Rho
entrez
212541
canonical
uniprot
P15409
canonical
ensembl
ENSMUSG00000030324
resolver
ensp
ENSMUSP00000032471
resolver
enst
ENSMUST00000032471
resolver
genesymbol
Rho
resolver
uniprot
Q8K0D8
resolver
uniprot
Q96DZ2
resolver
uniprot_entry
OPSD_MOUSE
resolver
uniprot_sec
Q8K0D8
resolver
uniprot_sec
Q96DZ2
resolver
amino_acid_sequence
MNGTEGPNFYVPFSNVTGVVRSPFEQPQYYLAEPWQFSMLAAYMFLLIVLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADLFMVFGGFTTTLYTSLHGYFVFGPTGCNLEGFFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVVFTWIMALACAAPPLVGWSRYIPEGMQCSCGIDYYTLKPEVNNESFVIYMFVVHFTIPMIVIFFCYGQLVFTVKEAAAQQQESATTQKAEKEVTRMVIIMVIFFLICWLPYASVAFYIFTHQGSNFGPIFMTLPAFFAKSSSIYNPVIYIMLNKQFRNCMLTTLCCGKNPLGDDDASATASKTETSQVAPA
uniprot
proteins
function
FUNCTION: G protein-coupled photoreceptor that activates the G protein transducin (t) signaling pathway in response to light and is essential for image-forming vision under low-light conditions. Required for postnatal photoreceptor cell viability (PubMed:9020854). Activation occurs when the covalently bound 11-cis-retinal chromophore absorbs a photon and isomerizes to all-trans-retinal, inducing a conformational change in the opsin that triggers G protein-mediated phototransduction. Signal termination occurs via receptor phosphorylation, which promotes binding of arrestin (SAG) and displacement of the G protein alpha subunit (PubMed:27353443). {ECO:0000269|PubMed:27353443, ECO:0000269|PubMed:9020854}.
uniprot
proteins
mass_dalton
39070
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region. {ECO:0000269|PubMed:11910029}.; PTM: Contains one covalently linked retinal chromophore. Upon light absorption, the covalently bound 11-cis-retinal is converted to all-trans-retinal. After hydrolysis of the Schiff base and release of the covalently bound all-trans-retinal, active rhodopsin is regenerated by binding of a fresh molecule of 11-cis-retinal. {ECO:0000250|UniProtKB:P02699}.; PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region (By similarity). {ECO:0000250|UniProtKB:P02699}.; PTM: Contains one covalently linked retinal chromophore. Upon light absorption, the covalently bound 11-cis-retinal is converted to all-trans-retinal. Following activation, the covalently bound all-trans-retinal is released through hydrolysis of the Schiff base, and rhodopsin is regenerated by binding a new 11-cis-retinal molecule. {ECO:0000250|UniProtKB:P08100}.
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
protein_family
Opsin subfamily
uniprot
proteins
pubmed
11910029
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15961391
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
1978723
uniprot
proteins
pubmed
27353443
uniprot
proteins
pubmed
27509380
uniprot
proteins
pubmed
28151698
uniprot
proteins
pubmed
2844600
uniprot
proteins
pubmed
32312889
uniprot
proteins
pubmed
9020854
uniprot
proteins
sequence_length
348
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Photoreceptor outer segment membrane {ECO:0000250|UniProtKB:P08100}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P08100}. Membrane {ECO:0000250|UniProtKB:P08100}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P08100}. Note=Synthesized in the inner segment (IS) of rod photoreceptor cells before vectorial transport to disk membranes in the rod outer segment (OS) photosensory cilia. {ECO:0000250|UniProtKB:P08100}.
uniprot
proteins
transmembrane_region
TRANSMEM 37..61; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:P02699"; TRANSMEM 74..96; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:P02699"; TRANSMEM 111..133; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:P02699"; TRANSMEM 153..173; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:P02699"; TRANSMEM 203..224; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:P02699"; TRANSMEM 253..274; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:P02699"; TRANSMEM 287..308; /note="Helical; Name=7"; /evidence="ECO:0000250|UniProtKB:P02699
uniprot
proteins