Q8R5M4 · OPTN_RAT
- ProteinOptineurin
- GeneOptn
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids585 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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. Links myosin VI to the Golgi complex and plays an important role in Golgi ribbon formation. Negatively regulates the induction of IFNB in response to RNA virus infection. Plays a neuroprotective role in the eye and optic nerve. Probably part of the TNF-alpha signaling pathway that can shift the equilibrium toward induction of cell death. 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 that 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) and appears to function in the same pathway as SQSTM1 and CALCOCO2/NDP52.
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameOptineurin
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ8R5M4
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Found in the perinuclear region and associates with the Golgi apparatus. 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.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000058072 | 1-585 | Optineurin | |||
Sequence: MSHQPLSCLTEKGDSSCETPGNGPSNMVHPNLDTFTPEELLQQMKELLVENHQLKEAMKLNNQAMKGRFEELSAWTEKQKEERQLFEIQSKEAKERLKALSHENERLKEELGKLKEKSERPFEDITGRCGFPRTDLEQEVEQLKRQVEQEVEHLKIQVRRLQAEKADLLGIVSELQLKLNSGGSSEDSFVEIRMTEGEAEGAMKEMRNSAGPTRTDSISMGKCTEDARTCVEFEELTVSQLLLCLREGNQKVERLEIALREAKERISDFEKKANGHSAIETQTEGSTQKEEEDKDPESVGIEVETLNVQVASLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELVYSNRKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHDKLLQEHNKALRTIEELTKQQAEKVDKVQLQELSEKLELAEQALASKQLQMDEMKQTIAKQEEDLETMAVLRAQMEVYCSDFHAERAAREKIHEEKEQLALQLAILLKENNDFEDGGSRQSLMEMQCRHGARTSDSDQQAYLFQRGAEDMSWQHGQQPRSIPIHSCPKCGEVLPDIDTLQIHVMDCII | ||||||
Modified residue | 188 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 209 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 346 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 531 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated by TBK1, leading to restrict bacterial proliferation in case of infection.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Self-associates (By similarity).
Interacts with HD, GTF3A, TRAF3, TBK1 and MYO6. Interacts (via UBAN) with ubiquitinated TFRC. Interacts with active GTP-bound Rab8 (RAB8A and/or RAB8B). Interacts with TBC1D17. 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). Interacts with RAB12; the interaction may be indirect (By similarity).
Interacts with palmitoyltransferase ZDHHC17/HIP14; the interaction does not lead to palmitoylation of OPTN (By similarity).
Interacts with CYLD (By similarity).
Interacts with TOM1; the interaction is indirect and is mediated by MYO6, which acts as a bridge between TOM1 and OPTN (By similarity).
Interacts with HD, GTF3A, TRAF3, TBK1 and MYO6. Interacts (via UBAN) with ubiquitinated TFRC. Interacts with active GTP-bound Rab8 (RAB8A and/or RAB8B). Interacts with TBC1D17. 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). Interacts with RAB12; the interaction may be indirect (By similarity).
Interacts with palmitoyltransferase ZDHHC17/HIP14; the interaction does not lead to palmitoylation of OPTN (By similarity).
Interacts with CYLD (By similarity).
