GENTAUR Molecular Products.

 OPTN_HUMAN              Reviewed;         577 AA.
 Q96CV9; B3KP00; D3DRS4; D3DRS8; Q5T672; Q5T673; Q5T674; Q5T675;
 Q7LDL9; Q8N562; Q9UET9; Q9UEV4; Q9Y218;
 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
 11-JAN-2011, sequence version 2.
 27-SEP-2017, entry version 138.
 RecName: Full=Optineurin;
 AltName: Full=E3-14.7K-interacting protein;
 AltName: Full=FIP-2;
 AltName: Full=Huntingtin yeast partner L;
 AltName: Full=Huntingtin-interacting protein 7;
          Short=HIP-7;
 AltName: Full=Huntingtin-interacting protein L;
 AltName: Full=NEMO-related protein;
 AltName: Full=Optic neuropathy-inducing protein;
 AltName: Full=Transcription factor IIIA-interacting protein;
          Short=TFIIIA-IntP;
 Name=OPTN; Synonyms=FIP2, GLC1E, HIP7, HYPL, NRP;
 Homo sapiens (Human).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
 Catarrhini; Hominidae; Homo.
 NCBI_TaxID=9606;
 [1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 3), VARIANTS
 SER-201; HIS-213; ARG-216; GLU-322 AND PRO-357, SUBCELLULAR LOCATION,
 TISSUE SPECIFICITY, INDUCTION, AND INTERACTION WITH ADENOVIRUS E3.
 TISSUE=Cervix carcinoma;
 PubMed=9488477; DOI=10.1128/MCB.18.3.1601;
 Li Y., Kang J., Horwitz M.S.;
 "Interaction of an adenovirus E3 14.7-kilodalton protein with a novel
 tumor necrosis factor alpha-inducible cellular protein containing
 leucine zipper domains.";
 Mol. Cell. Biol. 18:1601-1610(1998).
 [2]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
 LOCATION, TISSUE SPECIFICITY, VARIANTS GLC1E LYS-50 AND GLN-545, AND
 VARIANTS LYS-98; SER-201; HIS-213; ARG-216; GLU-322 AND PRO-357.
 TISSUE=Trabecular meshwork;
 PubMed=11834836; DOI=10.1126/science.1066901;
 Rezaie T., Child A., Hitchings R., Brice G., Miller L.,
 Coca-Prados M., Heon E., Krupin T., Ritch R., Kreutzer D., Crick R.P.,
 Sarfarazi M.;
 "Adult-onset primary open-angle glaucoma caused by mutations in
 optineurin.";
 Science 295:1077-1079(2002).
 [3]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-201; HIS-213;
 ARG-216; GLU-322 AND PRO-357.
 Li D., Roberts R.;
 "Human FIP-2: genomic structure and mutational analysis in ARVD
 patients.";
 Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
 [4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
 GLU-322.
 TISSUE=Brain;
 PubMed=14702039; DOI=10.1038/ng1285;
 Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
 Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
 Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
 Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
 Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
 Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
 Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
 Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
 Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
 Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
 Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
 Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
 Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
 Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
 Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
 Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
 Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
 Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
 Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
 Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
 Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
 Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
 Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
 Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
 Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
 Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
 Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
 Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
 "Complete sequencing and characterization of 21,243 full-length human
 cDNAs.";
 Nat. Genet. 36:40-45(2004).
 [5]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLU-322.
 PubMed=15164054; DOI=10.1038/nature02462;
 Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
 Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
 Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
 Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
 Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
 Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
 Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
 Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
 Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
 Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
 Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
 Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
 Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
 Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
 Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
 Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
 Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
 Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
 Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
 Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
 Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
 Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
 Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
 Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
 Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
 Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
 "The DNA sequence and comparative analysis of human chromosome 10.";
 Nature 429:375-381(2004).
 [6]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
 Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
 Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
 Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
 Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
 Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
 Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
 Venter J.C.;
 Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
 [7]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
 GLU-322.
 TISSUE=Cervix, and Skin;
 PubMed=15489334; DOI=10.1101/gr.2596504;
 The MGC Project Team;
 "The status, quality, and expansion of the NIH full-length cDNA
 project: the Mammalian Gene Collection (MGC).";
 Genome Res. 14:2121-2127(2004).
 [8]
 NUCLEOTIDE SEQUENCE [MRNA] OF 412-555, AND INTERACTION WITH HD.
 TISSUE=Testis;
 PubMed=9700202; DOI=10.1093/hmg/7.9.1463;
 Faber P.W., Barnes G.T., Srinidhi J., Chen J., Gusella J.F.,
 MacDonald M.E.;
 "Huntingtin interacts with a family of WW domain proteins.";
 Hum. Mol. Genet. 7:1463-1474(1998).
 [9]
 INTERACTION WITH HD AND RAB8.
 PubMed=11137014; DOI=10.1016/S0960-9822(00)00864-2;
 Hattula K., Peraenen J.;
 "FIP-2, a coiled-coil protein, links Huntingtin to Rab8 and modulates
 cellular morphogenesis.";
 Curr. Biol. 10:1603-1606(2000).
 [10]
 SUBCELLULAR LOCATION, INDUCTION, AND PHOSPHORYLATION.
 PubMed=10807909; DOI=10.1074/jbc.M001500200;
 Schwamborn K., Weil R., Courtois G., Whiteside S.T., Israeel A.;
 "Phorbol esters and cytokines regulate the expression of the NEMO-
 related protein, a molecule involved in a NF-kappa B-independent
 pathway.";
 J. Biol. Chem. 275:22780-22789(2000).
 [11]
 INTERACTION WITH GTF3A.
 PubMed=10756201; DOI=10.1093/nar/28.9.1986;
 Moreland R.J., Dresser M.E., Rodgers J.S., Roe B.A., Conaway J.W.,
 Conaway R.C., Hanas J.S.;
 "Identification of a transcription factor IIIA-interacting protein.";
 Nucleic Acids Res. 28:1986-1993(2000).
 [12]
 INDUCTION.
 PubMed=12379221; DOI=10.1016/S0006-291X(02)02395-1;
 Vittitow J., Borras T.;
 "Expression of optineurin, a glaucoma-linked gene, is influenced by
 elevated intraocular pressure.";
 Biochem. Biophys. Res. Commun. 298:67-74(2002).
 [13]
 INDUCTION.
 PubMed=12646749; DOI=10.1159/000069133;
 Kamphuis W., Schneemann A.;
 "Optineurin gene expression level in human trabecular meshwork does
 not change in response to pressure elevation.";
 Ophthalmic Res. 35:93-96(2003).
