ATS20_MOUSE
ID ATS20_MOUSE Reviewed; 1906 AA.
AC P59511; E9QLA1;
DT 04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 20;
DE Short=ADAM-TS 20;
DE Short=ADAM-TS20;
DE Short=ADAMTS-20;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=Adamts20;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=12562771; DOI=10.1074/jbc.m211900200;
RA Llamazares M., Cal S., Quesada V., Lopez-Otin C.;
RT "Identification and characterization of ADAMTS-20 defines a novel subfamily
RT of metalloproteinases-disintegrins with multiple thrombospondin-1 repeats
RT and a unique GON domain.";
RL J. Biol. Chem. 278:13382-13389(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND DISEASE.
RC STRAIN=DBA/2J;
RX PubMed=12925592; DOI=10.1242/dev.00668;
RA Rao C., Foernzler D., Loftus S.K., Liu S., McPherson J.D., Jungers K.A.,
RA Apte S.S., Pavan W.J., Beier D.R.;
RT "A defect in a novel ADAMTS family member is the cause of the belted white-
RT spotting mutation.";
RL Development 130:4665-4672(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: May play a role in tissue-remodeling process occurring in
CC both normal and pathological conditions. May have a protease-
CC independent function in the transport from the endoplasmic reticulum to
CC the Golgi apparatus of secretory cargos, mediated by the GON domain.
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=2;
CC Name=1; Synonyms=ADAMTS20 B long isoform;
CC IsoId=P59511-1; Sequence=Displayed;
CC Name=2; Synonyms=ADAMTS20 A short isoform;
CC IsoId=P59511-2; Sequence=VSP_007606, VSP_007607;
CC -!- TISSUE SPECIFICITY: Expressed at low level in testis and brain.
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 -!- DISEASE: Note=Defects in Adamts20 are the cause of the belted (bt)
CC phenotype. It is a pigmental defect which occurs as a result of a
CC defect in melanocyte development. {ECO:0000269|PubMed:12925592}.
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DR EMBL; AJ512753; CAD54808.3; -; mRNA.
DR EMBL; AY189815; AAO74895.1; -; mRNA.
DR EMBL; AY189816; AAO74896.1; -; mRNA.
DR EMBL; AC084382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC084384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS27770.1; -. [P59511-1]
DR CCDS; CCDS49711.1; -. [P59511-2]
DR RefSeq; NP_803180.3; NM_177431.5. [P59511-1]
DR AlphaFoldDB; P59511; -.
DR SMR; P59511; -.
DR BioGRID; 230203; 1.
DR STRING; 10090.ENSMUSP00000036330; -.
DR MEROPS; M12.188; -.
DR GlyGen; P59511; 10 sites.
DR PhosphoSitePlus; P59511; -.
DR CPTAC; non-CPTAC-3963; -.
DR PaxDb; P59511; -.
DR PeptideAtlas; P59511; -.
DR PRIDE; P59511; -.
DR Antibodypedia; 25100; 30 antibodies from 16 providers.
DR DNASU; 223838; -.
DR Ensembl; ENSMUST00000035342; ENSMUSP00000036330; ENSMUSG00000022449. [P59511-1]
DR Ensembl; ENSMUST00000155907; ENSMUSP00000121696; ENSMUSG00000022449. [P59511-2]
DR GeneID; 223838; -.
DR KEGG; mmu:223838; -.
DR UCSC; uc007xje.2; mouse. [P59511-1]
DR UCSC; uc007xjf.2; mouse. [P59511-2]
DR CTD; 80070; -.
DR MGI; MGI:2660628; Adamts20.
DR VEuPathDB; HostDB:ENSMUSG00000022449; -.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000158636; -.
DR HOGENOM; CLU_000660_0_1_1; -.
DR InParanoid; P59511; -.
DR OMA; YQECPVL; -.
DR OrthoDB; 125522at2759; -.
DR PhylomeDB; P59511; -.
DR TreeFam; TF331949; -.
DR Reactome; R-MMU-5173214; O-glycosylation of TSR domain-containing proteins.
DR BioGRID-ORCS; 223838; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Adamts20; mouse.
