RHO
entrez
6010
canonical
uniprot
P08100
canonical
ensembl
ENSG00000163914
resolver
ensp
ENSP00000296271
resolver
enst
ENST00000296271
resolver
genesymbol
RHO
resolver
genesymbol_syn
OPN2
resolver
hgnc
HGNC:10012
resolver
uniprot
Q16414
resolver
uniprot
Q2M249
resolver
uniprot_entry
OPSD_HUMAN
resolver
uniprot_sec
Q16414
resolver
uniprot_sec
Q2M249
resolver
amino_acid_sequence
MNGTEGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQFSMLAAYMFLLIVLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADLFMVLGGFTSTLYTSLHGYFVFGPTGCNLEGFFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMALACAAPPLAGWSRYIPEGLQCSCGIDYYTLKPEVNNESFVIYMFVVHFTIPMIIIFFCYGQLVFTVKEAAAQQQESATTQKAEKEVTRMVIIMVIAFLICWVPYASVAFYIFTHQGSNFGPIFMTIPAFFAKSAAIYNPVIYIMMNKQFRNCMLTTICCGKNPLGDDEASATVSKTETSQVAPA
uniprot
proteins
disease_involvement
DISEASE: Retinitis pigmentosa 4 (RP4) [MIM:613731]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:12566452, ECO:0000269|PubMed:1302614, ECO:0000269|PubMed:1391967, ECO:0000269|PubMed:15145060, ECO:0000269|PubMed:1765377, ECO:0000269|PubMed:1833777, ECO:0000269|PubMed:1840561, ECO:0000269|PubMed:1862076, ECO:0000269|PubMed:1897520, ECO:0000269|PubMed:1985460, ECO:0000269|PubMed:19934218, ECO:0000269|PubMed:19960070, ECO:0000269|PubMed:2137202, ECO:0000269|PubMed:2215617, ECO:0000269|PubMed:22334370, ECO:0000269|PubMed:2239971, ECO:0000269|PubMed:7633434, ECO:0000269|PubMed:7981701, ECO:0000269|PubMed:7987326, ECO:0000269|PubMed:7987331, ECO:0000269|PubMed:8045708, ECO:0000269|PubMed:8076945, ECO:0000269|PubMed:8081400, ECO:0000269|PubMed:8088850, ECO:0000269|PubMed:8317502, ECO:0000269|PubMed:8353500, ECO:0000269|PubMed:8364589, ECO:0000269|PubMed:8401533, ECO:0000269|PubMed:8406457, ECO:0000269|PubMed:8554077, ECO:0000269|PubMed:9452035}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Night blindness, congenital stationary, autosomal dominant 1 (CSNBAD1) [MIM:610445]: A non-progressive retinal disorder characterized by impaired night vision, often associated with nystagmus and myopia. {ECO:0000269|PubMed:7846071, ECO:0000269|PubMed:8107847, ECO:0000269|PubMed:8358437, ECO:0000269|PubMed:9888392}. Note=The disease is caused by variants affecting the gene represented in this entry.
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 (PubMed:6140680, PubMed:7846071, PubMed:8107847). Required for postnatal photoreceptor cell viability (PubMed:12566452, PubMed:2215617). 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 (Probable) (PubMed:26200343, PubMed:28753425, PubMed:8107847). Signal termination occurs via receptor phosphorylation, which promotes binding of arrestin (SAG) and displacement of the G protein alpha subunit (Probable) (PubMed:26200343). {ECO:0000269|PubMed:12566452, ECO:0000269|PubMed:2215617, ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425, ECO:0000269|PubMed:6140680, ECO:0000269|PubMed:7846071, ECO:0000269|PubMed:8107847, ECO:0000305|PubMed:28524165}.
