ATS18_MOUSE
ID ATS18_MOUSE Reviewed; 1219 AA.
AC Q4VC17; E9QNK0; Q8BZD1;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 18;
DE Short=ADAM-TS 18;
DE Short=ADAM-TS18;
DE Short=ADAMTS-18;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=Adamts18;
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 [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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-497.
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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 -!- 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; AC108856; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC125463; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC094674; AAH94674.1; -; mRNA.
DR EMBL; AK035797; BAC29190.1; -; mRNA.
DR CCDS; CCDS40485.1; -.
DR RefSeq; NP_766054.2; NM_172466.3.
DR AlphaFoldDB; Q4VC17; -.
DR SMR; Q4VC17; -.
DR BioGRID; 229026; 1.
DR STRING; 10090.ENSMUSP00000090801; -.
DR MEROPS; M12.030; -.
DR GlyGen; Q4VC17; 6 sites.
DR iPTMnet; Q4VC17; -.
DR PhosphoSitePlus; Q4VC17; -.
DR PaxDb; Q4VC17; -.
DR PRIDE; Q4VC17; -.
DR Antibodypedia; 30389; 157 antibodies from 24 providers.
DR DNASU; 208936; -.
DR Ensembl; ENSMUST00000093113; ENSMUSP00000090801; ENSMUSG00000053399.
DR GeneID; 208936; -.
DR KEGG; mmu:208936; -.
DR UCSC; uc009nnr.1; mouse.
DR CTD; 170692; -.
DR MGI; MGI:2442600; Adamts18.
DR VEuPathDB; HostDB:ENSMUSG00000053399; -.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000157553; -.
DR HOGENOM; CLU_000660_1_0_1; -.
DR InParanoid; Q4VC17; -.
DR OMA; CRNIKRP; -.
DR OrthoDB; 125522at2759; -.
DR PhylomeDB; Q4VC17; -.
DR TreeFam; TF313537; -.
DR Reactome; R-MMU-5173214; O-glycosylation of TSR domain-containing proteins.
DR BioGRID-ORCS; 208936; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q4VC17; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q4VC17; protein.
DR Bgee; ENSMUSG00000053399; Expressed in epithelium of lens and 76 other tissues.
DR ExpressionAtlas; Q4VC17; baseline and differential.
DR Genevisible; Q4VC17; MM.
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:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0001654; P:eye development; ISO:MGI.
DR GO; GO:0090331; P:negative regulation of platelet aggregation; IMP:MGI.
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; 6.
DR SUPFAM; SSF82895; SSF82895; 5.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 5.
PE 2: Evidence at transcript level;
KW Disulfide bond; Extracellular matrix; Glycoprotein; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Repeat;
KW Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..47
FT /evidence="ECO:0000255"
FT PROPEP 48..284
FT /evidence="ECO:0000250"
FT /id="PRO_0000437534"
FT CHAIN 285..1219
FT /note="A disintegrin and metalloproteinase with
FT thrombospondin motifs 18"
FT /id="PRO_0000042164"
FT DOMAIN 293..498
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 589..644
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 931..990
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 991..1049
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1052..1116
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1121..1176
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1182..1219
FT /note="PLAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00233"
FT REGION 217..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 437
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 436
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 440
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 446
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 745
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 838
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 865
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 909
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 369..420
FT /evidence="ECO:0000250"
FT DISULFID 395..402
FT /evidence="ECO:0000250"
FT DISULFID 414..493
FT /evidence="ECO:0000250"
FT DISULFID 453..477
FT /evidence="ECO:0000250"
FT DISULFID 521..546
FT /evidence="ECO:0000250"
FT DISULFID 532..553
FT /evidence="ECO:0000250"
FT DISULFID 541..572
FT /evidence="ECO:0000250"
FT DISULFID 566..577
FT /evidence="ECO:0000250"
FT DISULFID 601..638
FT /evidence="ECO:0000250"
FT DISULFID 605..643
FT /evidence="ECO:0000250"
FT DISULFID 616..628
FT /evidence="ECO:0000250"
FT CONFLICT 96
FT /note="S -> P (in Ref. 2; AAH94674)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="H -> L (in Ref. 2; AAH94674)"
FT /evidence="ECO:0000305"
FT CONFLICT 487..497
FT /note="STPQAGCLVDE -> RTPRCIAFLTG (in Ref. 3; BAC29190)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1219 AA; 135244 MW; 22D0A535E55553A2 CRC64;
MECALLCLCA LRAAGPGPPW GPAGLGRLAK ALQLCCFCCA SVAVALASDS GSSGGSGLND
DYVFVVPVEV DSGGSYISHD ILHHRKRRSA HGASNSLHYR VSAFGQDLHL ELKPSAILSS
HFRVQVLGKD GASETREPEV PQCLYQGFIR NDSSSSVAVS TCAGLSGLIR TRDNEFLISP
LPQLLAQEHN YSSPAGHHPH VLYKRTAEKR VRWYQDYPGS QRTYPGHSPS HTPPASQSQE
PEYSHRRWQK RHFCGRRKKY APKPPAEDAY LRFDEYGGTG RPRRSAGKSQ NGLNVETLVV
ADAKMVEKHG KDDVTTYILT VMNMVSSLFK DGTIGSDINI VVVSLILLEE EPEGLLINHH
ADQSLNSFCQ WQSALVGKNG KRHDHAILLT GFDICSWKNE PCDTLGFAPI SGMCSKYRSC
TINEDTGLGL AFTIAHESGH NFGMVHDGEG NPCRKAEGNI MSPTLTGNNG VFSWSSCSRQ
YLKKFLSTPQ AGCLVDEPKQ TGQYKYPDKL PGQIYDADMQ CKWQFGAKAK LCSLGVMKDI
CKSLWCHRVG HRCETKFMPA AEGTACGLSM WCRQGQCVKL GELGPRPIHG QWSAWSKWSE
CSRTCGGGVK FQERHCSNPK PQYGGKYCPG SSRIYKLCNI NPCPENSLDF RAQQCAEYNN
KPFRGWLYRW KPYTKVEEED RCKLYCKAEN FEFFFAMSGK VKDGTPCSPH RNDVCIDGIC
ELVGCDHELG SKAVSDACGV CKGDNSTCKF YKGLYLSQHK ANEYYPVVTI PAGARSIEIQ
ELQLSSSYLA VRSLSQKYYL TGGWSIDWPG DFTFAGTTFE YQRSFNRPER LYAPGPTNET
LVFEILTQGK NPGIAWKYAL PKVMNVTQPA TKRYHHTWRT VQSDCSVTCG GGYISIKAIC
LRDQHTQVNS SFCSVRTKPA TEPKICNAFS CPAYWLPGEW SACSKSCAGG QQSRKIRCVQ
KKPFQKEEAV LHSLCPVSTP TQVQVCNSHA CPPEWSPSPW SQCSKTCGRG VRRREVLCKS
PAAETLPESL CSSSPRPEAQ EGCVLGRCPK NNRLQWIASA WSECSATCGL GVRKRELKCV
EKTLQGKLIT FPERRCRNIK KPSLELEEAC NQRTCPVYSM AVASWYSSPW QQCTVTCGGG
VQTRSVHCMQ QGRPSSSCLL HQKPPVLRAC NTNFCPAPEK KDDPSCVDFF SWCHLVPQHG
VCNHKFYGKQ CCRSCTRKS
