551090.1. An
            unsupported intron in the 3' coding region of this transcript was
            replaced with sequence from the reference genome assembly.
            
            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 :: SRR10223969.9220.1,
                                           SRR9219380.72908.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1657
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 47.46 cM"
     Protein         1..1657
                     /product="A disintegrin and metalloproteinase with
                     thrombospondin motifs 7 isoform 4 preproprotein"
                     /EC_number="3.4.24.-"
                     /note="a disintegrin and metalloproteinase with
                     thrombospondin motifs 7; COMPase; a disintegrin-like and
                     metalloprotease (reprolysin type) with thrombospondin type
                     1 motif, 7; a disintegrin-like and metallopeptidase
                     (reprolysin type) with thrombospondin type 1 motif, 7"
                     /calculated_mol_wt=180212
     sig_peptide     1..20
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q68SA9.3)"
                     /calculated_mol_wt=2121
     Region          34..174
                     /region_name="Pep_M12B_propep"
                     /note="Reprolysin family propeptide; pfam01562"
                     /db_xref="CDD:460254"
     Site            84
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q68SA9.3)"
     Region          165..221
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68SA9.3)"
     Region          192..199
                     /region_name="Cysteine switch. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68SA9.3)"
     mat_peptide     221..1657
                     /product="A disintegrin and metalloproteinase with
                     thrombospondin motifs 7. /id=PRO_0000348235"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68SA9.3)"
                     /calculated_mol_wt=157959
     Region          226..434
                     /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(372..373,376,382)
                     /site_type="active"
                     /db_xref="CDD:239801"
     Region          449..513
                     /region_name="ADAMTS_CR_2"
                     /note="ADAMTS cysteine-rich domain 2; pfam17771"
                     /db_xref="CDD:465496"
     Region          526..578
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          584..682
                     /region_name="ADAMTS_CR_3"
                     /note="ADAMTS cysteine-rich domain; pfam19236"
                     /db_xref="CDD:437068"
     Site            622
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q68SA9.3)"
     Region          683..794
                     /region_name="Spacer"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68SA9.3)"
     Region          684..793
                     /region_name="ADAMTS_spacer1"
                     /note="ADAM-TS Spacer 1; pfam05986"
                     /db_xref="CDD:461796"
     Region          808..862
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          866..922
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          929..977
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          1009..1034
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68SA9.3)"
     Region          <1065..1403
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1073..1127
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68SA9.3)"
     Region          1140..1237
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68SA9.3)"
     Region          1283..1304
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68SA9.3)"
     Region          1317..1384
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68SA9.3)"
     Region          1386..1434
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          1437..1492
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          1495..1541
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          1544..1599
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     CDS             1..1657
                     /gene="Adamts7"
                     /gene_synonym="ADAM-TS7; ADAMTS7B"
                     /coded_by="NM_001326351.1:268..5241"
                     /note="isoform 4 preproprotein is encoded by transcript
                     variant 4"
                     /db_xref="CCDS:CCDS85708.1"
                     /db_xref="GeneID:108153"
                     /db_xref="MGI:MGI:1347346"
ORIGIN      
        1 mhrgpsllli lcalasrvlg pasglvtegr agldivhpvr vdaggsflsy elwprvlrkr
       61 dvsttqassa fyqlqyqgre llfnlttnpy lmapgfvsei rrhstlghah iqtsvptchl
      121 lgdvqdpele ggfaaisacd glrgvfqlsn edyfiepldg vsaqpghaqp hvvykhqgsr
      181 kqaqqgdsrp sgtcgmqvpp dleqqrehwe qqqqkrrqqr svskekwvet lvvadskmve
      241 yhgqpqvesy vltimnmvag lfhdpsignp ihisivrlii ledeekdlki thhaeetlkn
      301 fcrwqknini kgddhpqhhd tailltrkdl casmnqpcet lglshvsglc hpqlscsvse
      361 dtgmplaftv ahelghsfgi qhdgtgndce sigkrpfims pqllydrgip ltwsrcsrey
      421 itrfldrgwg lclddrpskd vialpsvlpg vlydvnhqcr lqygshsayc edmddvchtl
      481 wcsvgttchs kldaavdgts cgknkwclkg ecvpegfqpe avdggwsgws awsdcsrscg
      541 vgvrsserqc tqpvpknrgk ycvgerkrsq lcnlpacppd rpsfrhtqcs qfdgmlykgk
      601 lhkwvpvpnd dnpcelhcrp snssnteklr davvdgtpcy qsrisrdicl ngicknvgcd
      661 fvidsgaeed rcgvcrgdgs tcqtvsrtfk etegqgyvdi glipagarei lieevaeaan
      721 flalrsedpd kyflnggwti qwngdyrvag ttftyarkgn wenltspgpt sepvwiqllf
      781 qeknpgvhyq ytiqrdshdq vrppefswhy gpwskctvtc gtgvqrqsly cmerqagvva
      841 eeycntlnrp derqrkcsee pcpprwwage wqpcsrscgp eglsrravfc irsmgldeqr
      901 alelsacehl prplaetpcn rhvicpstwg vgnwsqcsvt cgagirqrsv lcinntdvpc
      961 deaerpitet fcflqpcqyp myivdtgasg sgssspelfn evdfipnqla prpspasspk
     1021 pvsisnaide eeldppgpvf vddfyydynf infhedlsyg sfeephpdlv dnggwtapph
     1081 irptespsdt pvptagalga eaediqgsws pspllseasy sppgleqtsi nplanfltee
     1141 dtpmgapelg fpslpwppas vddmmtpvgp gnpdellvke deqsppstpw sdrnklstdg
     1201 nplghtspal pqspiptqps ppsisptqas pspdvvevst gwnaawdpvl eadlkpghge
     1261 lpstvevasp pllpmatvpg iwgrdsplep gtptfsspel ssqhlktltm pgtllltvpt
     1321 dlrspgpsgq pqtpnlegtq spgllptpar etqtnsskdp evqplqpsle edgdpadplp
     1381 arnaswqvgn wsqcsttcgl gaiwrlvscs sgndedctla srpqparhch lrpcaawrtg
     1441 nwskcsrncg ggsstrdvqc vdtrdlrplr pfhcqpgptk ppnrqlcgtq pclpwytssw
     1501 recseacggg eqqrlvtcpe pglceeslrp nnsrpcnthp ctqwvvgpwg qcsapcgggv
     1561 qrrlvrcvnt qtglaeedsd lcsheawpes srpcatedce lvepprcerd rlsfnfcetl
     1621 rllgrcqlpt iraqccrscp plsrgvpsrg hqrvarr
//