 [14]
 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MYO6 AND RAB8.
 PubMed=15837803; DOI=10.1083/jcb.200501162;
 Sahlender D.A., Roberts R.C., Arden S.D., Spudich G., Taylor M.J.,
 Luzio J.P., Kendrick-Jones J., Buss F.;
 "Optineurin links myosin VI to the Golgi complex and is involved in
 Golgi organization and exocytosis.";
 J. Cell Biol. 169:285-295(2005).
 [15]
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Cervix carcinoma;
 PubMed=16964243; DOI=10.1038/nbt1240;
 Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
 "A probability-based approach for high-throughput protein
 phosphorylation analysis and site localization.";
 Nat. Biotechnol. 24:1285-1292(2006).
 [16]
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Cervix carcinoma;
 PubMed=18669648; DOI=10.1073/pnas.0805139105;
 Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
 Elledge S.J., Gygi S.P.;
 "A quantitative atlas of mitotic phosphorylation.";
 Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
 [17]
 FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TFRC AND RAB8A,
 MUTAGENESIS OF GLU-50 AND ASP-474, AND CHARACTERIZATION OF VARIANT
 GLC1E LYS-50.
 PubMed=20085643; DOI=10.1186/1471-2121-11-4;
 Nagabhushana A., Chalasani M.L., Jain N., Radha V., Rangaraj N.,
 Balasubramanian D., Swarup G.;
 "Regulation of endocytic trafficking of transferrin receptor by
 optineurin and its impairment by a glaucoma-associated mutant.";
 BMC Cell Biol. 11:4-4(2010).
 [18]
 FUNCTION, SUBCELLULAR LOCATION, INDUCTION, INTERACTION WITH TBK1 AND
 TRAF3, UBIQUITIN-BINDING MOTIF, AND MUTAGENESIS OF ASP-474.
 PubMed=20174559; DOI=10.1371/journal.ppat.1000778;
 Mankouri J., Fragkoudis R., Richards K.H., Wetherill L.F., Harris M.,
 Kohl A., Elliott R.M., Macdonald A.;
 "Optineurin negatively regulates the induction of IFNbeta in response
 to RNA virus infection.";
 PLoS Pathog. 6:E1000778-E1000778(2010).
 [19]
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Cervix carcinoma;
 PubMed=20068231; DOI=10.1126/scisignal.2000475;
 Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
 Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
 Mann M.;
 "Quantitative phosphoproteomics reveals widespread full
 phosphorylation site occupancy during mitosis.";
 Sci. Signal. 3:RA3-RA3(2010).
 [20]
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 PubMed=21406692; DOI=10.1126/scisignal.2001570;
 Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
 Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
 Blagoev B.;
 "System-wide temporal characterization of the proteome and
 phosphoproteome of human embryonic stem cell differentiation.";
 Sci. Signal. 4:RS3-RS3(2011).
 [21]
 FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TBC1D17, INTERACTION
 WITH RAB8A, AND CHARACTERIZATION OF VARIANT GLC1E LYS-50.
 PubMed=22854040; DOI=10.1242/jcs.102327;
 Vaibhava V., Nagabhushana A., Chalasani M.L., Sudhakar C., Kumari A.,
 Swarup G.;
 "Optineurin mediates a negative regulation of Rab8 by the GTPase-
 activating protein TBC1D17.";
 J. Cell Sci. 125:5026-5039(2012).
 [22]
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 PubMed=22814378; DOI=10.1073/pnas.1210303109;
 Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
 Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
 Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
 Aldabe R.;
 "N-terminal acetylome analyses and functional insights of the N-
 terminal acetyltransferase NatB.";
 Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
 [23]
 LIR MOTIF.
 PubMed=23908376; DOI=10.1242/jcs.126128;
 Birgisdottir A.B., Lamark T., Johansen T.;
 "The LIR motif - crucial for selective autophagy.";
 J. Cell Sci. 126:3237-3247(2013).
 [24]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177 AND SER-526, AND
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Cervix carcinoma, and Erythroleukemia;
 PubMed=23186163; DOI=10.1021/pr300630k;
 Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
 Mohammed S.;
 "Toward a comprehensive characterization of a human cancer cell
 phosphoproteome.";
 J. Proteome Res. 12:260-271(2013).
 [25]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-198 AND
 SER-342, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
 ANALYSIS].
 TISSUE=Liver;
 PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
 Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
 Wang L., Ye M., Zou H.;
 "An enzyme assisted RP-RPLC approach for in-depth analysis of human
 liver phosphoproteome.";
 J. Proteomics 96:253-262(2014).
 [26]
 X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 170-181, STRUCTURE BY NMR OF
 169-185, INTERACTION WITH MAP1LC3B, AND MUTAGENESIS OF MUTAGENESIS OF
 PHE-178.
 PubMed=23805866; DOI=10.1042/BJ20121907;
 Rogov V.V., Suzuki H., Fiskin E., Wild P., Kniss A., Rozenknop A.,
 Kato R., Kawasaki M., McEwan D.G., Lohr F., Guntert P., Dikic I.,
 Wakatsuki S., Dotsch V.;
 "Structural basis for phosphorylation-triggered autophagic clearance
 of Salmonella.";
 Biochem. J. 454:459-466(2013).
 [27]
 VARIANT LYS-98.
 PubMed=14627677; DOI=10.1136/jmg.40.11.842;
 Melki R., Belmouden A., Akhayat O., Brezin A., Garchon H.-J.;
 "The M98K variant of the OPTINEURIN (OPTN) gene modifies initial
 intraocular pressure in patients with primary open angle glaucoma.";
 J. Med. Genet. 40:842-844(2003).
 [28]
 VARIANTS GLC1E ASP-103 AND ARG-486.
 PubMed=12939304; DOI=10.1167/iovs.02-0693;
 Leung Y.F., Fan B.J., Lam D.S.C., Lee W.S., Tam P.O.S., Chua J.K.H.,
 Tham C.C.Y., Lai J.S.M., Fan D.S.P., Pang C.P.;
 "Different optineurin mutation pattern in primary open-angle
 glaucoma.";
 Invest. Ophthalmol. Vis. Sci. 44:3880-3884(2003).
 [29]
 VARIANT GLC1E GLN-545.
