true2004-07-192024-01-24183ADAM9_MOUSEMDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains.Weskamp G.Kraetzschmar J.Reid M.S.Blobel C.P.doi:10.1083/jcb.132.4.7171996J. Cell Biol.132717-726NUCLEOTIDE SEQUENCE [MRNA]LungPrediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries.Okazaki N.Kikuno R.Ohara R.Inamoto S.Aizawa H.Yuasa S.Nakajima D.Nagase T.Ohara O.Koga H.doi:10.1093/dnares/10.1.352003DNA Res.1035-48NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]BrainLineage-specific biology revealed by a finished genome assembly of the mouse.Church D.M.Goodstadt L.Hillier L.W.Zody M.C.Goldstein S.She X.Bult C.J.Agarwala R.Cherry J.L.DiCuccio M.Hlavina W.Kapustin Y.Meric P.Maglott D.Birtle Z.Marques A.C.Graves T.Zhou S.Teague B.Potamousis K.Churas C.Place M.Herschleb J.Runnheim R.Forrest D.Amos-Landgraf J.Schwartz D.C.Cheng Z.Lindblad-Toh K.Eichler E.E.Ponting C.P.doi:10.1371/journal.pbio.10001122009PLoS Biol.7E1000112NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]C57BL/6JThe status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).The MGC Project Teamdoi:10.1101/gr.25965042004Genome Res.142121-2127NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]FVB/N-3Mammary glandA metalloprotease-disintegrin participating in myoblast fusion.Yagami-Hiromasa T.Sato T.Kurisaki T.Kamijo K.Nabeshima Y.Fujisawa-Sehara A.doi:10.1038/377652a01995Nature377652-656NUCLEOTIDE SEQUENCE [MRNA] OF 426-575A family of cellular proteins related to snake venom disintegrins.Weskamp G.Blobel C.P.doi:10.1073/pnas.91.7.27481994Proc. Natl. Acad. Sci. U.S.A.912748-2751NUCLEOTIDE SEQUENCE [MRNA] OF 432-478BALB/cJMetalloprotease-disintegrin MDC9: intracellular maturation and catalytic activity.Roghani M.Becherer J.D.Moss M.L.Atherton R.E.Erdjument-Bromage H.Arribas J.Blackburn R.K.Weskamp G.Tempst P.Blobel C.P.doi:10.1074/jbc.274.6.35311999J. Biol. Chem.2743531-3540FUNCTIONCATALYTIC ACTIVITYPHOSPHORYLATIONACTIVITY REGULATIONPROTEIN SEQUENCE OF 206-212Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1.Howard L.Nelson K.K.Maciewicz R.A.Blobel C.P.doi:10.1074/jbc.274.44.316931999J. Biol. Chem.27431693-31699INTERACTION WITH SH3GL2 AND SNX9Meltrin gamma(ADAM-9) mediates cellular adhesion through alpha(6)beta(1)integrin, leading to a marked induction of fibroblast cell motility.Nath D.Slocombe P.M.Webster A.Stephens P.E.Docherty A.J.Murphy G.doi:10.1242/jcs.113.12.23192000J. Cell Sci.1132319-2328FUNCTIONINTERACTION WITH ITGA6Mice lacking the metalloprotease-disintegrin MDC9 (ADAM9) have no evident major abnormalities during development or adult life.Weskamp G.Cai H.Brodie T.A.Higashyama S.Manova K.Ludwig T.Blobel C.P.doi:10.1128/mcb.22.5.1537-1544.20022002Mol. Cell. Biol.221537-1544DISRUPTION PHENOTYPELoss of the metalloprotease ADAM9 leads to cone-rod dystrophy in humans and retinal degeneration in mice.Parry D.A.Toomes C.Bida L.Danciger M.Towns K.V.McKibbin M.Jacobson S.G.Logan C.V.Ali M.Bond J.Chance R.Swendeman S.Daniele L.L.Springell K.Adams M.Johnson C.A.Booth A.P.Jafri H.Rashid Y.Banin E.Strom T.M.Farber D.B.Sharon D.Blobel C.P.Pugh E.N. Jr.Pierce E.A.Inglehearn C.F.doi:10.1016/j.ajhg.2009.04.0052009Am. J. Hum. Genet.84683-691DISRUPTION PHENOTYPEADAM9 is involved in pathological retinal neovascularization.Guaiquil V.Swendeman S.Yoshida T.Chavala S.Campochiaro P.A.Blobel C.P.doi:10.1128/mcb.01460-082009Mol. Cell. Biol.292694-2703FUNCTIONMUTAGENESIS OF GLU-348A tissue-specific atlas of mouse protein phosphorylation and expression.Huttlin E.L.Jedrychowski M.P.Elias J.E.Goswami T.Rad R.Beausoleil S.A.Villen J.Haas W.Sowa M.E.Gygi S.P.doi:10.1016/j.cell.2010.12.0012010Cell1431174-1189IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]KidneyTestisThe functional maturation of a disintegrin and metalloproteinase (ADAM) 9, 10, and 17 requires processing at a newly identified proprotein convertase (PC) cleavage site.Wong E.Maretzky T.Peleg Y.Blobel C.P.Sagi I.doi:10.1074/jbc.m114.6240722015J. Biol. Chem.29012135-12146MUTAGENESIS OF ARG-53; ARG-56; ARG-202 AND ARG-205SUBCELLULAR LOCATIONACTIVITY REGULATIONDifferent initiation.234 N-Linked glycans (1 site)6 sites, 4 glycans6 sites, 4 N-linked glycans (1 site)404 antibodies from 35 providersmouseAdam9Eukaryota34740 hits in 39 CRISPR screensmouseProteinExpressed in endothelial cell of lymphatic vessel and 262 other cell types or tissuesbaseline and differentialZnMc_adamalysin_II_likeCollagenase (Catalytic Domain)Disintegrin domainADAM_Cys-richDisintegrin_CSDisintegrin_domDisintegrin_dom_sfEGF-like_domMetalloPept_cat_dom_sfPeptidase_M12BPeptidase_M12B_NReprolysin_adamalysinADAM A DISINTEGRIN AND METALLOPROTEASE DOMAINDISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 9ADAM_CRDisintegrinPep_M12B_propepReprolysinDISINTEGRINACRDISINBlood coagulation inhibitor (disintegrin)Metalloproteases ('zincins'), catalytic domainADAM_MEPRODISINTEGRIN_1DISINTEGRIN_2EGF_2EGF_3ZINC_PROTEASEMMDisintegrin and metalloproteinase domain-containing protein 9ADAM 93.4.24.