ID F7H0I0_MACMU Unreviewed; 1935 AA. AC F7H0I0; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 30-NOV-2016, sequence version 2. DT 03-AUG-2022, entry version 75. DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 9 {ECO:0000313|Ensembl:ENSMMUP00000039566}; GN Name=ADAMTS9 {ECO:0000313|Ensembl:ENSMMUP00000039566, GN ECO:0000313|VGNC:VGNC:69388}; 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:ENSMMUP00000039566, ECO:0000313|Proteomes:UP000006718}; RN [1] {ECO:0000313|Ensembl:ENSMMUP00000039566, ECO:0000313|Proteomes:UP000006718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000039566, 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:ENSMMUP00000039566} RP IDENTIFICATION. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000039566}; RG Ensembl; RL Submitted (JUL-2011) 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 --------------------------------------------------------------------------- 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 RefSeq; XP_014985954.1; XM_015130468.1. DR STRING; 9544.ENSMMUP00000039566; -. DR MEROPS; M12.021; -. DR Ensembl; ENSMMUT00000046533.3; ENSMMUP00000039566.2; ENSMMUG00000000265.4. DR GeneID; 698341; -. DR KEGG; mcc:698341; -. DR CTD; 56999; -. DR VEuPathDB; HostDB:ENSMMUG00000000265; -. DR VGNC; VGNC:69388; ADAMTS9. DR eggNOG; KOG3538; Eukaryota. DR GeneTree; ENSGT00940000156409; -. DR InParanoid; F7H0I0; -. DR OrthoDB; 125522at2759; -. DR TreeFam; TF331949; -. DR Proteomes; UP000006718; Chromosome 2. DR Bgee; ENSMMUG00000000265; Expressed in adipose tissue and 19 other tissues. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl. DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central. DR GO; GO:0005615; C:extracellular space; IEA:Ensembl. 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:0030318; P:melanocyte differentiation; IEA:Ensembl. DR GO; GO:0045636; P:positive regulation of melanocyte differentiation; IEA:Ensembl. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl. DR Gene3D; 2.20.100.10; -; 13. 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; IPR012314; Pept_M12B_GON-ADAMTSs. 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; PF08685; GON; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR Pfam; PF00090; TSP_1; 1. DR PRINTS; PR01857; ADAMTSFAMILY. DR SMART; SM00209; TSP1; 15. DR SUPFAM; SSF82895; SSF82895; 14. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS51046; GON; 1. DR PROSITE; PS50092; TSP1; 14. 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 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..18 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 19..1935 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5008957274" FT DOMAIN 293..499 FT /note="Peptidase M12B" FT /evidence="ECO:0000259|PROSITE:PS50215" FT DOMAIN 1735..1935 FT /note="GON" FT /evidence="ECO:0000259|PROSITE:PS51046" FT REGION 192..242 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1289..1330 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1289..1306 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1313..1330 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 435 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1" FT BINDING 223 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /note="in inhibited form" FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2" 