 PubMed=14597044; DOI=10.1016/S0002-9394(03)00577-4;
 Alward W.L.M., Kwon Y.H., Kawase K., Craig J.E., Hayreh S.S.,
 Johnson A.T., Khanna C.L., Yamamoto T., Mackey D.A., Roos B.R.,
 Affatigato L.M., Sheffield V.C., Stone E.M.;
 "Evaluation of optineurin sequence variations in 1,048 patients with
 open-angle glaucoma.";
 Am. J. Ophthalmol. 136:904-910(2003).
 [30]
 CHARACTERIZATION OF VARIANT LYS-98, AND INTERACTION WITH RAB12.
 PubMed=23357852; DOI=10.4161/auto.23458;
 Sirohi K., Chalasani M.L., Sudhakar C., Kumari A., Radha V.,
 Swarup G.;
 "M98K-OPTN induces transferrin receptor degradation and RAB12-mediated
 autophagic death in retinal ganglion cells.";
 Autophagy 9:510-527(2013).
 [31]
 SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT GLC1E LYS-50, AND
 MUTAGENESIS OF GLU-50 AND ASP-474.
 PubMed=24752605; DOI=10.1371/journal.pone.0095758;
 Chalasani M.L., Kumari A., Radha V., Swarup G.;
 "E50K-OPTN-induced retinal cell death involves the Rab GTPase-
 activating protein, TBC1D17 mediated block in autophagy.";
 PLoS ONE 9:E95758-E95758(2014).
 [32]
 SELF-ASSOCIATION, SUBCELLULAR LOCATION, INTERACTION WITH TBK1, AND
 CHARACTERIZATION OF VARIANT GLC1E LYS-50.
 PubMed=23669351; DOI=10.1093/hmg/ddt210;
 Minegishi Y., Iejima D., Kobayashi H., Chi Z.L., Kawase K.,
 Yamamoto T., Seki T., Yuasa S., Fukuda K., Iwata T.;
 "Enhanced optineurin E50K-TBK1 interaction evokes protein insolubility
 and initiates familial primary open-angle glaucoma.";
 Hum. Mol. Genet. 22:3559-3567(2013).
 [33]
 VARIANT LYS-98.
 PubMed=15498064; DOI=10.1111/j.1442-9071.2004.00886.x;
 Baird P.N., Richardson A.J., Craig J.E., Mackey D.A., Rochtchina E.,
 Mitchell P.;
 "Analysis of optineurin (OPTN) gene mutations in subjects with and
 without glaucoma: the blue mountains eye study.";
 Clin. Exp. Ophthalmol. 32:518-522(2004).
 [34]
 VARIANT GLC1E ARG-486.
 PubMed=15326130; DOI=10.1167/iovs.04-0107;
 Willoughby C.E., Chan L.L.Y., Herd S., Billingsley G., Noordeh N.,
 Levin A.V., Buys Y., Trope G., Sarfarazi M., Heon E.;
 "Defining the pathogenicity of optineurin in juvenile open-angle
 glaucoma.";
 Invest. Ophthalmol. Vis. Sci. 45:3122-3130(2004).
 [35]
 VARIANTS GLC1E ASP-26 AND GLN-545, AND VARIANT LYS-98.
 PubMed=15557444; DOI=10.1167/iovs.03-1403;
 Funayama T., Ishikawa K., Ohtake Y., Tanino T., Kurosaka D.,
 Kimura I., Suzuki K., Ideta H., Nakamoto K., Yasuda N., Fujimaki T.,
 Murakami A., Asaoka R., Hotta Y., Tanihara H., Kanamoto T.,
 Mishima H., Fukuchi T., Abe H., Iwata T., Shimada N., Kudoh J.,
 Shimizu N., Mashima Y.;
 "Variants in optineurin gene and their association with tumor necrosis
 factor-alpha polymorphisms in Japanese patients with glaucoma.";
 Invest. Ophthalmol. Vis. Sci. 45:4359-4367(2004).
 [36]
 VARIANT GLC1E ASP-26.
 PubMed=15226658; DOI=10.1097/00061198-200408000-00007;
 Fuse N., Takahashi K., Akiyama H., Nakazawa T., Seimiya M.,
 Kuwahara S., Tamai M.;
 "Molecular genetic analysis of optineurin gene for primary open-angle
 and normal tension glaucoma in the Japanese population.";
 J. Glaucoma 13:299-303(2004).
 [37]
 VARIANT NPG ASP-26.
 PubMed=15370540; DOI=10.1080/13816810490514298;
 Umeda T., Matsuo T., Nagayama M., Tamura N., Tanabe Y., Ohtsuki H.;
 "Clinical relevance of optineurin sequence alterations in Japanese
 glaucoma patients.";
 Ophthalmic Genet. 25:91-99(2004).
 [38]
 CHARACTERIZATION OF VARIANT GLC1E LYS-50.
 PubMed=17389490; DOI=10.1167/iovs.06-0834;
 Chalasani M.L., Radha V., Gupta V., Agarwal N., Balasubramanian D.,
 Swarup G.;
 "A glaucoma-associated mutant of optineurin selectively induces death
 of retinal ganglion cells which is inhibited by antioxidants.";
 Invest. Ophthalmol. Vis. Sci. 48:1607-1614(2007).
 [39]
 VARIANT ALS12 GLY-478, AND SUBCELLULAR LOCATION.
 PubMed=20428114; DOI=10.1038/nature08971;
 Maruyama H., Morino H., Ito H., Izumi Y., Kato H., Watanabe Y.,
 Kinoshita Y., Kamada M., Nodera H., Suzuki H., Komure O., Matsuura S.,
 Kobatake K., Morimoto N., Abe K., Suzuki N., Aoki M., Kawata A.,
 Hirai T., Kato T., Ogasawara K., Hirano A., Takumi T., Kusaka H.,
 Hagiwara K., Kaji R., Kawakami H.;
 "Mutations of optineurin in amyotrophic lateral sclerosis.";
 Nature 465:223-226(2010).
 [40]
 FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MAP1LC3A; MAP1LC3B;
 GABARAP; GABARAPL1 AND GABARAPL2, PHOSPHORYLATION AT SER-177 BY TBK1,
 UBIQUITIN-BINDING, AND MUTAGENESIS OF PHE-178 AND 474-ASP-PHE-475.