uniprot
proteins
mass_dalton
38893
uniprot
proteins
mutagenesis
MUTAGEN 113; /note="E->Q: Induces a conformation change that promotes interaction with GRK1 and SAG; when associated with Y-257."; /evidence="ECO:0000269|PubMed:26200343"; MUTAGEN 257; /note="M->Y: Induces a conformation change that promotes interaction with GRK1 and SAG; when associated with Q-113."; /evidence="ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28524165"; MUTAGEN 336..340; /note="TVSKT->AVAKA: Loss of phosphorylation sites and decreased interaction with SAG."; /evidence="ECO:0000269|PubMed:28753425"; MUTAGEN 336..338; /note="TVS->AVA: Loss of phosphorylation sites and decreased interaction with SAG; when associated with A-343."; /evidence="ECO:0000269|PubMed:28753425"; MUTAGEN 343; /note="S->A: Loss of phosphorylation sites and decreased interaction with SAG; when associated with 336-A--A-338."; /evidence="ECO:0000269|PubMed:28753425
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region (By similarity). After activation by light, phosphorylated by GRK1 (in vitro) (PubMed:28524165). {ECO:0000250|UniProtKB:P02699, ECO:0000269|PubMed:28524165}.; 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 (PubMed:12566452). {ECO:0000269|PubMed:12566452}.
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
protein_family
Opsin subfamily
uniprot
proteins
pubmed
12566452
uniprot
proteins
pubmed
1302614
uniprot
proteins
pubmed
1391967
uniprot
proteins
pubmed
15145060
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1765377
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
1833777
uniprot
proteins
pubmed
1840561
uniprot
proteins
pubmed
1862076
uniprot
proteins
pubmed
1897520
uniprot
proteins
pubmed
1985460
uniprot
proteins
pubmed
19934218
uniprot
proteins
pubmed
19960070
uniprot
proteins
pubmed
2137202
uniprot
proteins
pubmed
2215617
uniprot
proteins
pubmed
22334370
uniprot
proteins
pubmed
2239971
uniprot
proteins
pubmed
25664179
uniprot
proteins
pubmed
26200343
uniprot
proteins
pubmed
28524165
uniprot
proteins
pubmed
28753425
uniprot
proteins
pubmed
28837730
uniprot
proteins
pubmed
6140680
uniprot
proteins
pubmed
6589631
uniprot
proteins
pubmed
7633434
uniprot
proteins
pubmed
7846071
uniprot
proteins
pubmed
7981701
uniprot
proteins
pubmed
7987326
uniprot
proteins
pubmed
7987331
uniprot
proteins
pubmed
7987385
uniprot
proteins
pubmed
8045708
uniprot
proteins
pubmed
8076945
uniprot
proteins
pubmed
8081400
uniprot
proteins
pubmed
8088850
uniprot
proteins
pubmed
8107847
uniprot
proteins
pubmed
8317502
uniprot
proteins
pubmed
8353500
uniprot
proteins
pubmed
8358437
uniprot
proteins
pubmed
8364589
uniprot
proteins
pubmed
8401533
uniprot
proteins
pubmed
8406457
uniprot
proteins
pubmed
8554077
uniprot
proteins
pubmed
8566799
uniprot
proteins
pubmed
9452035
uniprot
proteins
pubmed
9888392
uniprot
proteins
sequence_length
348
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Photoreceptor outer segment membrane {ECO:0000269|PubMed:25664179}; Multi-pass membrane protein {ECO:0000269|PubMed:19934218, ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425}. Membrane {ECO:0000269|PubMed:12566452, ECO:0000269|PubMed:19934218, ECO:0000269|PubMed:25664179, ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425}; Multi-pass membrane protein {ECO:0000269|PubMed:19934218, ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425}. 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:0000269|PubMed:25664179}.
uniprot
proteins
transmembrane_region
TRANSMEM 37..61; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425"; TRANSMEM 74..96; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425"; TRANSMEM 111..133; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425"; TRANSMEM 153..173; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425"; TRANSMEM 203..224; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425"; TRANSMEM 253..274; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425"; TRANSMEM 285..309; /note="Helical; Name=7"; /evidence="ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
uniprot
proteins