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RHO rhodopsin [ Bos taurus (cattle) ]

Gene ID: 509933, updated on 5-Mar-2024

Summary

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Official Symbol
RHOprovided by VGNC
Official Full Name
rhodopsinprovided by VGNC
Primary source
VGNC:VGNC:33942
See related
BGD:BT14158; Ensembl:ENSBTAG00000001310
Gene type
protein coding
RefSeq status
VALIDATED
Organism
Bos taurus
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos
Orthologs
human mouse all
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Genomic context

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Location:
chromosome: 22
Exon count:
5
Annotation release Status Assembly Chr Location
RS_2023_09 current ARS-UCD2.0 (GCF_002263795.3) 22 NC_037349.1 (56225120..56231448, complement)

Chromosome 22 - NC_037349.1Genomic Context describing neighboring genes Neighboring gene plexin D1 Neighboring gene H1.8 linker histone Neighboring gene intraflagellar transport 122 Neighboring gene DNA-directed RNA polymerase II subunit RPB1-like Neighboring gene methyl-CpG binding domain 4, DNA glycosylase

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_037349.1 Chromosome 22 Reference ARS-UCD2.0 Primary Assembly

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. New insights into the molecular mechanism of rhodopsin retinitis pigmentosa from the biochemical and functional characterization of G90V, Y102H and I307N mutations. Herrera-Hernández MG, et al. Cell Mol Life Sci, 2022 Jan 7. PMID 34997336, Free PMC Article
  2. Simple Models to Study Spectral Properties of Microbial and Animal Rhodopsins: Evaluation of the Electrostatic Effect of Charged and Polar Residues on the First Absorption Band Maxima. Shtyrov AA, et al. Int J Mol Sci, 2021 Mar 16. PMID 33809708, Free PMC Article
  3. Disruption of Hydrogen-Bond Network in Rhodopsin Mutations Cause Night Blindness. Katayama K, et al. J Mol Biol, 2020 Sep 4. PMID 32795534
  4. Conformational perturbation, allosteric modulation of cellular signaling pathways, and disease in P23H rhodopsin. Woods KN, et al. Sci Rep, 2020 Feb 14. PMID 32060349, Free PMC Article
  5. Cryo-EM structure of the rhodopsin-Gαi-βγ complex reveals binding of the rhodopsin C-terminal tail to the gβ subunit. Tsai CJ, et al. Elife, 2019 Jun 28. PMID 31251171, Free PMC Article

See all (172) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. New insights into the molecular mechanism of rhodopsin retinitis pigmentosa from the biochemical and functional characterization of G90V, Y102H and I307N mutations.
    Title: New insights into the molecular mechanism of rhodopsin retinitis pigmentosa from the biochemical and functional characterization of G90V, Y102H and I307N mutations.
  2. Simple Models to Study Spectral Properties of Microbial and Animal Rhodopsins: Evaluation of the Electrostatic Effect of Charged and Polar Residues on the First Absorption Band Maxima.
    Title: Simple Models to Study Spectral Properties of Microbial and Animal Rhodopsins: Evaluation of the Electrostatic Effect of Charged and Polar Residues on the First Absorption Band Maxima.
  3. Disruption of Hydrogen-Bond Network in Rhodopsin Mutations Cause Night Blindness.
    Title: Disruption of Hydrogen-Bond Network in Rhodopsin Mutations Cause Night Blindness.
  4. Conformational perturbation, allosteric modulation of cellular signaling pathways, and disease in P23H rhodopsin.
    Title: Conformational perturbation, allosteric modulation of cellular signaling pathways, and disease in P23H rhodopsin.
  5. Data suggest functionality for mutant R171 in stabilizing the inactive arrestin-1 conformation as well as the rhodopsin-arrestin-1 complex.
    Title: Arrestin-1 engineering facilitates complex stabilization with native rhodopsin.
  6. The density map reveals the receptor C-terminal tail bound to the Gbeta subunit of the G protein, providing a structural foundation for the role of the C-terminal tail in GPCR signaling, and of Gbeta as scaffold for recruiting Galpha subunits and G protein-receptor kinases.
    Title: Cryo-EM structure of the rhodopsin-Gαi-βγ complex reveals binding of the rhodopsin C-terminal tail to the gβ subunit.
  7. the binding of flavonoids to an RP-linked P23H opsin variant partially restored its normal cellular trafficking.
    Title: Flavonoids enhance rod opsin stability, folding, and self-association by directly binding to ligand-free opsin and modulating its conformation.
  8. Crystal structure of rhodopsin bound to an engineered mini-Go protein reveals that rhodopsin seems to adopt predominantly one thermodynamically stable active conformation.
    Title: Crystal structure of rhodopsin in complex with a mini-G(o) sheds light on the principles of G protein selectivity.
  9. Lipids Alter Rhodopsin Function via Ligand-like and Solvent-like Interactions
    Title: Lipids Alter Rhodopsin Function via Ligand-like and Solvent-like Interactions.
  10. Data indicate molecular dynamics simulations and site-directed fluorescence experiments on arrestin-1 interactions with rhodopsin, showing that loops within the C-edge of arrestin function as a membrane anchor.
    Title: C-edge loops of arrestin function as a membrane anchor.
Submit: New GeneRIF Correction See all GeneRIFs (137)

Pathways from PubChem

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Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Markers

Homology

Gene Ontology Provided by RefSeq

Function Evidence Code Pubs
enables G protein-coupled receptor activity IEA
Inferred from Electronic Annotation
more info
 PubMed 
Process Evidence Code Pubs
involved_in G protein-coupled receptor signaling pathway IEA
Inferred from Electronic Annotation
more info
 PubMed 
involved_in phototransduction IEA
Inferred from Electronic Annotation
more info
 PubMed 
involved_in visual perception IEA
Inferred from Electronic Annotation
more info
 PubMed 
Component Evidence Code Pubs
located_in membrane IEA
Inferred from Electronic Annotation
more info
 PubMed 
located_in photoreceptor outer segment IEA
Inferred from Electronic Annotation
more info
 PubMed 

General protein information

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Preferred Names
rhodopsin
Names
rhodopsin (opsin 2, rod pigment) (retinitis pigmentosa 4, autosomal dominant)

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

  1. NM_001014890.2 → NP_001014890.1  rhodopsin

    See identical proteins and their annotated locations for NP_001014890.1

    Status: VALIDATED

    Source sequence(s)
    DAAA02054571
    UniProtKB/Swiss-Prot
    P02699
    Related
    ENSBTAP00000001730.5, ENSBTAT00000001730.7
    Conserved Domains (2) summary
    pfam10413
    Location:3 → 37
    Rhodopsin_N; Amino terminal of the G-protein receptor rhodopsin
    cd15080
    Location:38 → 317
    7tmA_MWS_opsin; medium wave-sensitive opsins, member of the class A family of seven-transmembrane G protein-coupled receptors

RefSeqs of Annotated Genomes: GCF_002263795.3-RS_2023_09

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference ARS-UCD2.0 Primary Assembly

Genomic

  1. NC_037349.1 Reference ARS-UCD2.0 Primary Assembly

    Range
    56225120..56231448 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)
Nucleotide Protein Strain
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P02699.1 GenPept UniProtKB/Swiss-Prot:P02699

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

Other Literature Sources
Molecular Biology Databases
Research Materials
Miscellaneous