 PubMed=21617041; DOI=10.1126/science.1205405;
 Wild P., Farhan H., McEwan D.G., Wagner S., Rogov V.V., Brady N.R.,
 Richter B., Korac J., Waidmann O., Choudhary C., Dotsch V., Bumann D.,
 Dikic I.;
 "Phosphorylation of the autophagy receptor optineurin restricts
 Salmonella growth.";
 Science 333:228-233(2011).
 [41]
 VARIANT ALS12 PHE-295, CHARACTERIZATION VARIANT ALS12 PHE-295,
 FUNCTION, AND SUBCELLULAR LOCATION.
 PubMed=27534431; DOI=10.1080/21678421.2016.1218517;
 Fifita J.A., Williams K.L., Sundaramoorthy V., Mccann E.P.,
 Nicholson G.A., Atkin J.D., Blair I.P.;
 "A novel amyotrophic lateral sclerosis mutation in OPTN induces ER
 stress and Golgi fragmentation in vitro.";
 Amyotroph. Lateral Scler. Frontotemporal Degener. 18:126-133(2017).
 -!- FUNCTION: Plays an important role in the maintenance of the Golgi
     complex, in membrane trafficking, in exocytosis, through its
     interaction with myosin VI and Rab8 (PubMed:27534431). Links
     myosin VI to the Golgi complex and plays an important role in
     Golgi ribbon formation (PubMed:27534431). Negatively regulates the
     induction of IFNB in response to RNA virus infection. Plays a
     neuroprotective role in the eye and optic nerve. Probably part of
     the TNF-alpha signaling pathway that can shift the equilibrium
     toward induction of cell death. May act by regulating membrane
     trafficking and cellular morphogenesis via a complex that contains
     Rab8 and hungtingtin (HD). Mediates the interaction of Rab8 with
     the probable GTPase-activating protein TBC1D17 during Rab8-
     mediated endocytic trafficking, such as of transferrin receptor
     (TFRC/TfR); regulates Rab8 recruitnment to tubules emanating from
     the endocytic recycling compartment. Autophagy receptor that
     interacts directly with both the cargo to become degraded and an
     autophagy modifier of the MAP1 LC3 family; targets ubiquitin-
     coated bacteria (xenophagy), such as cytoplasmic Salmonella
     enterica, and appears to function in the same pathway as SQSTM1
     and CALCOCO2/NDP52. May constitute a cellular target for
     adenovirus E3 14.7, an inhibitor of TNF-alpha functions, thereby
     affecting cell death. {ECO:0000269|PubMed:11834836,
     ECO:0000269|PubMed:15837803, ECO:0000269|PubMed:20085643,
     ECO:0000269|PubMed:20174559, ECO:0000269|PubMed:21617041,
     ECO:0000269|PubMed:22854040, ECO:0000269|PubMed:27534431}.
 -!- SUBUNIT: Interacts with HD, Rab8 (RAB8A and/or RAB8B) (active GTP-
     bound form), GTF3A, TRAF3, TBK1, MYO6 and TFRC. Binds to linear
     ubiquitin chains. Interacts with LC3 family members MAP1LC3A,
     MAP1LC3B, GABARAP, GABARAPL1 and GABARAPL2; OPTN phosphorylation
     increases the association (at least with MAP1LC3B). Self-
     associates. Interacts with RAB12; the interaction may be indirect.
     Interacts with E3 14.7 kDa protein of group C human adenovirus.
     {ECO:0000269|PubMed:10756201, ECO:0000269|PubMed:11137014,
     ECO:0000269|PubMed:15837803, ECO:0000269|PubMed:20085643,
     ECO:0000269|PubMed:20174559, ECO:0000269|PubMed:21617041,
     ECO:0000269|PubMed:22854040, ECO:0000269|PubMed:23357852,
     ECO:0000269|PubMed:23669351, ECO:0000269|PubMed:23805866,
     ECO:0000269|PubMed:9488477, ECO:0000269|PubMed:9700202}.
 -!- INTERACTION:
     Self; NbExp=12; IntAct=EBI-748974, EBI-748974;
     Q99IB8:- (xeno); NbExp=3; IntAct=EBI-748974, EBI-6858501;
     Q12904-2:AIMP1; NbExp=4; IntAct=EBI-748974, EBI-12412735;
     Q13023:AKAP6; NbExp=2; IntAct=EBI-748974, EBI-1056102;
     Q9UJX2:CDC23; NbExp=8; IntAct=EBI-748974, EBI-396137;
     Q15038:DAZAP2; NbExp=5; IntAct=EBI-748974, EBI-724310;
     Q03001:DST; NbExp=2; IntAct=EBI-748974, EBI-310758;
     O75923:DYSF; NbExp=3; IntAct=EBI-748974, EBI-2799016;
     Q8IYU2:HACE1; NbExp=15; IntAct=EBI-748974, EBI-308277;
     P42858:HTT; NbExp=9; IntAct=EBI-748974, EBI-466029;
     P40325:HUA1 (xeno); NbExp=3; IntAct=EBI-748974, EBI-23614;
     Q99732:LITAF; NbExp=3; IntAct=EBI-9091423, EBI-725647;
     Q00013:MPP1; NbExp=2; IntAct=EBI-748974, EBI-711788;
     P54845-1:NRL; NbExp=6; IntAct=EBI-748974, EBI-9819090;
     P40302:PRE5 (xeno); NbExp=3; IntAct=EBI-9091423, EBI-13955;
     O75360:PROP1; NbExp=4; IntAct=EBI-748974, EBI-9027467;
     P61026:RAB10; NbExp=3; IntAct=EBI-748974, EBI-726075;
     P61006:RAB8A; NbExp=4; IntAct=EBI-748974, EBI-722293;
     P61007:RAB8A (xeno); NbExp=2; IntAct=EBI-748974, EBI-7473289;
     Q9NTZ6:RBM12; NbExp=5; IntAct=EBI-748974, EBI-310707;
     P40454:RRD1 (xeno); NbExp=3; IntAct=EBI-9091423, EBI-25278;
     Q14BN4:SLMAP; NbExp=2; IntAct=EBI-748974, EBI-1043216;
     Q9UNH7:SNX6; NbExp=2; IntAct=EBI-748974, EBI-949294;
     Q13501:SQSTM1; NbExp=7; IntAct=EBI-748974, EBI-307104;
     Q8TC07:TBC1D15; NbExp=5; IntAct=EBI-748974, EBI-1048247;
     Q9HA65:TBC1D17; NbExp=7; IntAct=EBI-748974, EBI-714625;
     Q9UHD2:TBK1; NbExp=12; IntAct=EBI-748974, EBI-356402;
     Q15025:TNIP1; NbExp=12; IntAct=EBI-748974, EBI-357849;
     Q8WZ42:TTN; NbExp=2; IntAct=EBI-748974, EBI-681210;
     P04275:VWF; NbExp=2; IntAct=EBI-748974, EBI-981819;
     Q9Y3C0:WASHC3; NbExp=12; IntAct=EBI-748974, EBI-712969;
     P01123:YPT1 (xeno); NbExp=3; IntAct=EBI-9091423, EBI-29496;
     Q8IUH5:ZDHHC17; NbExp=2; IntAct=EBI-9091423, EBI-524753;
     Q86UD4:ZNF329; NbExp=3; IntAct=EBI-748974, EBI-7233259;
     Q8TD17:ZNF398; NbExp=3; IntAct=EBI-748974, EBI-8643207;
     Q9BUY5:ZNF426; NbExp=3; IntAct=EBI-748974, EBI-743265;
     Q9BS34:ZNF670; NbExp=5; IntAct=EBI-748974, EBI-745276;
 -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Golgi
     apparatus {ECO:0000269|PubMed:27534431}. Golgi apparatus, trans-
     Golgi network. Cytoplasmic vesicle, autophagosome. Cytoplasmic
     vesicle. Recycling endosome. Note=Found in the perinuclear region
     and associates with the Golgi apparatus (PubMed:27534431).
