ATS6_HUMAN
ID ATS6_HUMAN Reviewed; 1117 AA.
AC Q9UKP5; Q59EX6; Q5IR87; Q5IR88; Q5IR89; Q68DL1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 6;
DE Short=ADAM-TS 6;
DE Short=ADAM-TS6;
DE Short=ADAMTS-6;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=ADAMTS6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=10464288; DOI=10.1074/jbc.274.36.25555;
RA Hurskainen T.L., Hirohata S., Seldin M.F., Apte S.S.;
RT "ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc
RT metalloproteases.";
RL J. Biol. Chem. 274:25555-25563(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4), AND INDUCTION.
RX PubMed=16129570; DOI=10.1016/j.gene.2005.06.011;
RA Bevitt D.J., Li Z., Lindrop J.L., Barker M.D., Clarke M.P., McKie N.;
RT "Analysis of full length ADAMTS6 transcript reveals alternative splicing
RT and a role for the 5' untranslated region in translational control.";
RL Gene 359:99-110(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 588-1117 (ISOFORM 1).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 804-1117 (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP INDUCTION.
RX PubMed=12697333; DOI=10.1016/s0167-4781(03)00047-2;
RA Bevitt D.J., Mohamed J., Catterall J.B., Li Z., Arris C.E., Hiscott P.,
RA Sheridan C., Langton K.P., Barker M.D., Clarke M.P., McKie N.;
RT "Expression of ADAMTS metalloproteinases in the retinal pigment epithelium
RT derived cell line ARPE-19: transcriptional regulation by TNFalpha.";
RL Biochim. Biophys. Acta 1626:83-91(2003).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Variant 2;
CC IsoId=Q9UKP5-1; Sequence=Displayed;
CC Name=2; Synonyms=Variant 1;
CC IsoId=Q9UKP5-2; Sequence=VSP_037095, VSP_037098, VSP_037099;
CC Name=3; Synonyms=Variant 3;
CC IsoId=Q9UKP5-3; Sequence=VSP_037096, VSP_037097;
CC Name=4; Synonyms=Variant 4;
CC IsoId=Q9UKP5-4; Sequence=VSP_037093, VSP_037094;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in placenta and barely
CC detectable in a number of other tissues.
CC -!- INDUCTION: Isoform 1 and isoform 2 expressions are up-regulated by TNF
CC in retinal pigment epithelial cells. {ECO:0000269|PubMed:12697333,
CC ECO:0000269|PubMed:16129570}.
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 a furin endopeptidase. {ECO:0000250}.
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}.
CC -!- MISCELLANEOUS: [Isoform 2]: Contains critical point mutations in the
CC region encoding the catalytic domain as well as 2 point mutations
CC compared with genomic sequence. May either be a rare polymorphism or
CC may have arisen through a combination of aberrant RNA editing and point
CC mutation/sequencing error. {ECO:0000305}.
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DR EMBL; AF140674; AAD56357.1; -; mRNA.
DR EMBL; AY692424; AAW47397.1; -; mRNA.
DR EMBL; AY692425; AAW47398.1; -; mRNA.
DR EMBL; AY692426; AAW47399.1; -; mRNA.
DR EMBL; AC008847; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008868; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC099505; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB209685; BAD92922.1; -; mRNA.
DR EMBL; CR749356; CAH18209.1; -; mRNA.
DR CCDS; CCDS3983.2; -. [Q9UKP5-1]
DR RefSeq; NP_922932.2; NM_197941.3. [Q9UKP5-1]
DR RefSeq; XP_011541415.1; XM_011543113.2. [Q9UKP5-1]
DR RefSeq; XP_011541416.1; XM_011543114.2. [Q9UKP5-1]
DR AlphaFoldDB; Q9UKP5; -.
DR SMR; Q9UKP5; -.
DR BioGRID; 116345; 7.
DR IntAct; Q9UKP5; 2.
DR MINT; Q9UKP5; -.
DR STRING; 9606.ENSP00000370443; -.
DR BindingDB; Q9UKP5; -.
DR MEROPS; M12.230; -.
DR GlyGen; Q9UKP5; 6 sites.
DR iPTMnet; Q9UKP5; -.
DR PhosphoSitePlus; Q9UKP5; -.
DR BioMuta; ADAMTS6; -.
DR DMDM; 229462816; -.
DR MassIVE; Q9UKP5; -.
DR PaxDb; Q9UKP5; -.
DR PeptideAtlas; Q9UKP5; -.
DR PRIDE; Q9UKP5; -.
DR ProteomicsDB; 84829; -. [Q9UKP5-1]
DR ProteomicsDB; 84830; -. [Q9UKP5-2]
DR Antibodypedia; 11532; 62 antibodies from 16 providers.
