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Database: UniProt
Entry: ATS18_MOUSE
LinkDB: ATS18_MOUSE
Original site: 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   08-MAY-2019, entry version 115.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the 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
RT   project: 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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.
CC       {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)-
CC       (S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are
CC       the first and second cysteine residue of the repeat, respectively.
CC       Fucosylated repeats can then be further glycosylated by the
CC       addition of a beta-1,3-glucose residue by the glucosyltransferase,
CC       B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS
CC       family members. Also can be C-glycosylated with one or two mannose
CC       molecules on tryptophan residues within the consensus sequence W-
CC       X-X-W of the TPRs, and N-glycosylated. These other glycosylations
CC       can also facilitate secretion (By similarity). {ECO:0000250}.
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   SMR; Q4VC17; -.
DR   STRING; 10090.ENSMUSP00000090801; -.
DR   MEROPS; M12.030; -.
DR   iPTMnet; Q4VC17; -.
DR   PhosphoSitePlus; Q4VC17; -.
DR   PaxDb; Q4VC17; -.
DR   PRIDE; Q4VC17; -.
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   eggNOG; KOG3538; Eukaryota.
DR   eggNOG; ENOG410XPKZ; LUCA.
DR   GeneTree; ENSGT00940000157553; -.
DR   HOGENOM; HOG000004800; -.
DR   InParanoid; Q4VC17; -.
DR   KO; K08632; -.
DR   OMA; YQERHCN; -.
DR   OrthoDB; 125522at2759; -.
DR   TreeFam; TF313537; -.
DR   Reactome; R-MMU-5173214; O-glycosylation of TSR domain-containing proteins.
DR   PRO; PR:Q4VC17; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   Bgee; ENSMUSG00000053399; Expressed in 71 organ(s), highest expression level in epithelium of lens.
DR   ExpressionAtlas; Q4VC17; baseline and differential.
DR   Genevisible; Q4VC17; MM.
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; IEA:InterPro.
DR   GO; GO:0001654; P:eye development; ISO:MGI.
DR   GO; GO:0090331; P:negative regulation of platelet aggregation; IMP:MGI.
DR   Gene3D; 2.20.100.10; -; 5.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR041645; ADAM_CR_2.
DR   InterPro; IPR010294; ADAM_spacer1.
DR   InterPro; IPR013273; ADAMTS/ADAMTS-like.
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; 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; 5.
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   Complete proteome; Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL        1     47       {ECO:0000255}.
FT   PROPEP       48    284       {ECO:0000250}.
FT                                /FTId=PRO_0000437534.
FT   CHAIN       285   1219       A disintegrin and metalloproteinase with
FT                                thrombospondin motifs 18.
FT                                /FTId=PRO_0000042164.
FT   DOMAIN      293    498       Peptidase M12B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00276}.
FT   DOMAIN      589    644       TSP type-1 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      931    990       TSP type-1 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      991   1049       TSP type-1 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN     1052   1116       TSP type-1 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN     1121   1176       TSP type-1 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN     1182   1219       PLAC. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00233}.
FT   COMPBIAS    153    156       Poly-Ser.
FT   ACT_SITE    437    437       {ECO:0000255|PROSITE-ProRule:PRU00276}.
FT   METAL       436    436       Zinc; catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00276}.
FT   METAL       440    440       Zinc; catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00276}.
FT   METAL       446    446       Zinc; catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00276}.
FT   CARBOHYD    151    151       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    190    190       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    745    745       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    838    838       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    865    865       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    909    909       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    369    420       {ECO:0000250}.
FT   DISULFID    395    402       {ECO:0000250}.
FT   DISULFID    414    493       {ECO:0000250}.
FT   DISULFID    453    477       {ECO:0000250}.
FT   DISULFID    521    546       {ECO:0000250}.
FT   DISULFID    532    553       {ECO:0000250}.
FT   DISULFID    541    572       {ECO:0000250}.
FT   DISULFID    566    577       {ECO:0000250}.
FT   DISULFID    601    638       {ECO:0000250}.
FT   DISULFID    605    643       {ECO:0000250}.
FT   DISULFID    616    628       {ECO:0000250}.
FT   CONFLICT     96     96       S -> P (in Ref. 2; AAH94674).
FT                                {ECO:0000305}.
FT   CONFLICT    189    189       H -> L (in Ref. 2; AAH94674).
FT                                {ECO:0000305}.
FT   CONFLICT    487    497       STPQAGCLVDE -> RTPRCIAFLTG (in Ref. 3;
FT                                BAC29190). {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
//
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