OPTN_PONAB
ID OPTN_PONAB Reviewed; 527 AA.
AC Q5R923;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Optineurin;
GN Name=OPTN;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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: Ubiquitin-binding motif (UBAN) is essential for its inhibitory
CC function, subcellular localization and interaction with TBK1.
CC {ECO:0000250}.
CC -!- DOMAIN: The LIR (LC3-interacting region) motif mediates the interaction
CC with ATG8 family proteins. {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; CR859573; CAH91737.1; -; mRNA.
DR RefSeq; NP_001126008.1; NM_001132536.1.
DR AlphaFoldDB; Q5R923; -.
DR SMR; Q5R923; -.
DR GeneID; 100172952; -.
DR KEGG; pon:100172952; -.
DR CTD; 10133; -.
DR InParanoid; Q5R923; -.
DR Proteomes; UP000001595; 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; 2.
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..527
FT /note="Optineurin"
FT /id="PRO_0000058071"
FT ZN_FING 497..527
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 101..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..527
FT /note="Interaction with HD"
FT /evidence="ECO:0000250"
FT REGION 362..470
FT /note="Interaction with MYO6"
FT /evidence="ECO:0000250"
FT COILED 38..170
FT /evidence="ECO:0000255"
FT COILED 239..458
FT /evidence="ECO:0000255"
FT MOTIF 176..181
FT /note="LIR"
FT MOTIF 424..429
FT /note="UBAN"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 505
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01142"
FT BINDING 508
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01142"
FT BINDING 521
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01142"
FT BINDING 525
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 476
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96CV9"
SQ SEQUENCE 527 AA; 60159 MW; D9DE65E566439317 CRC64;
MSHQPLSCLT EKEDSPTEST GNGPPYLAHP NLDTFTPEEL LQQMKELLTE NHQLKEAMKL
NNQAMKGRFE ELSAWTEKQK EERQFFEIQS KEAKERLMAL SHENEKLKEE LGKLKGKSER
SSEDPTDDSR LPRAEAEQEK DQLRTQVVRL QAEKADLLGI VSELQLKLNS SGSSEDSFVE
IRMAEGEAEG SVKEIKHSPG PTRTVSTSRA LSKYRSRSAE GAKNYLEHEE LTVSQLLLCL
REGNQKVERL EIALKEAKER VSDFEKKASN RSEIETQTEG STEKENDEEK GLETVGSEVE
ALNLQVTSLF KELQEAHTKL SEAELMKKRL QEKSKLTVLQ MTHNKLLREH NNALKTIEEL
TRKESEKVDR AVLKELSEKL ELAEQALASK QLQMDEMKQT IAKQEEDLET MTVLRAQMEV
YCSDFHAERA AREKIHEQKE QLALQLAVLL KENDAFEDGG RQSLMEMQSR HGARTSGADQ
QAYLVQRGAE DRDWRQQRNI PIHSCPKCGE VLPDIDTLQI HVMDCII
