ID F6Q262_MACMU Unreviewed; 1221 AA. AC F6Q262; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 30-NOV-2016, sequence version 2. DT 22-FEB-2023, entry version 73. DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 18 {ECO:0000313|Ensembl:ENSMMUP00000001117.3}; GN Name=ADAMTS18 {ECO:0000313|VGNC:VGNC:69442}; OS Macaca mulatta (Rhesus macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; OC Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000001117.3, ECO:0000313|Proteomes:UP000006718}; RN [1] {ECO:0000313|Ensembl:ENSMMUP00000001117.3, ECO:0000313|Proteomes:UP000006718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000001117.3, RC ECO:0000313|Proteomes:UP000006718}; RX PubMed=17431167; DOI=10.1126/science.1139247; RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M., RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K., RA Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C., RA Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A., RA Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J., RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H., RA Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J., RA Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., RA Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S., RA Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V., RA Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C., RA Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J., RA Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R., RA Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L., RA Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X., RA Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P., RA Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L., RA Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H., RA Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E., RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J., RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J., RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A., RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A., RA Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A., RA Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D., RA Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y., RA Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N., RA Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E., RA Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P., RA Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D., RA Kuhn R.M., Smith K.E., Zwieg A.S.; RT "Evolutionary and biomedical insights from the rhesus macaque genome."; RL Science 316:222-234(2007). RN [2] {ECO:0000313|Ensembl:ENSMMUP00000001117.3} RP IDENTIFICATION. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000001117.3}; RG Ensembl; RL Submitted (OCT-2022) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR613273-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR613273-2}; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix {ECO:0000256|ARBA:ARBA00004498}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR AlphaFoldDB; F6Q262; -. DR STRING; 9544.ENSMMUP00000001117; -. DR MEROPS; M12.028; -. DR Ensembl; ENSMMUT00000001190.4; ENSMMUP00000001117.3; ENSMMUG00000000824.4. DR VEuPathDB; HostDB:ENSMMUG00000000824; -. DR VGNC; VGNC:69442; ADAMTS18. DR eggNOG; KOG3538; Eukaryota. DR GeneTree; ENSGT00940000157553; -. DR HOGENOM; CLU_000660_1_0_1; -. DR InParanoid; F6Q262; -. DR TreeFam; TF313537; -. DR Proteomes; UP000006718; Chromosome 20. DR Bgee; ENSMMUG00000000824; Expressed in olfactory segment of nasal mucosa and 8 other tissues. DR ExpressionAtlas; F6Q262; baseline. 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; IEA:Ensembl. DR GO; GO:0090331; P:negative regulation of platelet aggregation; IEA:Ensembl. 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; 5. 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 PANTHER; PTHR13723:SF167; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 18; 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; PF08686; PLAC; 1. DR Pfam; PF01421; Reprolysin; 1. DR Pfam; PF19030; TSP1_ADAMTS; 4. DR Pfam; PF00090; TSP_1; 1. DR PRINTS; PR01857; ADAMTSFAMILY. DR SMART; SM00209; TSP1; 6. DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1. DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 5. