Opn1sw
entrez
12057
canonical
uniprot
P51491
canonical
ensembl
ENSMUSG00000058831
resolver
ensp
ENSMUSP00000079289
resolver
enst
ENSMUST00000080428
resolver
genesymbol
Opn1sw
resolver
genesymbol_syn
Bcp
resolver
uniprot
Q548Z8
resolver
uniprot_entry
OPSB_MOUSE
resolver
uniprot_sec
Q548Z8
resolver
amino_acid_sequence
MSGEDDFYLFQNISSVGPWDGPQYHLAPVWAFRLQAAFMGFVFFVGTPLNAIVLVATLHYKKLRQPLNYILVNVSLGGFLFCIFSVFTVFIASCHGYFLFGRHVCALEAFLGSVAGLVTGWSLAFLAFERYVVICKPFGSIRFNSKHALMVVLATWIIGIGVSIPPFFGWSRFIPEGLQCSCGPDWYTVGTKYRSEYYTWFLFIFCFIIPLSLICFSYSQLLRTLRAVAAQQQESATTQKAEREVSHMVVVMVGSFCLCYVPYAALAMYMVNNRNHGLDLRLVTIPAFFSKSSCVYNPIIYCFMNKQFRACILEMVCRKPMADESDVSGSQKTEVSTVSSSKVGPH
uniprot
proteins
function
FUNCTION: G protein-coupled photoreceptor that selectively activates transducin G alpha protein (G(t)) in response to short-wavelength (blue-violet) light, thereby stimulating the G(t)/transducin protein pathway (By similarity). This activation leads to increased cGMP phosphodiesterase activity, resulting in decreased intracellular cGMP and subsequent closure of cGMP-gated ion channels. The process is initiated when the opsin-bound cis-retinal chromophore absorbs a photon and isomerizes to all-trans-retinal, inducing a conformational change in the opsin that triggers the G protein-mediated phototransduction cascade (By similarity). Required for the maintenance of cone outer segment organization in the ventral retina, but not essential for the maintenance of cone photoreceptor function (PubMed:21219924, PubMed:25416279). Involved in ensuring the correct abundance and localization of retinal membrane proteins (PubMed:25416279). Mediates visual perception of blue light (By similarity). May contribute to increased spectral sensitivity under dim light conditions (PubMed:11055434). Is not UV-sensitive (By similarity). {ECO:0000250|UniProtKB:D5H3X0, ECO:0000250|UniProtKB:P03999, ECO:0000250|UniProtKB:P04000}.
uniprot
proteins
mass_dalton
38922
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region.; 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 activation, the covalently bound all-trans-retinal is released through hydrolysis of the Schiff base, and OPN1 is regenerated by binding a new 11-cis-retinal molecule. {ECO:0000250|UniProtKB:P03999}.
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
protein_family
Opsin subfamily
uniprot
proteins
pubmed
11055434
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
21219924
uniprot
proteins
pubmed
25416279
uniprot
proteins
pubmed
8088841
uniprot
proteins
sequence_length
346
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P03999}; Multi-pass membrane protein {ECO:0000255}. Photoreceptor outer segment membrane {ECO:0000269|PubMed:11055434, ECO:0000269|PubMed:21219924}; Multi-pass membrane protein {ECO:0000255}. Photoreceptor inner segment {ECO:0000269|PubMed:21219924}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P03999}.
uniprot
proteins
transmembrane_region
TRANSMEM 32..56; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 69..94; /note="Helical; Name=2"; /evidence="ECO:0000255"; TRANSMEM 109..128; /note="Helical; Name=3"; /evidence="ECO:0000255"; TRANSMEM 148..171; /note="Helical; Name=4"; /evidence="ECO:0000255"; TRANSMEM 198..225; /note="Helical; Name=5"; /evidence="ECO:0000255"; TRANSMEM 248..271; /note="Helical; Name=6"; /evidence="ECO:0000255"; TRANSMEM 280..304; /note="Helical; Name=7"; /evidence="ECO:0000255
uniprot
proteins