Interacts with TOM1; the interaction is indirect and is mediated by MYO6, which acts as a bridge between TOM1 and OPTN (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, coiled coil, motif, compositional bias, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-32 | Disordered | ||||
Sequence: MSHQPLSCLTEKGDSSCETPGNGPSNMVHPNL | ||||||
Coiled coil | 38-181 | |||||
Sequence: EELLQQMKELLVENHQLKEAMKLNNQAMKGRFEELSAWTEKQKEERQLFEIQSKEAKERLKALSHENERLKEELGKLKEKSERPFEDITGRCGFPRTDLEQEVEQLKRQVEQEVEHLKIQVRRLQAEKADLLGIVSELQLKLNS | ||||||
Region | 58-220 | Interaction with Rab8 | ||||
Sequence: MKLNNQAMKGRFEELSAWTEKQKEERQLFEIQSKEAKERLKALSHENERLKEELGKLKEKSERPFEDITGRCGFPRTDLEQEVEQLKRQVEQEVEHLKIQVRRLQAEKADLLGIVSELQLKLNSGGSSEDSFVEIRMTEGEAEGAMKEMRNSAGPTRTDSISM | ||||||
Motif | 187-192 | LIR | ||||
Sequence: DSFVEI | ||||||
Region | 200-220 | Disordered | ||||
Sequence: EGAMKEMRNSAGPTRTDSISM | ||||||
Coiled coil | 244-512 | |||||
Sequence: CLREGNQKVERLEIALREAKERISDFEKKANGHSAIETQTEGSTQKEEEDKDPESVGIEVETLNVQVASLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELVYSNRKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHDKLLQEHNKALRTIEELTKQQAEKVDKVQLQELSEKLELAEQALASKQLQMDEMKQTIAKQEEDLETMAVLRAQMEVYCSDFHAERAAREKIHEEKEQLALQLAILLKENNDFED | ||||||
Region | 269-299 | Disordered | ||||
Sequence: FEKKANGHSAIETQTEGSTQKEEEDKDPESV | ||||||
Compositional bias | 285-299 | Basic and acidic residues | ||||
Sequence: GSTQKEEEDKDPESV | ||||||
Region | 415-585 | Interaction with HD | ||||
Sequence: TKQQAEKVDKVQLQELSEKLELAEQALASKQLQMDEMKQTIAKQEEDLETMAVLRAQMEVYCSDFHAERAAREKIHEEKEQLALQLAILLKENNDFEDGGSRQSLMEMQCRHGARTSDSDQQAYLFQRGAEDMSWQHGQQPRSIPIHSCPKCGEVLPDIDTLQIHVMDCII | ||||||
Region | 416-525 | Interaction with MYO6 | ||||
Sequence: KQQAEKVDKVQLQELSEKLELAEQALASKQLQMDEMKQTIAKQEEDLETMAVLRAQMEVYCSDFHAERAAREKIHEEKEQLALQLAILLKENNDFEDGGSRQSLMEMQCR | ||||||
Motif | 478-483 | UBAN | ||||
Sequence: DFHAER | ||||||
Zinc finger | 555-585 | CCHC NOA-type | ||||
Sequence: PRSIPIHSCPKCGEVLPDIDTLQIHVMDCII |
Domain
The LIR (LC3-interacting region) motif mediates the interaction with ATG8 family proteins.
Ubiquitin-binding motif (UBAN) is essential for its inhibitory function, subcellular localization and interaction with TBK1.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q8R5M4-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length585
- Mass (Da)67,014
- Last updated2005-03-29 v3
- Checksum05D3390151DADEC7
Q8R5M4-2
- Name2
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0G2K3Z1 | A0A0G2K3Z1_RAT | Optn | 569 | ||
M0RAB4 | M0RAB4_RAT | Optn | 585 | ||
F1M9C4 | F1M9C4_RAT | Optn | 647 |
Sequence caution
Features
Showing features for sequence conflict, alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 78 | in Ref. 1; BAB84696 | ||||
Sequence: K → R | ||||||
Alternative sequence | VSP_013263 | 156-195 | in isoform 2 | |||
Sequence: IQVRRLQAEKADLLGIVSELQLKLNSGGSSEDSFVEIRMT → NQ | ||||||
Sequence conflict | 172-174 | in Ref. 1 | ||||
Sequence: VSE → RLR | ||||||
Sequence conflict | 219 | in Ref. 1; BAB84696 | ||||
Sequence: S → I | ||||||
Compositional bias | 285-299 | Basic and acidic residues | ||||
Sequence: GSTQKEEEDKDPESV | ||||||
Sequence conflict | 316 | in Ref. 1; BAB84696 | ||||
Sequence: E → G | ||||||
Sequence conflict | 363 | in Ref. 1; BAB84696 | ||||
Sequence: R → W | ||||||
Alternative sequence | VSP_013264 | 515 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 545 | in Ref. 1; BAB84696 | ||||
Sequence: E → K |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB069907 EMBL· GenBank· DDBJ | BAB84696.2 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
BC086976 EMBL· GenBank· DDBJ | AAH86976.1 EMBL· GenBank· DDBJ | mRNA |