OPTN
entrez
10133
canonical
uniprot
Q96CV9
canonical
ensembl
ENSG00000123240
resolver
ensp
ENSP00000368021
resolver
ensp
ENSP00000368022
resolver
ensp
ENSP00000368032
resolver
ensp
ENSP00000537587
resolver
genesymbol
OPTN
resolver
genesymbol_syn
FIP2
resolver
genesymbol_syn
GLC1E
resolver
genesymbol_syn
HIP7
resolver
genesymbol_syn
HYPL
resolver
genesymbol_syn
NRP
resolver
hgnc
HGNC:17142
resolver
uniprot
B3KP00
resolver
uniprot
D3DRS4
resolver
uniprot
D3DRS8
resolver
uniprot
Q5T672
resolver
uniprot
Q5T673
resolver
uniprot
Q5T674
resolver
uniprot
Q5T675
resolver
uniprot
Q7LDL9
resolver
uniprot
Q8N562
resolver
uniprot
Q9UET9
resolver
uniprot
Q9UEV4
resolver
uniprot
Q9Y218
resolver
uniprot_entry
OPTN_HUMAN
resolver
uniprot_sec
B3KP00
resolver
uniprot_sec
D3DRS4
resolver
uniprot_sec
D3DRS8
resolver
uniprot_sec
Q5T672
resolver
uniprot_sec
Q5T673
resolver
uniprot_sec
Q5T674
resolver
uniprot_sec
Q5T675
resolver
uniprot_sec
Q7LDL9
resolver
uniprot_sec
Q8N562
resolver
uniprot_sec
Q9UET9
resolver
uniprot_sec
Q9UEV4
resolver
uniprot_sec
Q9Y218
resolver
amino_acid_sequence
MSHQPLSCLTEKEDSPSESTGNGPPHLAHPNLDTFTPEELLQQMKELLTENHQLKEAMKLNNQAMKGRFEELSAWTEKQKEERQFFEIQSKEAKERLMALSHENEKLKEELGKLKGKSERSSEDPTDDSRLPRAEAEQEKDQLRTQVVRLQAEKADLLGIVSELQLKLNSSGSSEDSFVEIRMAEGEAEGSVKEIKHSPGPTRTVSTGTALSKYRSRSADGAKNYFEHEELTVSQLLLCLREGNQKVERLEVALKEAKERVSDFEKKTSNRSEIETQTEGSTEKENDEEKGPETVGSEVEALNLQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSAIPSELNEKQELVYTNKKLELQVESMLSEIKMEQAKTEDEKSKLTVLQMTHNKLLQEHNNALKTIEELTRKESEKVDRAVLKELSEKLELAEKALASKQLQMDEMKQTIAKQEEDLETMTILRAQMEVYCSDFHAERAAREKIHEEKEQLALQLAVLLKENDAFEDGGRQSLMEMQSRHGARTSDSDQQAYLVQRGAEDRDWRQQRNIPIHSCPKCGEVLPDIDTLQIHVMDCII
uniprot
proteins
disease_involvement
DISEASE: Glaucoma 1, open angle, E (GLC1E) [MIM:137760]: A form of primary open angle glaucoma (POAG). POAG is characterized by a specific pattern of optic nerve and visual field defects. The angle of the anterior chamber of the eye is open, and usually the intraocular pressure is increased. However, glaucoma can occur at any intraocular pressure. The disease is generally asymptomatic until the late stages, by which time significant and irreversible optic nerve damage has already taken place. {ECO:0000269|PubMed:11834836, ECO:0000269|PubMed:12939304, ECO:0000269|PubMed:14597044, ECO:0000269|PubMed:15226658, ECO:0000269|PubMed:15326130, ECO:0000269|PubMed:15557444, ECO:0000269|PubMed:17389490, ECO:0000269|PubMed:20085643, ECO:0000269|PubMed:20388642, ECO:0000269|PubMed:22854040, ECO:0000269|PubMed:23669351, ECO:0000269|PubMed:24752605}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Glaucoma, normal pressure (NPG) [MIM:606657]: A primary glaucoma characterized by intraocular pression consistently within the statistically normal population range. {ECO:0000269|PubMed:15370540}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Amyotrophic lateral sclerosis 12 with or without frontotemporal dementia (ALS12) [MIM:613435]: A form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases. ALS12 inheritance can be autosomal dominant or autosomal recessive. There is also sporadic occurrence. ALS12 patients may develop frontotemporal dementia. {ECO:0000269|PubMed:20428114, ECO:0000269|PubMed:27534431}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
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 (PubMed:27534431). Links myosin VI to the Golgi complex and plays an important role in Golgi ribbon formation (PubMed:27534431). Plays a role in the activation of innate immune response during viral infection. Mechanistically, recruits TBK1 at the Golgi apparatus, promoting its trans-phosphorylation after RLR or TLR3 stimulation (PubMed:27538435). In turn, activated TBK1 phosphorylates its downstream partner IRF3 to produce IFN-beta/IFNB1. Plays a neuroprotective role in the eye and optic nerve. May act by regulating membrane trafficking and cellular morphogenesis via a complex that contains Rab8 and huntingtin (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 (PubMed:22854040). 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), such as cytoplasmic Salmonella enterica, and appears to function in the same pathway as SQSTM1 and CALCOCO2/NDP52. {ECO:0000269|PubMed:11834836, ECO:0000269|PubMed:15837803, ECO:0000269|PubMed:20085643, ECO:0000269|PubMed:20174559, ECO:0000269|PubMed:21617041, ECO:0000269|PubMed:22854040, ECO:0000269|PubMed:27534431, ECO:0000269|PubMed:27538435}.; FUNCTION: (Microbial infection) May constitute a cellular target for various viruses, such as adenovirus E3 14.7 or Bluetongue virus, to inhibit innate immune response (PubMed:27538435, PubMed:9488477). During RNA virus infection, such as that of Sendai virus, negatively regulates the induction of IFNB1 (PubMed:20174559). {ECO:0000269|PubMed:20174559, ECO:0000269|PubMed:27538435, ECO:0000269|PubMed:9488477}.
