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A disintegrin and metalloproteinase with thrombospondin motifs 20 (ADAM-TS 20) (ADAM-TS20) (ADAMTS-20) (EC 3.4.24.-)

 ATS20_MOUSE             Reviewed;        1906 AA.
P59511; E9QLA1;
04-APR-2003, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
07-NOV-2018, entry version 133.
RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 20;
Short=ADAM-TS 20;
Short=ADAM-TS20;
Short=ADAMTS-20;
EC=3.4.24.-;
Flags: Precursor;
Name=Adamts20;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fetal brain;
PubMed=12562771; DOI=10.1074/jbc.M211900200;
Llamazares M., Cal S., Quesada V., Lopez-Otin C.;
"Identification and characterization of ADAMTS-20 defines a novel
subfamily of metalloproteinases-disintegrins with multiple
thrombospondin-1 repeats and a unique GON domain.";
J. Biol. Chem. 278:13382-13389(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND DISEASE.
STRAIN=DBA/2J;
PubMed=12925592; DOI=10.1242/dev.00668;
Rao C., Foernzler D., Loftus S.K., Liu S., McPherson J.D.,
Jungers K.A., Apte S.S., Pavan W.J., Beier D.R.;
"A defect in a novel ADAMTS family member is the cause of the belted
white-spotting mutation.";
Development 130:4665-4672(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
-!- FUNCTION: May play a role in tissue-remodeling process occurring
in both normal and pathological conditions. May have a protease-
independent function in the transport from the endoplasmic
reticulum to the Golgi apparatus of secretory cargos, mediated by
the GON domain.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=ADAMTS20 B long isoform;
IsoId=P59511-1; Sequence=Displayed;
Name=2; Synonyms=ADAMTS20 A short isoform;
IsoId=P59511-2; Sequence=VSP_007606, VSP_007607;
-!- TISSUE SPECIFICITY: Expressed at low level in testis and brain.
-!- PTM: The precursor is cleaved by a furin endopeptidase.
{ECO:0000250}.
-!- PTM: Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a
threonine residue found within the consensus sequence C1-X(2)-
(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are
the first and second cysteine residue of the repeat, respectively.
Fucosylated repeats can then be further glycosylated by the
addition of a beta-1,3-glucose residue by the glucosyltransferase,
B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS
family members. Also can be C-glycosylated with one or two mannose
molecules on tryptophan residues within the consensus sequence W-
X-X-W of the TPRs, and N-glycosylated. These other glycosylations
can also facilitate secretion (By similarity). {ECO:0000250}.
-!- DISEASE: Note=Defects in Adamts20 are the cause of the belted (bt)
phenotype. It is a pigmental defect which occurs as a result of a
defect in melanocyte development. {ECO:0000269|PubMed:12925592}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AJ512753; CAD54808.3; -; mRNA.
EMBL; AY189815; AAO74895.1; -; mRNA.
EMBL; AY189816; AAO74896.1; -; mRNA.
EMBL; AC084382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC084384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS27770.1; -. [P59511-1]
CCDS; CCDS49711.1; -. [P59511-2]
RefSeq; NP_803180.3; NM_177431.5. [P59511-1]
UniGene; Mm.214132; -.
ProteinModelPortal; P59511; -.
SMR; P59511; -.
STRING; 10090.ENSMUSP00000036330; -.
MEROPS; M12.188; -.
PhosphoSitePlus; P59511; -.
PaxDb; P59511; -.
PeptideAtlas; P59511; -.
PRIDE; P59511; -.
Ensembl; ENSMUST00000035342; ENSMUSP00000036330; ENSMUSG00000022449. [P59511-1]
Ensembl; ENSMUST00000155907; ENSMUSP00000121696; ENSMUSG00000022449. [P59511-2]
GeneID; 223838; -.
KEGG; mmu:223838; -.
UCSC; uc007xje.2; mouse. [P59511-1]
UCSC; uc007xjf.2; mouse. [P59511-2]
CTD; 80070; -.
MGI; MGI:2660628; Adamts20.
eggNOG; KOG3538; Eukaryota.
eggNOG; ENOG410XPKZ; LUCA.
GeneTree; ENSGT00930000150848; -.
HOGENOM; HOG000004798; -.
HOVERGEN; HBG037334; -.
InParanoid; P59511; -.
KO; K09609; -.
OMA; AREKCDT; -.
OrthoDB; EOG091G00AX; -.
TreeFam; TF331949; -.
Reactome; R-MMU-5173214; O-glycosylation of TSR domain-containing proteins.
ChiTaRS; Adamts20; mouse.
PRO; PR:P59511; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000022449; Expressed in 171 organ(s), highest expression level in semi-lunar valve.
Genevisible; P59511; MM.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0004175; F:endopeptidase activity; IDA:MGI.
