OPN4
entrez
94233
canonical
uniprot
Q9UHM6
canonical
ensembl
ENSG00000122375
resolver
ensp
ENSP00000241891
resolver
ensp
ENSP00000361141
resolver
genesymbol
OPN4
resolver
genesymbol_syn
MOP
resolver
hgnc
HGNC:14449
resolver
uniprot
B7ZLB3
resolver
uniprot
Q14D01
resolver
uniprot
Q2PP22
resolver
uniprot
Q8NGQ9
resolver
uniprot_entry
OPN4_HUMAN
resolver
uniprot_sec
B7ZLB3
resolver
uniprot_sec
Q14D01
resolver
uniprot_sec
Q2PP22
resolver
uniprot_sec
Q8NGQ9
resolver
amino_acid_sequence
MNPPSGPRVPPSPTQEPSCMATPAPPSWWDSSQSSISSLGRLPSISPTAPGTWAAAWVPLPTVDVPDHAHYTLGTVILLVGLTGMLGNLTVIYTFCRSRSLRTPANMFIINLAVSDFLMSFTQAPVFFTSSLYKQWLFGETGCEFYAFCGALFGISSMITLTAIALDRYLVITRPLATFGVASKRRAAFVLLGVWLYALAWSLPPFFGWSAYVPEGLLTSCSWDYMSFTPAVRAYTMLLCCFVFFLPLLIIIYCYIFIFRAIRETGRALQTFGACKGNGESLWQRQRLQSECKMAKIMLLVILLFVLSWAPYSAVALVAFAGYAHVLTPYMSSVPAVIAKASAIHNPIIYAITHPKYRVAIAQHLPCLGVLLGVSRRHSRPYPSYRSTHRSTLTSHTSNLSWISIRRRQESLGSESEVGWTHMEAAAVWGAAQQANGRSLYGQGLEDLEAKAPPRPQGHEAETPGKTKGLIPSQDPRM
uniprot
proteins
function
FUNCTION: G protein-coupled photoreceptor that signals through the G(q/11) family of G proteins in response to light in intrinsically photosensitive retinal ganglion cells (ipRGCs) (By similarity). Can also activate other G proteins, including G(i/o) and G(s), depending on the cell type, leading to either activation or inhibition of adenylate cyclase and cAMP-dependent signaling (PubMed:35274137). Activation occurs when opsin-bound cis-retinal chromophore absorbs a photon and isomerizes to all-trans-retinal, inducing a conformational change in the opsin that triggers a G protein-mediated phototransduction cascade (PubMed:15674244). Acts as a bistable protein, allowing photoreversible regeneration of the cis-retinal chromophore after stimulation (PubMed:15674244). Contributes to non-image-forming visual response to light in ipRGCs, including the pupillary light reflex and the regulation of circadian rhythms (By similarity). In M1 ipRGCs (non-image forming) subtypes, activates a G(q)-phospholipase C (PLC) signaling cascade leading to depolarization through opening of TRPC6/7 channels and decreased intrisic excitability (By similarity). Mediates phototransduction in M4 ipRGCs (image forming) subtypes across dim to bright light conditions via G(q)-PLC signaling, resulting in increased intrisic excitability through closure of potassium leak channels (most likely TASK channels), thereby enhancing contrast sensitivity (By similarity). At bright light intensities, further enhances depolarization in M4 ipRGCs via activation of TRPC channels (By similarity). May be involved in the optokinetic visual tracking response. May also play a role in regulating retinal hyaloid vessel growth and regression (By similarity). {ECO:0000250|UniProtKB:Q9QXZ9, ECO:0000269|PubMed:15674244, ECO:0000269|PubMed:35274137}.; FUNCTION: [Isoform 2]: In contrast with isoform 1, cannot activate G(i/o) and G(s) family of G proteins in response to light. {ECO:0000269|PubMed:35274137}.
uniprot
proteins
mass_dalton
52635
uniprot
proteins
post_translational_modification
PTM: Contains one retinal chromophore covalently bound to a lysine residue via a Schiff base. Upon light absorption, the bound 11-cis-retinal isomerizes to all-trans-retinal. Following light exposure, all-trans-retinal is photoreconverted to 11-cis-retinal. {ECO:0000269|PubMed:15674244}.
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
protein_family
Opsin subfamily
uniprot
proteins
pubmed
10632589
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15674244
uniprot
proteins
pubmed
35274137
uniprot
proteins
sequence_length
478
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:35274137}; Multi-pass membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000250|UniProtKB:Q9QXZ9}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9QXZ9}. Perikaryon {ECO:0000250|UniProtKB:Q9QXZ9}.
uniprot
proteins
transmembrane_region
TRANSMEM 73..93; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 108..128; /note="Helical; Name=2"; /evidence="ECO:0000255"; TRANSMEM 145..165; /note="Helical; Name=3"; /evidence="ECO:0000255"; TRANSMEM 189..209; /note="Helical; Name=4"; /evidence="ECO:0000255"; TRANSMEM 239..259; /note="Helical; Name=5"; /evidence="ECO:0000255"; TRANSMEM 297..317; /note="Helical; Name=6"; /evidence="ECO:0000255"; TRANSMEM 333..353; /note="Helical; Name=7"; /evidence="ECO:0000255
uniprot
proteins