     Colocalizes with MYO6 and RAB8 at the Golgi complex and in
     vesicular structures close to the plasma membrane. Localizes to
     LC3-positive cytoplasmic vesicles upon induction of autophagy.
     {ECO:0000269|PubMed:27534431}.
 -!- ALTERNATIVE PRODUCTS:
     Event=Alternative splicing; Named isoforms=3;
     Name=1;
       IsoId=Q96CV9-1; Sequence=Displayed;
     Name=2;
       IsoId=Q96CV9-2; Sequence=VSP_013262;
       Note=No experimental confirmation available.;
     Name=3;
       IsoId=Q96CV9-3; Sequence=VSP_013261;
 -!- TISSUE SPECIFICITY: Present in aqueous humor of the eye (at
     protein level). Highly expressed in trabecular meshwork. Expressed
     nonpigmented ciliary epithelium, retina, brain, adrenal cortex,
     fetus, lymphocyte, fibroblast, skeletal muscle, heart, liver,
     brain and placenta. {ECO:0000269|PubMed:11834836,
     ECO:0000269|PubMed:9488477}.
 -!- INDUCTION: Upon TNF and interferon treatments. Up-regulated in
     direct response to viral infection. {ECO:0000269|PubMed:10807909,
     ECO:0000269|PubMed:12379221, ECO:0000269|PubMed:12646749,
     ECO:0000269|PubMed:20174559, ECO:0000269|PubMed:9488477}.
 -!- DOMAIN: Ubiquitin-binding motif (UBAN) is essential for its
     inhibitory function, subcellular localization and interaction with
     TBK1.
 -!- DOMAIN: The LIR (LC3-interacting region) motif mediates the
     interaction with ATG8 family proteins.
     {ECO:0000269|PubMed:23908376}.
 -!- PTM: Phosphorylated by TBK1, leading to restrict bacterial
     proliferation in case of infection. Phosphorylation is induced by
     phorbol esters and decreases its half-time.
     {ECO:0000269|PubMed:10807909, ECO:0000269|PubMed:21617041}.
 -!- DISEASE: Glaucoma 1, open angle, E (GLC1E) [MIM:137760]: A form of
     primary open angle glaucoma (POAG). POAG is characterized by a
     specific pattern of optic nerve and visual field defects. The
     angle of the anterior chamber of the eye is open, and usually the
     intraocular pressure is increased. However, glaucoma can occur at
     any intraocular pressure. The disease is generally asymptomatic
     until the late stages, by which time significant and irreversible
     optic nerve damage has already taken place.
     {ECO:0000269|PubMed:11834836, ECO:0000269|PubMed:12939304,
     ECO:0000269|PubMed:14597044, ECO:0000269|PubMed:15226658,
     ECO:0000269|PubMed:15326130, ECO:0000269|PubMed:15557444,
     ECO:0000269|PubMed:17389490, ECO:0000269|PubMed:20085643,
     ECO:0000269|PubMed:22854040, ECO:0000269|PubMed:23669351,
     ECO:0000269|PubMed:24752605}. Note=The disease is caused by
     mutations affecting the gene represented in this entry.
 -!- DISEASE: Glaucoma, normal pressure (NPG) [MIM:606657]: A primary
     glaucoma characterized by intraocular pression consistently within
     the statistically normal population range.
     {ECO:0000269|PubMed:15370540}. Note=Disease susceptibility is
     associated with variations affecting the gene represented in this
     entry.
 -!- DISEASE: Amyotrophic lateral sclerosis 12 (ALS12) [MIM:613435]: A
     neurodegenerative disorder affecting upper motor neurons in the
     brain and lower motor neurons in the brain stem and spinal cord,
     resulting in fatal paralysis. Sensory abnormalities are absent.
     The pathologic hallmarks of the disease include pallor of the
     corticospinal tract due to loss of motor neurons, presence of
     ubiquitin-positive inclusions within surviving motor neurons, and
     deposition of pathologic aggregates. The etiology of amyotrophic
     lateral sclerosis is likely to be multifactorial, involving both
     genetic and environmental factors. The disease is inherited in 5-
     10% of the cases. {ECO:0000269|PubMed:20428114,
     ECO:0000269|PubMed:27534431}. Note=The disease is caused by
     mutations affecting the gene represented in this entry.
 -!- CAUTION: According to some authors (PubMed:12379221) its
     expression is regulated by intraocular pressure, suggesting a
     protective role in case of high pressure, while according to other
     authors (PubMed:12646749), it is not up-regulated in response to
     pressure elevation. {ECO:0000305|PubMed:12379221,
     ECO:0000305|PubMed:12646749}.
