LOCUS       NP_112217               1594 aa            linear   PRI 13-NOV-2024
DEFINITION  A disintegrin and metalloproteinase with thrombospondin motifs 12
            isoform 1 preproprotein [Homo sapiens].
ACCESSION   NP_112217
VERSION     NP_112217.2
DBSOURCE    REFSEQ: accession NM_030955.4
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 1594)
  AUTHORS   Hoeft,K., Koch,L., Ziegler,S., Zhang,L., Luetke,S., Tanzer,M.C.,
            Mohanta,D., Schumacher,D., Schreibing,F., Long,Q., Kim,H.,
            Klinkhammer,B.M., Schikarski,C., Maryam,S., Baens,M., Hermann,J.,
            Krieg,S., Peisker,F., De Laporte,L., Schaefer,G.J., Menzel,S.,
            Jankowski,J., Humphreys,B.D., Wahida,A., Schneider,R.K.,
            Versele,M., Boor,P., Mann,M., Sengle,G., Hayat,S. and Kramann,R.
  TITLE     ADAMTS12 promotes fibrosis by restructuring extracellular matrix to
            enable activation of injury-responsive fibroblasts
  JOURNAL   J Clin Invest 134 (18), e170246 (2024)
   PUBMED   39286973
  REMARK    GeneRIF: ADAMTS12 promotes fibrosis by restructuring extracellular
            matrix to enable activation of injury-responsive fibroblasts.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1594)
  AUTHORS   Dekky,B., Azar,F., Bonnier,D., Monseur,C., Kalebic,C., Arpigny,E.,
            Colige,A., Legagneux,V. and Theret,N.
  TITLE     ADAMTS12 is a stromal modulator in chronic liver disease
  JOURNAL   FASEB J 37 (11), e23237 (2023)
   PUBMED   37819632
  REMARK    GeneRIF: ADAMTS12 is a stromal modulator in chronic liver disease.
REFERENCE   3  (residues 1 to 1594)
  AUTHORS   Jiang,Y., Huang,J., Huang,Z., Li,W., Tan,R., Li,T., Chen,Z.,
            Tang,X., Zhao,Y., Qiu,J., Li,C., Chen,H. and Yang,Z.
  TITLE     ADAMTS12 promotes oxaliplatin chemoresistance and angiogenesis in
            gastric cancer through VEGF upregulation
  JOURNAL   Cell Signal 111, 110866 (2023)
   PUBMED   37619822
  REMARK    GeneRIF: ADAMTS12 promotes oxaliplatin chemoresistance and
            angiogenesis in gastric cancer through VEGF upregulation.
REFERENCE   4  (residues 1 to 1594)
  AUTHORS   He,R.Z., Zheng,J.H., Yao,H.F., Xu,D.P., Yang,M.W., Liu,D.J.,
            Sun,Y.W. and Huo,Y.M.
  TITLE     ADAMTS12 promotes migration and epithelial-mesenchymal transition
            and predicts poor prognosis for pancreatic cancer
  JOURNAL   Hepatobiliary Pancreat Dis Int 22 (2), 169-178 (2023)
   PUBMED   35508435
  REMARK    GeneRIF: ADAMTS12 promotes migration and epithelial-mesenchymal
            transition and predicts poor prognosis for pancreatic cancer.
REFERENCE   5  (residues 1 to 1594)
  AUTHORS   Liang,J.F., Li,P.H., Zhu,Y., Zheng,S.S., Liu,J.W. and Song,S.Q.
  TITLE     MicroRNA-186 suppresses cell proliferation and metastasis in
            bladder cancer
  JOURNAL   Afr Health Sci 22 (4), 56-63 (2022)
   PUBMED   37092087
  REMARK    GeneRIF: MicroRNA-186 suppresses cell proliferation and metastasis
            in bladder cancer.
REFERENCE   6  (residues 1 to 1594)
  AUTHORS   Luan,Y., Kong,L., Howell,D.R., Ilalov,K., Fajardo,M., Bai,X.H., Di
            Cesare,P.E., Goldring,M.B., Abramson,S.B. and Liu,C.J.