-Meltrin-gammaMetalloprotease/disintegrin/cysteine-rich protein 9Myeloma cell metalloproteinaseAdam9Kiaa0021Mdc9MltngMetalloprotease that cleaves and releases a number of molecules with important roles in tumorigenesis and angiogenesis, such as TEK, KDR, EPHB4, CD40, VCAM1 and CDH5 (PubMed:9920899, PubMed:19273593). May mediate cell-cell, cell-matrix interactions and regulate the motility of cells via interactions with integrins (PubMed:10825303).Binds 1 zinc ion per subunit.Synthesized as an inactive form which is proteolytically cleaved to generate an active enzyme. Processing at the upstream site is particularly important for activation of the proenzyme, whereas processing at the boundary between the pro-domain and the catalytic domain does not appear to be essential (PubMed:25795784). Inhibited by hydroxamic acid-based inhibitors (PubMed:9920899).Interacts with SH3GL2 and SNX9 through its cytoplasmic tail (PubMed:10531379). Interacts with ITGA6 (PubMed:10825303).Proteolytically cleaved in the trans-Golgi network before it reaches the plasma membrane to generate a mature protein. The removal of the pro-domain occurs via cleavage at two different sites. Processed most likely by a pro-protein convertase such as furin, at the boundary between the pro-domain and the catalytic domain. An additional upstream cleavage pro-protein convertase site (Arg-56/Glu-57) has an important role in the activation of ADAM9.Phosphorylation is induced in vitro by phorbol-12-myristate-13-acetate (PMA) (PubMed:9920899).Deficient mice appear to develop normally, are viable and fertile, and do not have any major pathological phenotypes (PubMed:11839819). In adulthood, 20 months after birth, mice display progressive retinal degeneration, disorganized retinal layers and a degenerate retinal pigment epithelium (PubMed:19409519).Extended N-terminus.129Disintegrin and metalloproteinase domain-containing protein 98902330845Extracellular697Helical698718Cytoplasmic719Peptidase M12B212406Disintegrin414501EGF-like644Disordered729Pro residues752798348347351357Cleavage5657Cleavage; by furin-like protease205206N-linked (GlcNAc...) asparagine144N-linked (GlcNAc...) asparagine154N-linked (GlcNAc...) asparagine231N-linked (GlcNAc...) asparagine381N-linked (GlcNAc...) asparagine487N-linked (GlcNAc...) asparagine636322401363385365370473493656650662664673Reduces the shedding activity; when associated with A-56. Does not prevent pro-domain processing between the pro- and metalloprotease domain; when associated with A-56.A53Reduces the shedding activity; when associated with A-56. Does not prevent pro-domain processing between the pro- and metalloprotease domain; when associated with A-56.ADoes not affect shedding activity; when associated with A-205.A202Does not affect shedding activity; when associated with A-203.AAbolishes catalytic activity.AR296RRcatalytic2011-07-272true9207942a90c6f3f4ed7ab47dadee78ee662c7MGPRALSPLASLRLRWLLACGLLGPVLEAGRPDLEQTVHLSSYEIITPWRLTRERREALGPSSQQISYVIQAQGKQHIIHLERNTDLLPNDFVVYTYDKEGSLLSDHPNVQSHCHYRGYVEGVQNSAVAVSACFGLRGLLHLENASFGIEPLHNSSHFEHIFYPMDGIHQEPLRCGVSNRDTEKEGTQGDEEEHPSVTQLLRRRRAVLPQTRYVELFIVVDKERYDMMGRNQTAVREEMIRLANYLDSMYIMLNIRIVLVGLEIWTDRNPINIIGGAGDVLGNFVQWREKFLITRWRHDSAQLVLKKGFGGTAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDGRECFCGAKSCIMNSGASGSRNFSSCSAEDFEKLTLNKGGSCLLNIPKPDEAYSAPSCGNKLVDPGEECDCGTAKECEVDPCCEGSTCKLKSFAECAYGDCCKDCQFLPGGSMCRGKTSECDVPEYCNGSSQFCPPDVFIQNGYPCQNSKAYCYNGMCQYYDAQCQVIFGSKAKAAPRDCFIEVNSKGDRFGNCGFSGSEYKKCATGNALCGKLQCENVQDMPVFGIVPAIIQTPSRGTKCWGVDFQLGSDVPDPGMVNEGTKCDAGKICRNFQCVNASVLNYDCDIQGKCHGHGVCNSNKNCHCEDGWAPPHCDTKGYGGSVDSGPTYNAKSTALRDGLLVFFFLIVPLVAAAIFLFIKRDELRKTFRKKRSQMSDGRNQANVSRQPGDPSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPPGHGNRFPVPTYAAKQPAQFPSRPPPPQPKISSQGNLIPARPAPAPPLYSSLTtruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetrue