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 03-AUG-2022, entry version 82. 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; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; OC 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 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 virus CC infection. Plays a neuroprotective role in the eye and optic nerve. CC Probably part of the TNF-alpha signaling pathway that can shift the CC equilibrium toward induction of cell death. May act by regulating CC membrane trafficking and cellular morphogenesis via a complex that CC contains Rab8 and hungtingtin (HD). Mediates the interaction of Rab8 CC with the probable GTPase-activating protein TBC1D17 during Rab8- CC mediated endocytic trafficking, such as of transferrin receptor CC (TFRC/TfR); regulates Rab8 recruitnment to tubules emanating from the CC endocytic recycling compartment. Autophagy receptor that interacts CC directly with both the cargo to become degraded and an autophagy CC modifier of the MAP1 LC3 family; targets ubiquitin-coated bacteria CC (xenophagy) and appears to function in the same pathway as SQSTM1 and CC CALCOCO2/NDP52. {ECO:0000250, ECO:0000250|UniProtKB:Q96CV9}. CC -!- SUBUNIT: Self-associates (By similarity). Interacts with HD, Rab8 CC (RAB8A and/or RAB8B) (active GTP-bound form), GTF3A, TRAF3, TBK1, MYO6 CC and TFRC. Binds to linear ubiquitin chains. Interacts with LC3 family CC members MAP1LC3A, MAP1LC3B, GABARAP, GABARAPL1 and GABARAPL2; OPTN CC phosphorylation increases the association (at least with MAP1LC3B). CC Interacts with RAB12; the interaction may be indirect (By similarity). CC Interacts with palmitoyltransferase ZDHHC17/HIP14; the interaction does CC not lead to palmitoylation of OPTN (By similarity). Interacts with CYLD CC (By similarity). {ECO:0000250|UniProtKB:Q96CV9}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. CC Golgi apparatus {ECO:0000250|UniProtKB:Q96CV9}. Golgi apparatus, trans- CC Golgi network {ECO:0000250}. Cytoplasmic vesicle, autophagosome CC {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Recycling endosome CC {ECO:0000250}. Note=Found in the perinuclear region and associates with CC the Golgi apparatus. Colocalizes with MYO6 and RAB8 at the Golgi CC complex and in vesicular structures close to the plasma membrane. CC Localizes to LC3-positive cytoplasmic vesicles upon induction of CC autophagy. {ECO:0000250, ECO:0000250|UniProtKB:Q96CV9}. CC -!- DOMAIN: The LIR (LC3-interacting region) motif mediates the interaction CC with ATG8 family proteins. {ECO:0000250}. CC -!- DOMAIN: Ubiquitin-binding motif (UBAN) is essential for its inhibitory CC function, subcellular localization and interaction with TBK1. CC {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; 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 AlphaFoldDB; Q95KA2; -. DR SMR; Q95KA2; -. DR STRING; 9541.XP_005564694.1; -. DR GeneID; 102122718; -. DR KEGG; mcf:102122718; -. DR CTD; 10133; -. DR eggNOG; ENOG502QTG2; Eukaryota. DR OrthoDB; 745047at2759; -. DR Proteomes; UP000233100; Unplaced. DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell. DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB. 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:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW. DR GO; GO:0034620; P:cellular response to unfolded protein; ISS:UniProtKB. DR GO; GO:0090161; P:Golgi ribbon formation; ISS:UniProtKB. DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro. DR InterPro; IPR032419; CC2-LZ_dom. DR InterPro; IPR021063; NEMO_N. DR InterPro; IPR034735; NEMO_ZF. DR InterPro; IPR032939; Optineurin. DR PANTHER; PTHR31553:SF2; PTHR31553:SF2; 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; Reference proteome; Zinc; KW Zinc-finger. FT CHAIN 1..571 FT /note="Optineurin" FT /id="PRO_0000058067" FT ZN_FING 541..571 FT /note="CCHC NOA-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01142" FT REGION 1..32 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 58..209 FT /note="Interaction with Rab8" FT /evidence="ECO:0000250" FT REGION 100..144 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 186..210 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 255..291 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 405..571 FT /note="Interaction with HD" FT /evidence="ECO:0000250" FT REGION 406..514 FT /note="Interaction with MYO6" FT /evidence="ECO:0000250" FT COILED 38..170 FT /evidence="ECO:0000255" FT COILED 233..502 FT /evidence="ECO:0000255" FT MOTIF 176..181 FT /note="LIR" FT MOTIF 468..473 FT /note="UBAN" FT COMPBIAS 1..24 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 255..289 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 549 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01142" FT BINDING 552 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01142" FT BINDING 565 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01142" FT BINDING 569 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01142" FT MOD_RES 177 FT /note="Phosphoserine; by TBK1" FT /evidence="ECO:0000250|UniProtKB:Q96CV9" FT MOD_RES 198 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q96CV9" FT MOD_RES 336 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q96CV9" FT MOD_RES 520 FT /note="Phosphoserine" FT /evidence="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 //