  TITLE     Inhibition of ADAMTS-7 and ADAMTS-12 degradation of cartilage
            oligomeric matrix protein by alpha-2-macroglobulin
  JOURNAL   Osteoarthritis Cartilage 16 (11), 1413-1420 (2008)
   PUBMED   18485748
REFERENCE   7  (residues 1 to 1594)
  AUTHORS   Llamazares,M., Obaya,A.J., Moncada-Pazos,A., Heljasvaara,R.,
            Espada,J., Lopez-Otin,C. and Cal,S.
  TITLE     The ADAMTS12 metalloproteinase exhibits anti-tumorigenic properties
            through modulation of the Ras-dependent ERK signalling pathway
  JOURNAL   J Cell Sci 120 (Pt 20), 3544-3552 (2007)
   PUBMED   17895370
  REMARK    GeneRIF: data suggest that ADAMTS12 confers tumour-protective
            functions upon cells that produce this proteolytic enzyme
REFERENCE   8  (residues 1 to 1594)
  AUTHORS   Liu,C.J., Kong,W., Xu,K., Luan,Y., Ilalov,K., Sehgal,B., Yu,S.,
            Howell,R.D. and Di Cesare,P.E.
  TITLE     ADAMTS-12 associates with and degrades cartilage oligomeric matrix
            protein
  JOURNAL   J Biol Chem 281 (23), 15800-15808 (2006)
   PUBMED   16611630
  REMARK    GeneRIF: ADAMTS-12 is a new COMP-interacting and -degrading enzyme
            and thus may play an important role in the COMP degradation in the
            initiation and progression of arthritis
REFERENCE   9  (residues 1 to 1594)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   10 (residues 1 to 1594)
  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
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC058841.1, AY358745.1,
            AJ250725.1, AW938686.1, AC034232.8 and CA413137.1.
            
            On Aug 26, 2004 this sequence version replaced NP_112217.1.
            
            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-1) motif.
            Individual members of this family differ in the number of
            C-terminal TS-1 motifs, and some have unique C-terminal domains.
            The enzyme encoded by this gene contains eight TS-1 motifs. It may
            play roles in pulmonary cells during fetal development or in tumor
            processes through its proteolytic activity or as a molecule
            potentially involved in regulation of cell adhesion. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            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 :: AJ250725.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000504830.6/ ENSP00000422554.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1594
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.3-p13.2"
     Protein         1..1594
                     /product="A disintegrin and metalloproteinase with
                     thrombospondin motifs 12 isoform 1 preproprotein"
                     /note="a disintegrin-like and metalloprotease (reprolysin
                     type) with thrombospondin type 1 motif, 12; a disintegrin
                     and metalloproteinase with thrombospondin motifs 12;
                     ADAM-TS12; ADAMTS-12; ADAM-TS 12"
                     /calculated_mol_wt=174768
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2926
     Region          54..195
                     /region_name="Pep_M12B_propep"
                     /note="Reprolysin family propeptide; pfam01562"
                     /db_xref="CDD:460254"
     Site            105
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P58397.2)"
     Site            125
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P58397.2)"
     Region          208..213
                     /region_name="Cysteine switch. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P58397.2)"
     Site            215
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P58397.2)"
     mat_peptide     241..1594
                     /product="A disintegrin and metalloproteinase with
                     thrombospondin motifs 12. /id=PRO_0000029187"
                     /note="propagated from UniProtKB/Swiss-Prot (P58397.2)"
                     /calculated_mol_wt=150210
     Region          246..453
                     /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(392..393,396,402)
                     /site_type="active"
                     /db_xref="CDD:239801"
     Region          468..532
                     /region_name="ADAMTS_CR_2"
                     /note="ADAMTS cysteine-rich domain 2; pfam17771"
                     /db_xref="CDD:465496"
     Site            485
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P58397.2)"
     Region          545..596
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          603..701
                     /region_name="ADAMTS_CR_3"