GO; GO:0004222; F:metalloendopeptidase activity; IDA:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
GO; GO:0045636; P:positive regulation of melanocyte differentiation; IMP:MGI.
GO; GO:0009967; P:positive regulation of signal transduction; IMP:MGI.
GO; GO:0006508; P:proteolysis; IDA:MGI.
GO; GO:0048070; P:regulation of developmental pigmentation; IMP:MGI.
Gene3D; 2.20.100.10; -; 11.
Gene3D; 3.40.390.10; -; 1.
InterPro; IPR010294; ADAM_spacer1.
InterPro; IPR013273; ADAMTS/ADAMTS-like.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR012314; Pept_M12B_GON-ADAMTSs.
InterPro; IPR001590; Peptidase_M12B.
InterPro; IPR002870; Peptidase_M12B_N.
InterPro; IPR000884; TSP1_rpt.
InterPro; IPR036383; TSP1_rpt_sf.
Pfam; PF05986; ADAM_spacer1; 1.
Pfam; PF08685; GON; 1.
Pfam; PF01562; Pep_M12B_propep; 1.
Pfam; PF01421; Reprolysin; 1.
Pfam; PF00090; TSP_1; 11.
PRINTS; PR01857; ADAMTSFAMILY.
SMART; SM00209; TSP1; 14.
SUPFAM; SSF82895; SSF82895; 13.
PROSITE; PS50215; ADAM_MEPRO; 1.
PROSITE; PS51046; GON; 1.
PROSITE; PS50092; TSP1; 13.
PROSITE; PS00142; ZINC_PROTEASE; 1.
2: Evidence at transcript level;
Alternative splicing; Cleavage on pair of basic residues;
Complete proteome; Disulfide bond; Extracellular matrix; Glycoprotein;
Hydrolase; Metal-binding; Metalloprotease; Protease;
Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
SIGNAL 1 26 {ECO:0000255}.
PROPEP 27 249 {ECO:0000250}.
/FTId=PRO_0000029208.
CHAIN 250 1906 A disintegrin and metalloproteinase with
thrombospondin motifs 20.
/FTId=PRO_0000029209.
DOMAIN 255 464 Peptidase M12B. {ECO:0000255|PROSITE-
ProRule:PRU00276}.
DOMAIN 465 552 Disintegrin.
DOMAIN 553 608 TSP type-1 1. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 843 901 TSP type-1 2. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 906 962 TSP type-1 3. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 962 1015 TSP type-1 4. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 1017 1074 TSP type-1 5. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 1075 1131 TSP type-1 6. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 1148 1202 TSP type-1 7. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 1203 1260 TSP type-1 8. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 1300 1351 TSP type-1 9. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 1354 1411 TSP type-1 10. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 1412 1465 TSP type-1 11. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 1468 1526 TSP type-1 12. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 1527 1584 TSP type-1 13. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 1585 1648 TSP type-1 14. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 1650 1706 TSP type-1 15. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 1707 1906 GON. {ECO:0000255|PROSITE-
ProRule:PRU00383}.
REGION 721 842 Spacer.
COMPBIAS 609 720 Cys-rich.
ACT_SITE 400 400 {ECO:0000255|PROSITE-ProRule:PRU00276,
ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 399 399 Zinc; catalytic. {ECO:0000250}.
METAL 403 403 Zinc; catalytic. {ECO:0000250}.
METAL 409 409 Zinc; catalytic. {ECO:0000250}.
CARBOHYD 92 92 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 221 221 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 714 714 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 798 798 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 805 805 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1057 1057 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1562 1562 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1719 1719 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1759 1759 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1777 1777 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 330 383 {ECO:0000250}.
DISULFID 359 365 {ECO:0000250}.
DISULFID 377 459 {ECO:0000250}.
DISULFID 415 443 {ECO:0000250}.
DISULFID 486 508 {ECO:0000250}.
DISULFID 497 518 {ECO:0000250}.
DISULFID 503 537 {ECO:0000250}.
DISULFID 531 542 {ECO:0000250}.
DISULFID 565 602 {ECO:0000250}.
DISULFID 569 607 {ECO:0000250}.
DISULFID 580 592 {ECO:0000250}.
VAR_SEQ 1424 1425 CS -> VR (in isoform 2).
{ECO:0000303|PubMed:12925592}.
/FTId=VSP_007606.
VAR_SEQ 1426 1906 Missing (in isoform 2).
{ECO:0000303|PubMed:12925592}.
/FTId=VSP_007607.
CONFLICT 1211 1211 D -> Y (in Ref. 2; AAO74895/AAO74896).
{ECO:0000305}.
CONFLICT 1262 1262 L -> S (in Ref. 1; CAD54808).
{ECO:0000305}.
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


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