 -!- CAUTION: Interaction of variant GLC1E LYS-50 with Rab8 is reported
     conflictingly. Coimmunoprecipitation experiments with
     overexpressed proteins suggested an increased interaction
     (PubMed:20085643) while yeast-two-hybrid (PubMed:22854040) and
     protein complentation assays with an equivalent mouse Optn
     construct (AC Q8K3K8) failed to show an interaction.
     {ECO:0000305|PubMed:20085643, ECO:0000305|PubMed:22854040}.
 -!- SEQUENCE CAUTION:
     Sequence=CAI16552.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
 -----------------------------------------------------------------------
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 Distributed under the Creative Commons Attribution-NoDerivs License
 -----------------------------------------------------------------------
 EMBL; AF061034; AAC16046.1; -; mRNA.
 EMBL; AF061034; AAC16047.1; -; mRNA.
 EMBL; AF420371; AAL76327.1; -; mRNA.
 EMBL; AF420372; AAL76328.1; -; mRNA.
 EMBL; AF420373; AAL76329.1; -; mRNA.
 EMBL; AF283527; AAG00497.1; -; Genomic_DNA.
 EMBL; AF283520; AAG00497.1; JOINED; Genomic_DNA.
 EMBL; AF283521; AAG00497.1; JOINED; Genomic_DNA.
 EMBL; AF283522; AAG00497.1; JOINED; Genomic_DNA.
 EMBL; AF283523; AAG00497.1; JOINED; Genomic_DNA.
 EMBL; AF283524; AAG00497.1; JOINED; Genomic_DNA.
 EMBL; AF283525; AAG00497.1; JOINED; Genomic_DNA.
 EMBL; AF283526; AAG00497.1; JOINED; Genomic_DNA.
 EMBL; AK055403; BAG51512.1; -; mRNA.
 EMBL; AL355355; CAI16549.1; -; Genomic_DNA.
 EMBL; AL355355; CAI16550.1; -; Genomic_DNA.
 EMBL; AL355355; CAI16551.1; -; Genomic_DNA.
 EMBL; AL355355; CAI16552.1; ALT_SEQ; Genomic_DNA.
 EMBL; CH471072; EAW86301.1; -; Genomic_DNA.
 EMBL; CH471072; EAW86302.1; -; Genomic_DNA.
 EMBL; CH471072; EAW86303.1; -; Genomic_DNA.
 EMBL; CH471072; EAW86304.1; -; Genomic_DNA.
 EMBL; CH471072; EAW86306.1; -; Genomic_DNA.
 EMBL; CH471072; EAW86308.1; -; Genomic_DNA.
 EMBL; CH471072; EAW86309.1; -; Genomic_DNA.
 EMBL; BC013876; AAH13876.1; -; mRNA.
 EMBL; BC032762; AAH32762.1; -; mRNA.
 EMBL; AF049614; AAC26850.1; -; mRNA.
 CCDS; CCDS7094.1; -. [Q96CV9-1]
 RefSeq; NP_001008212.1; NM_001008211.1.
 RefSeq; NP_001008213.1; NM_001008212.1.
 RefSeq; NP_001008214.1; NM_001008213.1.
 RefSeq; NP_068815.2; NM_021980.4.
 UniGene; Hs.332706; -.
 PDB; 2LO4; NMR; -; A=550-577.
 PDB; 2LUE; NMR; -; B=169-185.
 PDB; 3VTV; X-ray; 1.70 A; A=170-181.
 PDB; 3VTW; X-ray; 2.52 A; A/B/C=170-181.
 PDB; 5AAZ; NMR; -; A=548-577.
 PDB; 5B83; X-ray; 2.69 A; B/C/E/F=416-510.
 PDB; 5EOA; X-ray; 2.50 A; A/B=26-103.
 PDB; 5EOF; X-ray; 2.05 A; A/B=26-103.
 PDBsum; 2LO4; -.
 PDBsum; 2LUE; -.
 PDBsum; 3VTV; -.
 PDBsum; 3VTW; -.
 PDBsum; 5AAZ; -.
 PDBsum; 5B83; -.
 PDBsum; 5EOA; -.
 PDBsum; 5EOF; -.
 ProteinModelPortal; Q96CV9; -.
 SMR; Q96CV9; -.
 BioGrid; 115436; 78.
 CORUM; Q96CV9; -.
 DIP; DIP-42001N; -.
 IntAct; Q96CV9; 95.
 MINT; MINT-155870; -.
 STRING; 9606.ENSP00000263036; -.
 iPTMnet; Q96CV9; -.
 PhosphoSitePlus; Q96CV9; -.
 BioMuta; OPTN; -.
 DMDM; 317373403; -.
 EPD; Q96CV9; -.
 MaxQB; Q96CV9; -.
 PaxDb; Q96CV9; -.
 PeptideAtlas; Q96CV9; -.
 PRIDE; Q96CV9; -.
 DNASU; 10133; -.
 Ensembl; ENST00000263036; ENSP00000263036; ENSG00000123240.
 Ensembl; ENST00000378747; ENSP00000368021; ENSG00000123240.
 Ensembl; ENST00000378748; ENSP00000368022; ENSG00000123240.
 Ensembl; ENST00000378752; ENSP00000368027; ENSG00000123240.
 Ensembl; ENST00000378757; ENSP00000368032; ENSG00000123240.
 Ensembl; ENST00000378764; ENSP00000368040; ENSG00000123240.
 GeneID; 10133; -.
 KEGG; hsa:10133; -.
 UCSC; uc001ilv.2; human. [Q96CV9-1]
 CTD; 10133; -.
 DisGeNET; 10133; -.
 EuPathDB; HostDB:ENSG00000123240.16; -.
 GeneCards; OPTN; -.
 GeneReviews; OPTN; -.
 HGNC; HGNC:17142; OPTN.
 HPA; CAB019303; -.
 HPA; HPA003279; -.
 HPA; HPA003360; -.
 MalaCards; OPTN; -.
 MIM; 137760; phenotype.
 MIM; 602432; gene.
 MIM; 606657; phenotype.
 MIM; 613435; phenotype.
 neXtProt; NX_Q96CV9; -.
 Orphanet; 803; Amyotrophic lateral sclerosis.
 Orphanet; 353225; Primary adult open-angle glaucoma.
 PharmGKB; PA31948; -.
 eggNOG; ENOG410IE97; Eukaryota.
 eggNOG; ENOG410Z0DF; LUCA.
 HOVERGEN; HBG106481; -.
 InParanoid; Q96CV9; -.
 KO; K19946; -.