DR DNASU; 11174; -.
DR Ensembl; ENST00000381052.8; ENSP00000424377.1; ENSG00000049192.15. [Q9UKP5-4]
DR Ensembl; ENST00000381055.8; ENSP00000370443.3; ENSG00000049192.15. [Q9UKP5-1]
DR GeneID; 11174; -.
DR KEGG; hsa:11174; -.
DR MANE-Select; ENST00000381055.8; ENSP00000370443.3; NM_197941.4; NP_922932.2.
DR UCSC; uc003jtp.4; human. [Q9UKP5-1]
DR CTD; 11174; -.
DR DisGeNET; 11174; -.
DR GeneCards; ADAMTS6; -.
DR HGNC; HGNC:222; ADAMTS6.
DR HPA; ENSG00000049192; Tissue enhanced (placenta).
DR MIM; 605008; gene.
DR neXtProt; NX_Q9UKP5; -.
DR OpenTargets; ENSG00000049192; -.
DR PharmGKB; PA24550; -.
DR VEuPathDB; HostDB:ENSG00000049192; -.
DR eggNOG; KOG3538; Eukaryota.
DR eggNOG; KOG4597; Eukaryota.
DR GeneTree; ENSGT00940000156571; -.
DR HOGENOM; CLU_000660_1_1_1; -.
DR InParanoid; Q9UKP5; -.
DR OMA; NGKPWWL; -.
DR PhylomeDB; Q9UKP5; -.
DR TreeFam; TF313537; -.
DR PathwayCommons; Q9UKP5; -.
DR Reactome; R-HSA-5083635; Defective B3GALTL causes PpS.
DR Reactome; R-HSA-5173214; O-glycosylation of TSR domain-containing proteins.
DR SignaLink; Q9UKP5; -.
DR BioGRID-ORCS; 11174; 6 hits in 1016 CRISPR screens.
DR ChiTaRS; ADAMTS6; human.
DR GenomeRNAi; 11174; -.
DR Pharos; Q9UKP5; Tbio.
DR PRO; PR:Q9UKP5; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9UKP5; protein.
DR Bgee; ENSG00000049192; Expressed in tibia and 126 other tissues.
DR Genevisible; Q9UKP5; HS.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0008237; F:metallopeptidase activity; TAS:ProtInc.
DR GO; GO:0035904; P:aorta development; IEA:Ensembl.
DR GO; GO:0003279; P:cardiac septum development; IEA:Ensembl.
DR GO; GO:0060976; P:coronary vasculature development; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.20.100.10; -; 5.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR045371; ADAMTS_CR_3.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR010909; PLAC.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR Pfam; PF17771; ADAM_CR_2; 1.
DR Pfam; PF19236; ADAM_CR_3; 1.
DR Pfam; PF05986; ADAM_spacer1; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF08686; PLAC; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 5.
DR SUPFAM; SSF82895; SSF82895; 5.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 4.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cleavage on pair of basic residues; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Repeat; Secreted; Signal;
KW Zinc; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..244
FT /evidence="ECO:0000250"
FT /id="PRO_0000029174"
FT CHAIN 245..1117
FT /note="A disintegrin and metalloproteinase with
FT thrombospondin motifs 6"
FT /id="PRO_0000029175"
FT DOMAIN 250..468
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 495..557
FT /note="Disintegrin"
FT DOMAIN 558..613
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 840..900
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 902..960
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 962..1007
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1018..1073
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1079..1117
FT /note="PLAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00233"
FT REGION 717..843
FT /note="Spacer"
FT ACT_SITE 404
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 403
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 407
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 413
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 724
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 956
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 326..387
FT /evidence="ECO:0000250"
FT DISULFID 362..369
FT /evidence="ECO:0000250"
