ID OPTN_MACFA Reviewed; 571 AA. AC Q95KA2; Q9BGR3; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 29-MAR-2005, sequence version 2. DT 15-FEB-2017, entry version 61. DE RecName: Full=Optineurin; GN Name=OPTN; ORFNames=QflA-13191, QmoA-11721; OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9541; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Frontal cortex, and Medulla oblongata; RA Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K., RA Suzuki Y., Sugano S., Hashimoto K.; RT "Isolation of full-length cDNA clones from macaque brain cDNA RT libraries."; RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Plays an important role in the maintenance of the Golgi CC complex, in membrane trafficking, in exocytosis, through its CC interaction with myosin VI and Rab8. Links myosin VI to the Golgi CC complex and plays an important role in Golgi ribbon formation. CC Negatively regulates the induction of IFNB in response to RNA CC virus infection. Plays a neuroprotective role in the eye and optic CC nerve. Probably part of the TNF-alpha signaling pathway that can CC shift the equilibrium toward induction of cell death. May act by CC regulating membrane trafficking and cellular morphogenesis via a CC complex that contains Rab8 and hungtingtin (HD). Mediates the CC interaction of Rab8 with the probable GTPase-activating protein CC TBC1D17 during Rab8-mediated endocytic trafficking, such as of CC transferrin receptor (TFRC/TfR); regulates Rab8 recruitnment to CC tubules emanating from the endocytic recycling compartment. CC Autophagy receptor that interacts directly with both the cargo to CC become degraded and an autophagy modifier of the MAP1 LC3 family; CC targets ubiquitin-coated bacteria (xenophagy) and appears to CC function in the same pathway as SQSTM1 and CALCOCO2/NDP52 (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts with HD, Rab8 (RAB8A and/or RAB8B) (active GTP- CC bound form), GTF3A, TRAF3, TBK1, MYO6 and TFRC. Binds to linear CC ubiquitin chains. Interacts with LC3 family members MAP1LC3A, CC MAP1LC3B, GABARAP, GABARAPL1 and GABARAPL2; OPTN phosphorylation CC increases the association (at least with MAP1LC3B). Self- CC associates. Interacts with RAB12; the interaction may be indirect CC (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. CC Golgi apparatus {ECO:0000250}. Golgi apparatus, trans-Golgi CC network {ECO:0000250}. Cytoplasmic vesicle, autophagosome CC {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Recycling CC endosome {ECO:0000250}. Note=Found in the perinuclear region and CC associates with the Golgi apparatus. Colocalizes with MYO6 and CC RAB8 at the Golgi complex and in vesicular structures close to the CC plasma membrane. Localizes to LC3-positive cytoplasmic vesicles CC upon induction of autophagy (By similarity). {ECO:0000250}. CC -!- DOMAIN: The LIR (LC3-interacting region) motif mediates the CC interaction with ATG8 family proteins. {ECO:0000250}. CC -!- DOMAIN: Ubiquitin-binding motif (UBAN) is essential for its CC inhibitory function, subcellular localization and interaction with CC TBK1. {ECO:0000250}. CC -!- PTM: Phosphorylated by TBK1, leading to restrict bacterial CC proliferation in case of infection. {ECO:0000250}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB60774.1; Type=Frameshift; Positions=23; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB056409; BAB33067.1; -; mRNA. DR EMBL; AB063036; BAB60774.1; ALT_FRAME; mRNA. DR RefSeq; NP_001272065.1; NM_001285136.1. DR RefSeq; XP_015310940.1; XM_015455454.1. DR RefSeq; XP_015310941.1; XM_015455455.1. DR RefSeq; XP_015310942.1; XM_015455456.1. DR RefSeq; XP_015310943.1; XM_015455457.1. DR RefSeq; XP_015310944.1; XM_015455458.1. DR RefSeq; XP_015310945.1; XM_015455459.1. DR UniGene; Mfa.174; -. DR ProteinModelPortal; Q95KA2; -. DR GeneID; 102122718; -. DR KEGG; mcf:102122718; -. DR CTD; 10133; -. DR HOVERGEN; HBG106481; -. DR KO; K19946; -. DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell. DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW. DR GO; GO:0090161; P:Golgi ribbon formation; ISS:UniProtKB. DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro. DR Gene3D; 1.20.5.990; -; 1. DR InterPro; IPR032419; CC2-LZ_dom. DR InterPro; IPR021063; NEMO_N. DR InterPro; IPR032939; Optineurin. DR PANTHER; PTHR31553:SF6; PTHR31553:SF6; 1. DR Pfam; PF16516; CC2-LZ; 1. DR Pfam; PF11577; NEMO; 1. DR PROSITE; PS51801; ZF_CCHC_NOA; 1. PE 2: Evidence at transcript level; KW Autophagy; Coiled coil; Cytoplasm; Cytoplasmic vesicle; Endosome; KW Golgi apparatus; Metal-binding; Phosphoprotein; Zinc; Zinc-finger. FT CHAIN 1 571 Optineurin. FT /FTId=PRO_0000058067. FT ZN_FING 541 571 CCHC NOA-type. {ECO:0000255|PROSITE- FT ProRule:PRU01142}. FT REGION 58 209 Interaction with Rab8. {ECO:0000250}. FT REGION 405 571 Interaction with HD. {ECO:0000250}. FT REGION 406 514 Interaction with MYO6. {ECO:0000250}. FT COILED 38 170 {ECO:0000255}. FT COILED 233 502 {ECO:0000255}. FT MOTIF 176 181 LIR. FT MOTIF 468 473 UBAN. FT MOD_RES 177 177 Phosphoserine; by TBK1. {ECO:0000250}. FT MOD_RES 198 198 Phosphoserine. FT {ECO:0000250|UniProtKB:Q96CV9}. FT MOD_RES 336 336 Phosphoserine. FT {ECO:0000250|UniProtKB:Q96CV9}. FT MOD_RES 520 520 Phosphoserine. FT {ECO:0000250|UniProtKB:Q96CV9}. SQ SEQUENCE 571 AA; 65046 MW; D5D6822940397E1D CRC64; MSHQPLSCLT EKGDSPSEST GNGPPHLAHP NLDTFTPEEL LQQMKELLTE NHQLKEAMKL NNQAMKGRFE ELSAWTEKQK EERQFFETQS KEAKERLMAL SHENEKLKEE LGKLKGKSER SSEDPTGDSR LPRAEAEQEK DQLRTQVTRL QAEKADLLGI VSELQLKLNS SGSSEDSFVE IRMAEGEAEG SVKEIKHSPG PTRTVSIGTS RSAEGAKNYL EHEELTVSQL LLCLREGNQK VERLEIALKE AKERVSDFEK KASNRSEIET QTEGSTEKEN EEEKGPETVG SEVEALNLQV TSLFKELQEA HTKLSEAELM KKRLQEKCQA LERKNSATPS ELNEKQELVY TNKKLELQVE SMLSEIKMEQ AKTEDEKSKL AMLQLTHNKL LQEHNHALKT IEELTRKESE KVDRAVLKEL SEKLELAEKA LASKQLQMDE MKQTIAKQEE DLETMTVLRA QMEVYCSDFH AERAAREKIH EEKEQLALQL AVLLKENDAF EDGGRQSLME MQSRHGARTS DPDQQAYLVQ RGTEDRDWQQ QRNIPIHSCP KCGEVLPDID TLQIHVMDCI I //