ATS8_MOUSE
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 03-AUG-2022, entry version 154.
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 GlyGen; P57110; 4 sites.
DR PhosphoSitePlus; P57110; -.
DR PaxDb; P57110; -.
DR PRIDE; P57110; -.
DR ProteomicsDB; 273587; -.
DR DNASU; 30806; -.
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 Gene3D; 2.20.100.10; -; 2.
DR Gene3D; 3.40.390.10; -; 1.
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 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; PF01421; Reprolysin; 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; SSF82895; SSF82895; 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