DR PRO; PR:P59511; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P59511; protein.
DR Bgee; ENSMUSG00000022449; Expressed in presomitic mesoderm and 164 other tissues.
DR Genevisible; P59511; MM.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0004175; F:endopeptidase activity; IDA:MGI.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
DR GO; GO:0030318; P:melanocyte differentiation; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0045636; P:positive regulation of melanocyte differentiation; IMP:MGI.
DR GO; GO:0009967; P:positive regulation of signal transduction; IMP:MGI.
DR GO; GO:0006508; P:proteolysis; IDA:MGI.
DR GO; GO:0048070; P:regulation of developmental pigmentation; IMP:MGI.
DR GO; GO:0007165; P:signal transduction; IMP:MGI.
DR Gene3D; 2.20.100.10; -; 12.
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; IPR012314; Pept_M12B_GON-ADAMTSs.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
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; PF08685; GON; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 14.
DR SUPFAM; SSF82895; SSF82895; 13.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS51046; GON; 1.
DR PROSITE; PS50092; TSP1; 13.
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..26
FT /evidence="ECO:0000255"
FT PROPEP 27..249
FT /evidence="ECO:0000250"
FT /id="PRO_0000029208"
FT CHAIN 250..1906
FT /note="A disintegrin and metalloproteinase with
FT thrombospondin motifs 20"
FT /id="PRO_0000029209"
FT DOMAIN 255..464
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 465..552
FT /note="Disintegrin"
FT DOMAIN 553..608
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 843..901
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 906..962
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 962..1015
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1017..1074
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1075..1131
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1148..1202
FT /note="TSP type-1 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1203..1260
FT /note="TSP type-1 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1300..1351
FT /note="TSP type-1 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1354..1411
FT /note="TSP type-1 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1412..1465
FT /note="TSP type-1 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1468..1526
FT /note="TSP type-1 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1527..1584
FT /note="TSP type-1 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1585..1648
FT /note="TSP type-1 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1650..1706
FT /note="TSP type-1 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1707..1906
FT /note="GON"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00383"
FT REGION 201..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..842
FT /note="Spacer"
FT REGION 1265..1295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 400
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 399
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 403
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 409
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 714
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 798
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 805
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1057