uniprot
proteins
mass_dalton
65922
uniprot
proteins
mutagenesis
MUTAGEN 50; /note="E->K: No effect on retinal ganglion cell death, decreased interaction with TFRC, loss of localization to recycling endosomes, loss of ubiquitin-binding; when associated with N-474."; /evidence="ECO:0000269|PubMed:20085643, ECO:0000269|PubMed:24752605"; MUTAGEN 178; /note="F->A: Abolishes interaction with MAP1LC3A and GABARAPL1, no effect on binding to linear ubiquitin."; /evidence="ECO:0000269|PubMed:21617041, ECO:0000269|PubMed:23805866"; MUTAGEN 178; /note="F->W: Increases interaction with MAP1LC3B."; /evidence="ECO:0000269|PubMed:21617041, ECO:0000269|PubMed:23805866"; MUTAGEN 474..475; /note="DF->NA: Abolishes colocalization with cytosolic Salmonella."; /evidence="ECO:0000269|PubMed:21617041"; MUTAGEN 474; /note="D->N: No effect on retinal ganglion cell death, drastically decreased interaction with TFRC, loss of localization to recycling endosomes, loss of ubiquitin-binding; when associated with K-50."; /evidence="ECO:0000269|PubMed:20085643, ECO:0000269|PubMed:20174559, ECO:0000269|PubMed:24752605"; MUTAGEN 474; /note="D->N: Significant reduction in ubiquitin binding, decreased interaction with TBK1, loss of localization to recycling endosomes, disruption of interaction with TFRC, loss of inhibition of IFNB activation in response to TLR3 or RIG-I signaling, no effect on retinal ganglion cell death."; /evidence="ECO:0000269|PubMed:20085643, ECO:0000269|PubMed:20174559, ECO:0000269|PubMed:24752605
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by TBK1, leading to restrict bacterial proliferation in case of infection. Phosphorylation is induced by phorbol esters and decreases its half-time. {ECO:0000269|PubMed:10807909, ECO:0000269|PubMed:21617041}.
uniprot
proteins
pubmed
10756201
uniprot
proteins
pubmed
10807909
uniprot
proteins
pubmed
11137014
uniprot
proteins
pubmed
11834836
uniprot
proteins
pubmed
12379221
uniprot
proteins
pubmed
12646749
uniprot
proteins
pubmed
12939304
uniprot
proteins
pubmed
14597044
uniprot
proteins
pubmed
14627677
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
15226658
uniprot
proteins
pubmed
15326130
uniprot
proteins
pubmed
15370540
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15498064
uniprot
proteins
pubmed
15557444
uniprot
proteins
pubmed
15837803
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17389490
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20085643
uniprot
proteins
pubmed
20174559
uniprot
proteins
pubmed
20388642
uniprot
proteins
pubmed
20428114
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21617041
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
22854040
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23357852
uniprot
proteins
pubmed
23669351
uniprot
proteins
pubmed
23805866
uniprot
proteins
pubmed
23908376
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24705354
uniprot
proteins
pubmed
24752605
uniprot
proteins
pubmed
27534431
uniprot
proteins
pubmed
27538435
uniprot
proteins
pubmed
30266909
uniprot
proteins
pubmed
31371777
uniprot
proteins
pubmed
32185393
uniprot
proteins
pubmed
9488477
uniprot
proteins
pubmed
9700202
uniprot
proteins
sequence_length
577
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Golgi apparatus {ECO:0000269|PubMed:10807909, ECO:0000269|PubMed:20085643, ECO:0000269|PubMed:20174559, ECO:0000269|PubMed:27534431, ECO:0000269|PubMed:27538435}. Golgi apparatus, trans-Golgi network. Cytoplasmic vesicle, autophagosome. Cytoplasmic vesicle. Recycling endosome {ECO:0000269|PubMed:20085643}. Note=Found in the perinuclear region and associates with the Golgi apparatus (PubMed:27534431). 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. {ECO:0000269|PubMed:27534431}.
uniprot
proteins