OPTN_MACMU
ID OPTN_MACMU Reviewed; 571 AA.
AC Q861Q8;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Optineurin;
GN Name=OPTN;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Rezaie T., Sarfarazi M.;
RT "Genomic structure of optineurin (OPTN) in Rhesus monkey.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=11834836; DOI=10.1126/science.1066901;
RA Rezaie T., Child A., Hitchings R., Brice G., Miller L., Coca-Prados M.,
RA Heon E., Krupin T., Ritch R., Kreutzer D., Crick R.P., Sarfarazi M.;
RT "Adult-onset primary open-angle glaucoma caused by mutations in
RT optineurin.";
RL Science 295:1077-1079(2002).
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 -!- TISSUE SPECIFICITY: Present in aqueous humor of the eye (at protein
CC level). {ECO:0000269|PubMed:11834836}.
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}.
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DR EMBL; AY228374; AAO73054.1; -; mRNA.
DR EMBL; AY228373; AAO73053.1; -; mRNA.
DR EMBL; AY749122; AAV28653.1; -; Genomic_DNA.
DR EMBL; AY749110; AAV28653.1; JOINED; Genomic_DNA.
DR EMBL; AY749111; AAV28653.1; JOINED; Genomic_DNA.
DR EMBL; AY749112; AAV28653.1; JOINED; Genomic_DNA.
DR EMBL; AY749113; AAV28653.1; JOINED; Genomic_DNA.
DR EMBL; AY749114; AAV28653.1; JOINED; Genomic_DNA.
DR EMBL; AY749115; AAV28653.1; JOINED; Genomic_DNA.
DR EMBL; AY749116; AAV28653.1; JOINED; Genomic_DNA.
DR EMBL; AY749117; AAV28653.1; JOINED; Genomic_DNA.
DR EMBL; AY749118; AAV28653.1; JOINED; Genomic_DNA.
DR EMBL; AY749119; AAV28653.1; JOINED; Genomic_DNA.
DR EMBL; AY749120; AAV28653.1; JOINED; Genomic_DNA.
DR EMBL; AY749121; AAV28653.1; JOINED; Genomic_DNA.
DR RefSeq; NP_001028069.1; NM_001032897.1.
DR RefSeq; XP_015001948.1; XM_015146462.1.
DR RefSeq; XP_015001949.1; XM_015146463.1.
DR RefSeq; XP_015001950.1; XM_015146464.1.
DR RefSeq; XP_015001951.1; XM_015146465.1.
DR AlphaFoldDB; Q861Q8; -.
DR SMR; Q861Q8; -.
DR STRING; 9544.ENSMMUP00000036260; -.
DR Ensembl; ENSMMUT00000007881; ENSMMUP00000007407; ENSMMUG00000005601.
DR Ensembl; ENSMMUT00000043249; ENSMMUP00000036258; ENSMMUG00000005601.
DR Ensembl; ENSMMUT00000043250; ENSMMUP00000036259; ENSMMUG00000005601.
DR Ensembl; ENSMMUT00000092013; ENSMMUP00000079351; ENSMMUG00000005601.
DR Ensembl; ENSMMUT00000102245; ENSMMUP00000067667; ENSMMUG00000005601.
DR GeneID; 574252; -.
DR KEGG; mcc:574252; -.
DR CTD; 10133; -.
DR VEuPathDB; HostDB:ENSMMUG00000005601; -.
DR VGNC; VGNC:75415; OPTN.
DR eggNOG; ENOG502QTG2; Eukaryota.
DR GeneTree; ENSGT00530000063808; -.
DR HOGENOM; CLU_034097_1_0_1; -.
DR InParanoid; Q861Q8; -.
DR OrthoDB; 745047at2759; -.
DR Proteomes; UP000006718; Chromosome 9.
DR Bgee; ENSMMUG00000005601; Expressed in hindlimb stylopod muscle and 22 other tissues.
DR ExpressionAtlas; Q861Q8; baseline.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
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:0034067; P:protein localization to Golgi apparatus; IBA:GO_Central.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
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 1: Evidence at protein 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_0000058068"
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; 65104 MW; FB8B1305CFF7AE6E CRC64;
MSHQPLSCLT EKGDSPSEST GNGPPHLAHP NLDTFTPEEL LQQMKELLTE NHQLKEAMKL
NNQAMKGRFE ELSAWTEKQK EERQFFETQS KEAKERLMAL SHENEKLKEE LGKLKGKSER
SSEDPTDDSR 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