FT DISULFID 381..463
FT /evidence="ECO:0000250"
FT DISULFID 420..447
FT /evidence="ECO:0000250"
FT DISULFID 490..512
FT /evidence="ECO:0000250"
FT DISULFID 501..519
FT /evidence="ECO:0000250"
FT DISULFID 507..542
FT /evidence="ECO:0000250"
FT DISULFID 532..547
FT /evidence="ECO:0000250"
FT DISULFID 570..607
FT /evidence="ECO:0000250"
FT DISULFID 574..612
FT /evidence="ECO:0000250"
FT DISULFID 585..597
FT /evidence="ECO:0000250"
FT DISULFID 911..954
FT /evidence="ECO:0000250"
FT DISULFID 915..959
FT /evidence="ECO:0000250"
FT DISULFID 926..943
FT /evidence="ECO:0000250"
FT VAR_SEQ 283..292
FT /note="AKLYRDSSLG -> RLPNFTVIPA (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16129570"
FT /id="VSP_037093"
FT VAR_SEQ 293..1117
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16129570"
FT /id="VSP_037094"
FT VAR_SEQ 422..504
FT /note="TKGHEAAKLMAAHITANTNPFSWSACSRDYITSFLDSGRGTCLDNEPPKRDF
FT LYPAVAPGQVYDADEQCRFQYGATSRQCKYG -> RKVMKQQNYGSSHYCEYQSFFLVC
FT LQSRFHHQLFR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10464288"
FT /id="VSP_037095"
FT VAR_SEQ 457..468
FT /note="DSGRGTCLDNEP -> EFLKLGDSISGS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16129570"
FT /id="VSP_037096"
FT VAR_SEQ 469..1117
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16129570"
FT /id="VSP_037097"
FT VAR_SEQ 860..908
FT /note="VQRQEVVCKRLDDNSIVQNNYCDPDSKPPENQRACNTEPCPPEWFIGDW ->
FT KMPTRQPTQRARWRTKHILSYALCLLKKLIGNISCRFASSCNLAKETLL (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:10464288"
FT /id="VSP_037098"
FT VAR_SEQ 909..1117
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10464288"
FT /id="VSP_037099"
FT CONFLICT 4
FT /note="L -> S (in Ref. 2; AAW47399)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="D -> G (in Ref. 2; AAW47398)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="S -> P (in Ref. 2; AAW47398)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="Y -> H (in Ref. 2; AAW47397)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="G -> V (in Ref. 1; AAD56357)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="E -> G (in Ref. 1; AAD56357 and 2; AAW47397)"
FT /evidence="ECO:0000305"
FT CONFLICT 588..589
FT /note="PA -> LK (in Ref. 4; BAD92922)"
FT /evidence="ECO:0000305"
FT CONFLICT 712
FT /note="D -> G (in Ref. 1; AAD56357)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1117 AA; 125273 MW; 5901E86BC82A9A87 CRC64;
MEILWKTLTW ILSLIMASSE FHSDHRLSYS SQEEFLTYLE HYQLTIPIRV DQNGAFLSFT
VKNDKHSRRR RSMDPIDPQQ AVSKLFFKLS AYGKHFHLNL TLNTDFVSKH FTVEYWGKDG
PQWKHDFLDN CHYTGYLQDQ RSTTKVALSN CVGLHGVIAT EDEEYFIEPL KNTTEDSKHF
SYENGHPHVI YKKSALQQRH LYDHSHCGVS DFTRSGKPWW LNDTSTVSYS LPINNTHIHH
RQKRSVSIER FVETLVVADK MMVGYHGRKD IEHYILSVMN IVAKLYRDSS LGNVVNIIVA
RLIVLTEDQP NLEINHHADK SLDSFCKWQK SILSHQSDGN TIPENGIAHH DNAVLITRYD
ICTYKNKPCG TLGLASVAGM CEPERSCSIN EDIGLGSAFT IAHEIGHNFG MNHDGIGNSC
GTKGHEAAKL MAAHITANTN PFSWSACSRD YITSFLDSGR GTCLDNEPPK RDFLYPAVAP
GQVYDADEQC RFQYGATSRQ CKYGEVCREL WCLSKSNRCV TNSIPAAEGT LCQTGNIEKG
WCYQGDCVPF GTWPQSIDGG WGPWSLWGEC SRTCGGGVSS SLRHCDSPAP SGGGKYCLGE
RKRYRSCNTD PCPLGSRDFR EKQCADFDNM PFRGKYYNWK PYTGGGVKPC ALNCLAEGYN
FYTERAPAVI DGTQCNADSL DICINGECKH VGCDNILGSD AREDRCRVCG GDGSTCDAIE
GFFNDSLPRG GYMEVVQIPR GSVHIEVREV AMSKNYIALK SEGDDYYING AWTIDWPRKF
DVAGTAFHYK RPTDEPESLE ALGPTSENLI VMVLLQEQNL GIRYKFNVPI TRTGSGDNEV
GFTWNHQPWS ECSATCAGGV QRQEVVCKRL DDNSIVQNNY CDPDSKPPEN QRACNTEPCP
PEWFIGDWLE CSKTCDGGMR TRAVLCIRKI GPSEEETLDY SGCLTHRPVE KEPCNNQSCP
PQWVALDWSE CTPKCGPGFK HRIVLCKSSD LSKTFPAAQC PEESKPPVRI RCSLGRCPPP
RWVTGDWGQC SAQCGLGQQM RTVQCLSYTG QASSDCLETV RPPSMQQCES KCDSTPISNT
EECKDVNKVA YCPLVLKFKF CSRAYFRQMC CKTCQGH