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50900; PLAC; 1. DR PROSITE; PS50092; TSP1; 5. PE 4: Predicted; KW Calcium {ECO:0000256|PIRSR:PIRSR613273-2}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, KW ECO:0000256|PIRSR:PIRSR613273-3}; KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR613273-2}; KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049}; KW Protease {ECO:0000256|ARBA:ARBA00022670}; KW Reference proteome {ECO:0000313|Proteomes:UP000006718}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2}; KW Zymogen {ECO:0000256|ARBA:ARBA00023145}. FT SIGNAL 1..16 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 17..1221 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5003344473" FT DOMAIN 293..498 FT /note="Peptidase M12B" FT /evidence="ECO:0000259|PROSITE:PS50215" FT DOMAIN 1184..1221 FT /note="PLAC" FT /evidence="ECO:0000259|PROSITE:PS50900" FT REGION 216..291 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 216..237 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 437 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1, FT ECO:0000256|PROSITE-ProRule:PRU00276" FT BINDING 296 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2" FT BINDING 296 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2" FT BINDING 384 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2" FT BINDING 436 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2, FT ECO:0000256|PROSITE-ProRule:PRU00276" FT BINDING 440 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2, FT ECO:0000256|PROSITE-ProRule:PRU00276" FT BINDING 446 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2, FT ECO:0000256|PROSITE-ProRule:PRU00276" FT BINDING 493 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2" FT BINDING 496 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2" FT BINDING 496 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2" FT DISULFID 369..420 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 395..402 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 414..493 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 453..477 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 521..546 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 532..553 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 541..572 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 566..577 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 601..638 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 605..643 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 616..628 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" SQ SEQUENCE 1221 AA; 135080 MW; F8FC3790D808CC55 CRC64; MECALLLACA LPAAGSGPPR GPAGLGRVAK ALQLCCLCCA SVAAALASDS SSGASGLNDD YVFVTPVEVD SAGSYISHDI LHNGRKKRSA QNARSSLHYR FSAFGQELHL ELKPSAILSS HFIVQVVGKD GASETLKPEV QQCFYQGFIR NDSSSSVAVS TCAGLSGLIR TRKNEFLISP LPQLLAQEHN YSSPAGHHPH VLYKRTAEEK VQRYRGYPSS GQNYPGYSPS HIPHASQSQE TEYHHRRLQK QHFCGRRKKY APKPPTEDTY LRFDEYGSSG RPRRSAGKSQ KGLNVETLVV ADKKMVEKHG KGNVTTYILT VMNMVSGLFK DGTIGSDINV VVVSLILLEQ EPGGLLINHH ADQSLNSFCQ WQSALIGKNG KRHDHAILLT GFDICSWKNE PCDTLGFAPI SGMCSKYRSC TINEDTGLGL AFTIAHESGH NFGMIHDGEG NPCRKAEGNI MSPTLTGNNG VFSWSSCSRQ YLKKFLSTPQ AGCLVDEPKQ AGQYKYPDKL PGQIYDADTQ CKWQFGAKAK LCSLGFVKDI CKSLWCHRVG HRCETKFMPA AEGTVCGLSM WCRQGQCVKF GELGPRPIHG QWSAWSKWSE CSRTCGGGVK YQERHCNNPK PQYGGKFCPG SSRIYQLCNI NPCNENSLDF RAQQCAEYNS KPFRGWFYQW KPYTKVEEED RCKLYCKAEN FEFFFAMSGK VKDGTPCSPN KNDVCIDGVC ELVGCDHELG SKAVSDACGV CKGDNSTCKF YKGLYLNQHK ANEYYPVVII PAGARSIEIQ ELQVSSSYLA VRSLSQKYYL TGGWSIDWPG EFPFAGTTFE YQRSFNLPER LYAPGPTNET LVFEILMQGK NPGIAWKYAL PKVMNGTPPA TKRPAYAWSI VQSECPVSCG GGYINVKAIC LRDQNIQVNS SFCSVRTKPV TEPKICNAFS CPAYWMPGEW STCSKSCAGG QQSRKIQCVQ KKPFQKEEAV LHSLCPVSTP TQVQACNSHA CPPEWSLGPW SQCSKTCGRG VRRRELLCKG SAAETLPESQ CTSLPRPELQ EGCVLGRCPK NNRLQWVASS WSECSATCGL GVRKREIKCS EKGFQGKLIT FPERRCRNIK RPNLDLEETC NQRACPAHPV YNVVAGWYSS PWQQCTVTCG GGVQTRSVHC VQQGRPSSSC LLHQKPPVLR ACNTNFCPAP EKREDPSCVD FFNWCHLVPQ HGVCNHKFYG KQCCKSCTRK I //