 OrthoDB; EOG091G0576; -.
 PhylomeDB; Q96CV9; -.
 TreeFam; TF326608; -.
 Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
 Reactome; R-HSA-8854214; TBC/RABGAPs.
 SIGNOR; Q96CV9; -.
 ChiTaRS; OPTN; human.
 GeneWiki; Optineurin; -.
 GenomeRNAi; 10133; -.
 PRO; PR:Q96CV9; -.
 Proteomes; UP000005640; Chromosome 10.
 Bgee; ENSG00000123240; -.
 ExpressionAtlas; Q96CV9; baseline and differential.
 Genevisible; Q96CV9; HS.
 GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
 GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
 GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
 GO; GO:0005829; C:cytosol; IDA:HPA.
 GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
 GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
 GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO; GO:0005634; C:nucleus; IBA:GO_Central.
 GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
 GO; GO:0055038; C:recycling endosome membrane; TAS:Reactome.
 GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
 GO; GO:0042802; F:identical protein binding; IPI:IntAct.
 GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IBA:GO_Central.
 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
 GO; GO:0030674; F:protein binding, bridging; IPI:ParkinsonsUK-UCL.
 GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
 GO; GO:0017137; F:Rab GTPase binding; IPI:UniProtKB.
 GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
 GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
 GO; GO:0008219; P:cell death; TAS:ProtInc.
 GO; GO:0034620; P:cellular response to unfolded protein; IMP:UniProtKB.
 GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
 GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
 GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
 GO; GO:0090161; P:Golgi ribbon formation; IDA:UniProtKB.
 GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:UniProtKB.
 GO; GO:0061024; P:membrane organization; TAS:Reactome.
 GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
 GO; GO:0001920; P:negative regulation of receptor recycling; IMP:UniProtKB.
 GO; GO:0061734; P:parkin-mediated stimulation of mitophagy in response to mitochondrial depolarization; IMP:ParkinsonsUK-UCL.
 GO; GO:0010508; P:positive regulation of autophagy; IDA:GO_Central.
 GO; GO:1904417; P:positive regulation of xenophagy; IMP:ParkinsonsUK-UCL.
 GO; GO:0000042; P:protein targeting to Golgi; IMP:UniProtKB.
 GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
 GO; GO:0007165; P:signal transduction; TAS:ProtInc.
 InterPro; IPR032419; CC2-LZ_dom.
 InterPro; IPR021063; NEMO_N.
 InterPro; IPR034735; NEMO_ZF.
 InterPro; IPR032939; Optineurin.
 PANTHER; PTHR31553:SF6; PTHR31553:SF6; 1.
 Pfam; PF16516; CC2-LZ; 1.
 Pfam; PF11577; NEMO; 1.
 PROSITE; PS51801; ZF_CCHC_NOA; 1.
 1: Evidence at protein level;
 3D-structure; Alternative splicing; Amyotrophic lateral sclerosis;
 Autophagy; Coiled coil; Complete proteome; Cytoplasm;
 Cytoplasmic vesicle; Disease mutation; Endosome; Glaucoma;
 Golgi apparatus; Metal-binding; Neurodegeneration; Phosphoprotein;
 Polymorphism; Reference proteome; Zinc; Zinc-finger.
 CHAIN         1    577       Optineurin.
                              /FTId=PRO_0000058066.
 ZN_FING     547    577       CCHC NOA-type. {ECO:0000255|PROSITE-
                              ProRule:PRU01142}.
 REGION       58    209       Interaction with Rab8.
 REGION      411    577       Interaction with HD.
 REGION      412    520       Interaction with MYO6.
                              {ECO:0000269|PubMed:15837803}.
 COILED       38    170       {ECO:0000255}.
 COILED      239    508       {ECO:0000255}.
 MOTIF       176    181       LIR.
 MOTIF       474    479       UBAN.
 MOD_RES     177    177       Phosphoserine; by TBK1.
                              {ECO:0000244|PubMed:23186163,
                              ECO:0000244|PubMed:24275569,
                              ECO:0000269|PubMed:21617041}.
 MOD_RES     198    198       Phosphoserine.
                              {ECO:0000244|PubMed:24275569}.
 MOD_RES     342    342       Phosphoserine.
                              {ECO:0000244|PubMed:24275569}.
 MOD_RES     526    526       Phosphoserine.
                              {ECO:0000244|PubMed:23186163}.
 VAR_SEQ       1     57       Missing (in isoform 3).
                              {ECO:0000303|PubMed:9488477}.
                              /FTId=VSP_013261.
 VAR_SEQ     210    215       Missing (in isoform 2).
                              {ECO:0000303|PubMed:15489334}.
                              /FTId=VSP_013262.
 VARIANT      26     26       H -> D (in GLC1E).
                              {ECO:0000269|PubMed:15226658,
                              ECO:0000269|PubMed:15370540,
                              ECO:0000269|PubMed:15557444}.
                              /FTId=VAR_021537.
 VARIANT      50     50       E -> K (in GLC1E; selectively promotes
                              cell death of retinal ganglion cells
                              probably by inducing TBC1D17-mediated
                              inhibition of autophagy; altered
                              interaction with RAB8A; no effect on
                              interaction with TBC1D17; increases
                              interaction with TFRC and impairs its
                              endocytic recycling; increases
                              interactions with TBK1; decreases self-
                              association; disturbs transition from the
                              ER to Golgi; dbSNP:rs28939688).
                              {ECO:0000269|PubMed:11834836,
                              ECO:0000269|PubMed:17389490,
                              ECO:0000269|PubMed:20085643,
                              ECO:0000269|PubMed:22854040,
                              ECO:0000269|PubMed:23669351,
                              ECO:0000269|PubMed:24752605}.
                              /FTId=VAR_021538.
 VARIANT      98     98       M -> K (polymorphism; may modify
                              intraocular pressure and increase risk of
                              GLC1E and NPG; induces TFRC degradation
                              leading to autophagic death in retinal
                              ganglion cells; dbSNP:rs11258194).
                              {ECO:0000269|PubMed:11834836,
                              ECO:0000269|PubMed:14627677,
                              ECO:0000269|PubMed:15498064,
                              ECO:0000269|PubMed:15557444,
                              ECO:0000269|PubMed:23357852}.
                              /FTId=VAR_021539.
 VARIANT     103    103       E -> D (in GLC1E).