                     /note="ADAMTS cysteine-rich domain; pfam19236"
                     /db_xref="CDD:437068"
     Site            685
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P58397.2)"
     Region          701..827
                     /region_name="Spacer 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P58397.2)"
     Region          703..812
                     /region_name="ADAMTS_spacer1"
                     /note="ADAM-TS Spacer 1; pfam05986"
                     /db_xref="CDD:461796"
     Site            790
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P58397.2)"
     Region          828..882
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          886..940
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          948..996
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Site            952
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P58397.2)"
     Region          997..1316
                     /region_name="Spacer 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P58397.2)"
     Region          1002..1076
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P58397.2)"
     Region          1095..1174
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P58397.2)"
     Site            1105
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P58397.2)"
     Region          1249..1283
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P58397.2)"
     Site            1276
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P58397.2)"
     Site            1301
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P58397.2)"
     Region          1317..1365
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Site            1321
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P58397.2)"
     Region          1368..1424
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Site            1372
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P58397.2)"
     Site            1379
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P58397.2)"
     Region          1427..1472
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          1475..1531
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Site            1504
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P58397.2)"
     CDS             1..1594
                     /gene="ADAMTS12"
                     /gene_synonym="PRO4389"
                     /coded_by="NM_030955.4:135..4919"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS34140.1"
                     /db_xref="GeneID:81792"
                     /db_xref="HGNC:HGNC:14605"
                     /db_xref="MIM:606184"
ORIGIN      
        1 mpcaqrswla nlsvvaqlln fgalcygrqp qpgpvrfpdr rqehfikglp eyhvvgpvrv
       61 dasghflsyg lhypitssrr krdldgsedw vyyrisheek dlffnltvnq gflsnsyime
      121 krygnlshvk mmassaplch lsgtvlqqgt rvgtaalsac hgltgffqlp hgdffiepvk
      181 khplveggyh phivyrrqkv petkeptcgl kdsvnisqkq elwrekwerh nlpsrslsrr
      241 siskerwvet lvvadtkmie yhgsenvesy iltimnmvtg lfhnpsigna ihivvvrlil
      301 leeeeqglki vhhaektlss fckwqksinp ksdlnpvhhd vavlltrkdi cagfnrpcet
      361 lglshlsgmc qphrscnine dsglplafti ahelghsfgi qhdgkendce pvgrhpyims
      421 rqlqydptpl twskcseeyi trfldrgwgf clddipkkkg lkskviapgv iydvhhqcql
      481 qygpnatfcq evenvcqtlw csvkgfcrsk ldaaadgtqc gekkwcmagk citvgkkpes
      541 ipggwgrwsp wshcsrtcga gvqsaerlcn npepkfggky ctgerkryrl cnvhpcrsea
      601 ptfrqmqcse fdtvpyknel yhwfpifnpa hpcelycrpi dgqfsekmld avidgtpcfe
      661 ggnsrnvcin gickmvgcdy eidsnatedr cgvclgdgss cqtvrkmfkq kegsgyvdig
      721 lipkgardir vmeiegagnf lairsedpek yylnggfiiq wngnyklagt vfqydrkgdl
      781 eklmatgptn esvwiqllfq vtnpgikyey tiqkdgldnd veqqmyfwqy ghwtecsvtc
      841 gtgirrqtah cikkgrgmvk atfcdpetqp ngrqkkchek acpprwwage weacsatcgp
      901 hgekkrtvlc iqtmvsdeqa lpptdcqhll kpktllscnr dilcpsdwtv gnwsecsvsc
      961 gggvrirsvt caknhdepcd vtrkpnsral cglqqcpssr rvlkpnkgti sngknpptlk
     1021 pvppptsrpr mlttptgpes mststpaiss pspttaskeg dlggkqwqds stqpelssry
     1081 listgstsqp iltsqslsiq pseenvsssd tgptsegglv atttsgsgls ssrnpitwpv
     1141 tpfyntltkg pemeihsgsg eereqpedkd esnpviwtki rvpgndapve stemplappl
     1201 tpdlsresww ppfstvmegl lpsqrpttse tgtprvegmv tekpantllp lggdhqpeps
     1261 gktanrnhlk lpnnmnqtks sepvlteeda tslitegfll nasnykqltn ghgsahwivg
     1321 nwsecsttcg lgaywrrvec stqmdsdcaa iqrpdpakrc hlrpcagwkv gnwskcsrnc
     1381 sggfkireiq cvdsrdhrnl rpfhcqflag ippplsmscn pepceawqve pwsqcsrscg
     1441 ggvqergvfc pgglcdwtkr ptstmscneh lcchwatgnw dlcstscggg fqkrtvqcvp
     1501 segnktedqd qclcdhkprp pefkkcnqqa ckksadllct kdklsasfcq tlkamkkcsv
     1561 ptvraeccfs cpqthithtq rqrrqrllqk skel
//
