ID   ATS8_MOUSE              Reviewed;         905 AA.
AC   P57110;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   08-NOV-2023, entry version 158.
DE   RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 8;
DE            Short=ADAM-TS 8;
DE            Short=ADAM-TS8;
DE            Short=ADAMTS-8;
DE            EC=3.4.24.-;
DE   AltName: Full=METH-2;
DE   Flags: Precursor;
GN   Name=Adamts8;
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].
RX   PubMed=10610729; DOI=10.1006/geno.1999.6014;
RA   Georgiadis K.E., Hirohata S., Seldin M.F., Apte S.S.;
RT   "ADAM-TS8, a novel metalloprotease of the ADAM-TS family located on mouse
RT   chromosome 9 and human chromosome 11.";
RL   Genomics 62:312-315(1999).
CC   -!- FUNCTION: Has anti-angiogenic properties. {ECO:0000250}.
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   -!- TISSUE SPECIFICITY: Expressed specifically in adult lung and heart and
CC       low expression during mouse development.
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}.
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DR   EMBL; AF175282; AAF25805.1; -; mRNA.
DR   CCDS; CCDS22946.1; -.
DR   AlphaFoldDB; P57110; -.
DR   SMR; P57110; -.
DR   STRING; 10090.ENSMUSP00000069644; -.
DR   MEROPS; M12.226; -.
DR   GlyCosmos; P57110; 4 sites, No reported glycans.
DR   GlyGen; P57110; 4 sites.
DR   PhosphoSitePlus; P57110; -.
DR   PaxDb; 10090-ENSMUSP00000069644; -.
DR   ProteomicsDB; 273587; -.
DR   DNASU; 30806; -.
DR   AGR; MGI:1353468; -.
DR   MGI; MGI:1353468; Adamts8.
DR   eggNOG; KOG3538; Eukaryota.
DR   InParanoid; P57110; -.
DR   PhylomeDB; P57110; -.
DR   Reactome; R-MMU-5173214; O-glycosylation of TSR domain-containing proteins.
DR   PRO; PR:P57110; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P57110; Protein.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04273; ZnMc_ADAMTS_like; 1.
DR   Gene3D; 2.60.120.830; -; 1.
DR   Gene3D; 3.40.1620.60; -; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 2.
DR   InterPro; IPR006586; ADAM_Cys-rich.
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; IPR013277; Pept_M12B_ADAM-TS8.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   PANTHER; PTHR13723:SF41; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 8; 1.
DR   PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR   Pfam; PF17771; ADAMTS_CR_2; 1.
DR   Pfam; PF19236; ADAMTS_CR_3; 1.
DR   Pfam; PF05986; ADAMTS_spacer1; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   Pfam; PF19030; TSP1_ADAMTS; 1.
DR   Pfam; PF00090; TSP_1; 1.
DR   PRINTS; PR01861; ADAMTS8.
DR   PRINTS; PR01857; ADAMTSFAMILY.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00209; TSP1; 2.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF82895; TSP-1 type 1 repeat; 2.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS50092; TSP1; 2.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Disulfide bond; Extracellular matrix;
KW   Glycoprotein; Heparin-binding; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   PROPEP          29..228
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000029180"
FT   CHAIN           229..905
FT                   /note="A disintegrin and metalloproteinase with
FT                   thrombospondin motifs 8"
FT                   /id="PRO_0000029181"
FT   DOMAIN          234..444
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DOMAIN          453..541
FT                   /note="Disintegrin"
FT   DOMAIN          542..597
FT                   /note="TSP type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          848..904
FT                   /note="TSP type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   REGION          139..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          186..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          706..847
FT                   /note="Spacer"
FT   REGION          877..905
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        190..218
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        379
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         378
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         382
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         388
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        415
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        480
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        506
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        615
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        309..362
FT                   /evidence="ECO:0000250"
FT   DISULFID        338..344
FT                   /evidence="ECO:0000250"
FT   DISULFID        356..439
FT                   /evidence="ECO:0000250"
FT   DISULFID        394..423
FT                   /evidence="ECO:0000250"
FT   DISULFID        478..502
FT                   /evidence="ECO:0000250"
FT   DISULFID        487..523
FT                   /evidence="ECO:0000250"
FT   DISULFID        517..528
FT                   /evidence="ECO:0000250"
FT   DISULFID        554..591
FT                   /evidence="ECO:0000250"
FT   DISULFID        558..596
FT                   /evidence="ECO:0000250"
FT   DISULFID        569..581
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   905 AA;  98880 MW;  124D4132B33A0CAE CRC64;
     MLRDPTTTGW PPLLLLLLQL PPPPLVCGAP AGPGTGAQAS ELVVPTRLPG SASELAFHLS
     AFGQGFVLRL APDASFLAPE FKIERLGGSS AAAGGEPGLR GCFFSGTVNG ERESLAAMSC
     VAGWSGSFLL AGEEFTIQPQ GAGDSLDQPH RLQRWGPGQR REDPGLAAAE VFPLPQGLEW
     EVEMGNGQGQ ERSDNEEDRK QDKEGLLKET EDSRKVPPPF GSKTRSKRFV SEARFVETLL
     VADASMAAFY GTDLQNHILT VMSMAARIYK HPSIRNSVNL VVVKVLIVEK ERWGPEVSDN
     GGLTLRNFCS WQRRFNKPSD RHPEHYDTAI LFTRQNFCGK GEQCDTLGMA DVGTICDPDK
     SCSVIKDEGL QAAYTLAHEL GHVLSMPHDD SKPCVRLFGP MGKYHMMAPF FIHVNKTLPW
     SPCSAVYLTE LLDDGHGDCL LDAPTSVLPL PTGLPGHSTL YELDQQCKQI FGPDFRHCPN
     TSVEDICVQL CARHRDSDEP ICHTKNGSLL WADGTPCGPG HLCLDGSCVL KEDVENPKAV
     VDGDWGPWRP WGQCSRTCGG GIQFSNRECD NPMPQNGGRF CLGERVKYQS CNTEECPPNG
     KSFREQQCEK YNAYNHTDLD GNFLQWVPKY SGVSPRDRCK LFCRARGRSE FKVFEAKVID
     GTLCGPDTLS ICVRGQCVKA GCDHVVNSPK KLDKCGVCGG KGTACRKISG SFTPFSYGYN
     DIVTIPAGAT NIDVKQRSHP GVRNDGSYLA LKTANGQYLL NGNLAISAIE QDILVKGTIL
     KYSGSMATLE RLQSFQALPE PLTVQLLTVS GEVFPPKVRY TFFVPNDMDF SVQNSKERAT
     TNIIQSLPSA EWVLGDWSEC PSTCRGSWQR RTVECRDPSG QASDTCDEAL KPEDAKPCGS
     QPCPL
//