                              {ECO:0000269|PubMed:12939304}.
                              /FTId=VAR_021540.
 VARIANT     201    201       P -> S. {ECO:0000269|PubMed:11834836,
                              ECO:0000269|PubMed:9488477,
                              ECO:0000269|Ref.3}.
                              /FTId=VAR_021541.
 VARIANT     213    213       K -> H (requires 2 nucleotide
                              substitutions).
                              {ECO:0000269|PubMed:11834836,
                              ECO:0000269|PubMed:9488477,
                              ECO:0000269|Ref.3}.
                              /FTId=VAR_021542.
 VARIANT     216    216       S -> R. {ECO:0000269|PubMed:11834836,
                              ECO:0000269|PubMed:9488477,
                              ECO:0000269|Ref.3}.
                              /FTId=VAR_021543.
 VARIANT     295    295       V -> F (in ALS12; no effect on Golgi
                              subcellular location; no effect on
                              protein expression level; increased Golgi
                              fragmentation; decreased Golgi ribbon
                              formation; increased susceptibility to
                              endoplasmic reticulum (ER) stress).
                              {ECO:0000269|PubMed:27534431}.
                              /FTId=VAR_078108.
 VARIANT     308    308       S -> P (in dbSNP:rs7068431).
                              /FTId=VAR_030769.
 VARIANT     322    322       K -> E (in dbSNP:rs523747).
                              {ECO:0000269|PubMed:11834836,
                              ECO:0000269|PubMed:14702039,
                              ECO:0000269|PubMed:15164054,
                              ECO:0000269|PubMed:15489334,
                              ECO:0000269|PubMed:9488477,
                              ECO:0000269|Ref.3}.
                              /FTId=VAR_021544.
 VARIANT     357    357       T -> P. {ECO:0000269|PubMed:11834836,
                              ECO:0000269|PubMed:9488477,
                              ECO:0000269|Ref.3}.
                              /FTId=VAR_021545.
 VARIANT     478    478       E -> G (in ALS12).
                              {ECO:0000269|PubMed:20428114}.
                              /FTId=VAR_063597.
 VARIANT     486    486       H -> R (in GLC1E; juvenile onset).
                              {ECO:0000269|PubMed:12939304,
                              ECO:0000269|PubMed:15326130}.
                              /FTId=VAR_021546.
 VARIANT     545    545       R -> Q (in GLC1E; unknown pathological
                              significance; dbSNP:rs28939689).
                              {ECO:0000269|PubMed:11834836,
                              ECO:0000269|PubMed:14597044,
                              ECO:0000269|PubMed:15557444}.
                              /FTId=VAR_021547.
 MUTAGEN      50     50       E->K: Reduces cell death, decreased
                              interaction with TFRC; when associated
                              with N-474. {ECO:0000269|PubMed:20085643,
                              ECO:0000269|PubMed:24752605}.
 MUTAGEN     178    178       F->A: Abolishes interaction with MAP1LC3A
                              and GABARAPL1, no effect on binding to
                              linear ubiquitin.
                              {ECO:0000269|PubMed:21617041,
                              ECO:0000269|PubMed:23805866}.
 MUTAGEN     178    178       F->W: Increases interaction with
                              MAP1LC3B. {ECO:0000269|PubMed:21617041,
                              ECO:0000269|PubMed:23805866}.
 MUTAGEN     474    475       DF->NA: Abolishes colocalization with
                              cytosolic Salmonella.
                              {ECO:0000269|PubMed:21617041}.
 MUTAGEN     474    474       D->N: Reduces cell death, decreased
                              interaction with TFRC; when associated
                              with K-50. {ECO:0000269|PubMed:20085643,
                              ECO:0000269|PubMed:20174559,
                              ECO:0000269|PubMed:24752605}.
 MUTAGEN     474    474       D->N: Significant reduction in ubiquitin
                              binding and interaction with TBK1.
                              Inhibits localization to recycling
                              endosomes and disrupts interaction with
                              TFRC. Loss of ability to inhibit the
                              activation of the IFNB promoter in
                              response to TLR3 or RIG-I signaling.
                              {ECO:0000269|PubMed:20085643,
                              ECO:0000269|PubMed:20174559,
                              ECO:0000269|PubMed:24752605}.
 CONFLICT    436    436       A -> V (in Ref. 8; AAC26850).
                              {ECO:0000305}.
 TURN         30     33       {ECO:0000244|PDB:5EOF}.
 HELIX        37     98       {ECO:0000244|PDB:5EOF}.
 STRAND      178    180       {ECO:0000244|PDB:2LUE}.
 HELIX       447    497       {ECO:0000244|PDB:5B83}.
 TURN        556    560       {ECO:0000244|PDB:2LO4}.
 STRAND      561    564       {ECO:0000244|PDB:5AAZ}.
 HELIX       566    574       {ECO:0000244|PDB:2LO4}.
 SEQUENCE   577 AA;  65921 MW;  DB0F841E3315AAE1 CRC64;
 MSHQPLSCLT EKEDSPSEST GNGPPHLAHP NLDTFTPEEL LQQMKELLTE NHQLKEAMKL
 NNQAMKGRFE ELSAWTEKQK EERQFFEIQS KEAKERLMAL SHENEKLKEE LGKLKGKSER
 SSEDPTDDSR LPRAEAEQEK DQLRTQVVRL QAEKADLLGI VSELQLKLNS SGSSEDSFVE
 IRMAEGEAEG SVKEIKHSPG PTRTVSTGTA LSKYRSRSAD GAKNYFEHEE LTVSQLLLCL
 REGNQKVERL EVALKEAKER VSDFEKKTSN RSEIETQTEG STEKENDEEK GPETVGSEVE
 ALNLQVTSLF KELQEAHTKL SKAELMKKRL QEKCQALERK NSAIPSELNE KQELVYTNKK
 LELQVESMLS EIKMEQAKTE DEKSKLTVLQ MTHNKLLQEH NNALKTIEEL TRKESEKVDR
 AVLKELSEKL ELAEKALASK QLQMDEMKQT IAKQEEDLET MTILRAQMEV YCSDFHAERA
 AREKIHEEKE QLALQLAVLL KENDAFEDGG RQSLMEMQSR HGARTSDSDQ QAYLVQRGAE
 DRDWRQQRNI PIHSCPKCGE VLPDIDTLQI HVMDCII

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