GENTAUR Molecular Products.
Monoclonal Antibody, ELISA Kit, Polyclonal Antibody, Recombinant/Purified Protein.Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery
Optineurin (E3-14.7K-interacting protein) (FIP-2) (Huntingtin yeast partner L) (Huntingtin-interacting protein 7) (HIP-7) (Huntingtin-interacting protein L) (NEMO-related protein) (Optic neuropathy-inducing protein) (Transcription factor IIIA-interacting protein) (TFIIIA-IntP)
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.
28-MAR-2018, sequence version 3.
28-MAR-2018, entry version 144.
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 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 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 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).
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].
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).
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]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TBK1 AND
BLUETONGUE VIRUS PROTEIN NS3.
PubMed=27538435; DOI=10.1186/s12915-016-0292-z;
Pourcelot M., Zemirli N., Silva Da Costa L., Loyant R., Garcin D.,
Vitour D., Munitic I., Vazquez A., Arnoult D.;
"The Golgi apparatus acts as a platform for TBK1 activation after
viral RNA sensing.";
BMC Biol. 14:69-69(2016).
[27]
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).
[28]
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).
[29]
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).
[30]
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).
[31]
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).
[32]
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).
[33]
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).
[34]
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).
[35]
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).
[36]
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).
[37]
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).
[38]
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).
[39]
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).
[40]
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).
[41]
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).
[42]
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). Plays a role in the
activation of innate immune response during viral infection.
Mechanistically, recruits TBK1 at the Golgi apparatus, promoting
its trans-phosphorylation after RLR or TLR3 stimulation
(PubMed:27538435). In turn, activated TBK1 phosphorylates its
downstream partner IRF3 to produce IFN-beta. Plays a
neuroprotective role in the eye and optic nerve. 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 recruitment 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. {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,
ECO:0000269|PubMed:27538435}.
-!- FUNCTION: (Microbial infection) May constitute a cellular target
for adenovirus E3 14.7 and Bluetongue virus protein NS3 to inhibit
innate immune response. {ECO:0000269|PubMed:27538435,
ECO:0000269|PubMed:9488477}.
-!- 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 TBK1; this interaction leads to the Golgi
localization of TBK1 and its subsequent activation.
{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:27538435, ECO:0000269|PubMed:9700202}.
-!- SUBUNIT: (Microbial infection) Interacts with E3 14.7 kDa protein
of group C human adenovirus (PubMed:9488477). Interacts with
Bluetongue virus protein NS3 (PubMed:27538435).
{ECO:0000269|PubMed:27538435, ECO:0000269|PubMed:9488477}.
-!- INTERACTION:
Self; NbExp=15; 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;
Q29122:MYO6 (xeno); NbExp=3; IntAct=EBI-748974, EBI-15804516;
P54845-1:NRL; NbExp=6; IntAct=EBI-748974, EBI-9819090;
P40302:PRE5 (xeno); NbExp=3; IntAct=EBI-748974, 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-748974, 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=15; 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=15; 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,
ECO:0000269|PubMed:27538435}. 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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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; 96.
MINT; Q96CV9; -.
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: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:0045087; P:innate immune response; IEA:UniProtKB-KW.
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:SF2; PTHR31553:SF2; 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; Immunity; Innate immunity; 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 E -> K (in dbSNP:rs523747).
/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:rs75654767).
{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; 65922 MW; 2BAF841BA515AAE2 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 SEAELMKKRL 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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Pathways :
WP2199: Seed Development
WP2272: Pathogenic Escherichia coli infection
WP731: Sterol regulatory element binding protein related
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation
Related Genes :
[OPTN FIP2 GLC1E HIP7 HYPL NRP] Optineurin (E3-14.7K-interacting protein) (FIP-2) (Huntingtin yeast partner L) (Huntingtin-interacting protein 7) (HIP-7) (Huntingtin-interacting protein L) (NEMO-related protein) (Optic neuropathy-inducing protein) (Transcription factor IIIA-interacting protein) (TFIIIA-IntP)
[Optn] Optineurin
[Optn] Optineurin (FIP-2-like protein)
[OPTN] Optineurin (Ag9-C5) (FIP-2)
[OPTN] Optineurin
[OPTN] Optineurin
[optn si:ch211-240l19.3 zgc:66386 zgc:77868] Optineurin
[OPTN QflA-13191 QmoA-11721] Optineurin
[OPTN] Optineurin
[TBK1 NAK] Serine/threonine-protein kinase TBK1 (EC 2.7.11.1) (NF-kappa-B-activating kinase) (T2K) (TANK-binding kinase 1)
[OPTN] Optineurin
[OPTN] Optineurin
[OPTN] Optineurin
[optn] Optineurin
[OPTN] Optineurin
[OPTN] Optineurin
[OPTN] Optineurin
[OPTN] Optineurin
[Optn] Optineurin
[OPTN] Optineurin
[OPTN] Optineurin
[OPTN] Optineurin
[OPTN] Optineurin
[OPTN] Optineurin
[OPTN] Optineurin
[OPTN] Optineurin
[OPTN] Optineurin
[OPTN] Optineurin
[OPTN] Optineurin
[OPTN] Optineurin
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