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 383 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2" FT BINDING 434 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2" FT BINDING 438 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2" FT BINDING 444 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2" FT BINDING 494 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2" FT DISULFID 368..418 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 394..400 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 412..494 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 450..478 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 521..543 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 532..553 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 538..572 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 566..577 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 600..637 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 604..642 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 615..627 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" SQ SEQUENCE 1935 AA; 216557 MW; C3A6C7D96FD41F27 CRC64; MQFVSWATLL TLLVRDLAEM GIPDAAAAVR KDRLHPRQVK LLETLSEYEI VSPIRVNALG EPFPTNVHFK RRRRSINSAT DPWPAFASSS SSSTSSQAHY RLSAFGQQFL FNLTANAGFI APLFTVTLLG TPGVNQTKFY SEEEAELKHC FYKGYVNTKS EHTAVISLCS GMLGTFRSYD GDYFIEPLQS MDEQEDEEEQ NKPHIIYRRS TPQREPSTGR HACDTSEHKN RHSKDKKKTR ARKWGERINL ADDVAALNSG LATEAFSAYG NKTDNTTEKR THRRTKRFLS YPRFVEVLVV ADNRMVSYHG ENLQHYILTL MSIVASIYKD PSIGNLINIV IVNLIVIHNE QDGPSISFNA QTTLKNFCQW QHSKNSPGGI HHDTAVLLTR QDICRAHDKC DTLGLAELGT ICDPYRSCSI SEDSGLSTAF TIAHELGHVF NMPHDDNNKC KEEGVKSPQH VMAPTLNFYT NPWMWSKCSR KYITEFLDTG YGECLLNEPE SRPYPLPVQL PGILYNVNKQ CELIFGPGSQ VCPYMMQCRR LWCNNVNGVH KGCRTQHTPW ADGTECEPGK HCKYGFCVPK EMDVPVTDGS WGSWSPFGTC SRTCGGGIKT AIRECNRPEP KNGGKYCVGR RMKFKSCNTE PCLKQKRDFR DEQCAHFDGK HFNINGLLPN VRWVPKYSGI LMKDRCKLFC RVAGNTAYYQ LRDRVIDGTP CGQDTNDICV QGLCRQAGCD HVLNSKARRD KCGVCGGDNS SCKTVAGTFN TVHYGYNTVV RIPAGATNID VRQHSFSGET DDDNYLALSS SKGEFLLNGN FVVTMAKREI RIGNAVVEYS GSETAVERIN STDRIEQELL LQVLSVGKLY NPDVRYSFNI PIEDKPQQFY WNSHGPWQAC SKPCQGERKR KLVCTRESDQ LTVSDQRCDR LPQPGPITEP CGTDCDLRWH VASRSECSAQ CGLGYRTLDI YCAKYSRLDG KTEKVDDGFC SSHPKPSNRE KCSGECNTGG WRYSAWTECS KSCDGGTQRR RAICVNTRND VLDDSKCTHQ EKVTIQRCSE FPCPQWKSGD WSECLVTCGK GHKHRQVWCQ FGEDRLNDRM CDPETKPTSM QTCQQPECAS WQAGPWGQCS VTCGQGYQLR AVKCIIGTYM SVVDDNDCNA ATRPTDTQDC ELPSCHPPPA APETRRSTYS APRTQWRFGS WTPCSATCGK GTRMRYVSCR DENGSVADES ACATLPRPVA KEECSVTPCG QWKALDWSSC SVTCGQGRAT RQVVCVNYSD HVIDRSECDQ DYIPETDQDC SMSPCPQRTP DSGLAQHPFQ NEDYRPRSAS PSRTHVLGGN QWRTGPWGAC SSTCAGGSQR RVVVCQDENG YTANDCVERI KPDEQRACES GPCPQWAYGN WGECTKLCGG GIRTRLVVCQ RSNGERFPDL SCEILDKPPD REQCNTHACP HDAAWSTGPW SSCSVSCGRG HKQRNVYCMA KDGSHLESDY CKHLAKPHGH RKCRGGRCPK WKTGAWSQCS VSCGRGVQQR HVGCQIGTHK IARETECNPY TRPESERDCQ GPRCPLYTWR AEEWQECTKT CGEGSRYRKV VCVDDSKNEV HGARCDVSKR PADHESCSLQ PCEYVWITGE WSECSVTCGK GYKQRLVSCS EIYTGKENYE YSYQTTVNCP GTQPPSVHPC YLRECPVSAT WRVGNWGSCS VSCGVGVMQR SVQCLTNEDQ PSHLCHTDLK PEERKTCRNI YNCELPQNCK EVKRLKGASE DGEYFLMIRG KLLKIFCAGM HSDHPKEYVT LVHGDSENFS EVYGHRLHNP TECPYNGSRR DDCQCRKDYT AAGFSSFQKI RIDLTSMQII TTDLQFARTS EGHPVPFATA GDCYSAAKCP QGRFSINLYG TGLSLTESAR WISQGNYAVS DIKKSPDGTR VIGKCGGYCG KCTPSSGTGL EVRVL //