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1562
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1719
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1759
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1777
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 330..383
FT /evidence="ECO:0000250"
FT DISULFID 359..365
FT /evidence="ECO:0000250"
FT DISULFID 377..459
FT /evidence="ECO:0000250"
FT DISULFID 415..443
FT /evidence="ECO:0000250"
FT DISULFID 486..508
FT /evidence="ECO:0000250"
FT DISULFID 497..518
FT /evidence="ECO:0000250"
FT DISULFID 503..537
FT /evidence="ECO:0000250"
FT DISULFID 531..542
FT /evidence="ECO:0000250"
FT DISULFID 565..602
FT /evidence="ECO:0000250"
FT DISULFID 569..607
FT /evidence="ECO:0000250"
FT DISULFID 580..592
FT /evidence="ECO:0000250"
FT VAR_SEQ 1424..1425
FT /note="CS -> VR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12925592"
FT /id="VSP_007606"
FT VAR_SEQ 1426..1906
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12925592"
FT /id="VSP_007607"
FT CONFLICT 1211
FT /note="D -> Y (in Ref. 2; AAO74895/AAO74896)"
FT /evidence="ECO:0000305"
FT CONFLICT 1262
FT /note="L -> S (in Ref. 1; CAD54808)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1906 AA; 212068 MW; A7B152DA0D93CD03 CRC64;
MRVAKWLTGL LCPISLLLTG SWEVRFHPRQ EALVKTLASY EVVTPTRVNE FGDVFPQNRH
FSRKKRSSGV PEPPPFRTHY RISAYGQLFQ LNLSADAAFL AAGYTEVHLG TPVPGPGGRS
TESPDLRHCF YRGQVNARED HTAVFSLCGG LMGTFKANDG EYFLEPVLRA DGSAHDDDHN
KPHLIYRQEL KRNSFARSHK PCEVSENQME KTALPSQSSR NTTGDVDIEE EAVFRLEGER
SQLHSRNKRF LSYPRYVEVM VTADAKMVHH HGQNLQHYVL TLMSIVAAIY KDSSIGNLIN
IVIVKLVVIH SEQEGPVISF NAATTLRNFC LWQQSQNVPD DAHPSHHDTA VLITREDICG
AKEKCDTLGL AELGTLCDPS RSCSISEENG LSAAFTIAHE LGHVFNVPHD DSFKCKEAGI
KHQYHVMAPT LNYHTSPWTW SACSQKHITE FLDTGHGECL LDKPNGRTYD LSPQLPGSVY
DGNRQCELMF GPGSQVCPYL KHCRRLWCTS AEGVHKGCRT QHMPLADGTS CGPGMHCHRG
LCVTRDMETR PVDGEWGPWG PYSSCSRTCG GGIKSTARLC DRPEPRNGGR YCVGRRMKFR
SCNTDSCPKG KRDFREKQCS DFDGKHFDIN GLPPNVRWLP KYSGIAVKDR CKLYCRVAGT
TSFYQLKDRV ADGTPCGTET NDICVQGLCR QAGCDHVLNS KAKRDKCGVC GGDNSSCQTL
AGVFNSAHYG YNVVVKIPAG ATNIEILQHS YSGRPEDDNY LALSDTQGNF LLNGNFVVSM
AKKEINIQGA VFEYSGSNNS IERINSTDRL EAELVLQVLC VGNLYNPDVR YSFNIPIEER
SNLFSWDPYG PWQDCTKMCQ GLHRRKIACV RKSDHAVVSD HNCGHLPMPL FVTEKCNMDC
ELRWHIIGKS DCSSQCGQGY RTLDVHCMKY SVHKGQAVPV GDQYCGDQLK PPSREPCHGS
CVLTRWHYSE WSQCSRSCGG GDKTRESYCV NGFGHRLAES ECRELPRVVL ENCNEFPCPS
WATSEWSECP VTCGKGMKQR QVWCQLSEDP MRDGFCNAST KPESLRPCEL RACASWHVGP
WGSCTATCGH GYQMRAVKCI SEIFGTMLDD RECPQASRPS DRQDCILAPC LAIPEVGATS
LPAIPLGRAA QWRHGSWTPC SVSCGRGSQA RYVSCRDAHD EVADESNCAH LPRPAAVSLC
FSPCGEWQAG DWSPCSASCG HGKTTRRVLC VNYHQLVDES YCDPEGRPVT EQECSLAACP
PLYSRAPSSS EQPSHVPSRN VPLTHKPGEN QDQGAQLSIR GNQWRTGPWG ACSRSCAGGL
QHRAVVCQDE DGRSATSCDG SSKPPESRHC GSGPCPHWNY GDWGECTQTC GGGVKSRFVI
CQFPNGQMTQ EHSCELPKPP SMMQCHLHAC PEDVSWYRGP WKSCSASCGK GVKYREVLCI
DQFQRKLEEK YCSHLHKPRT HKACRSGRCP SWKANKWKEC SVTCGSGVQQ REVYCRLRGT
GRVSEDMCDP STRPQGQRQC WRQDCMRYQW TTGDWLDCST SCKKKETYRL VKCVNEQNVQ
ANESLCDPLT KPLSIKKCRN PHCKYSVVTG DSSQCAGNCG FTSPQKITYC TKIQSSKKHT
FHQLRPVVYG ECPVIPSPQA YKCDLRSCLH VATWKVGKWS KCSVTCGIGI MERRVACRTE
NGWPSDLCLK RLKPDAQKKC YANDCKLLTT CKELQVTNNV TKDGDYDLNV RGRILKIHCS
GMQLENPREY LPLVKSEDNF SEIYGLRLQN PYECPFNGSR RPDCACENDY LPAGYTVFSK
VRVDLESMQI KTADLLFSQT LSGKAVPFAT AGDCYSAARC PQGQFSINLA GTGMKISNTA
KWLAQGRYAS VIIHRSQDGT KVYGRCGGFC GKCIPHMATG LSIQVL
