P08255 · OPS4_DROME
- ProteinOpsin Rh4
- GeneRh4
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids378 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal.
Miscellaneous
Each Drosophila eye is composed of 800 facets or ommatidia. Each ommatidium contains 8 photoreceptor cells (R1-R8), the R1 to R6 cells are outer cells, while R7 and R8 are inner cells.
Opsin Rh4 is sensitive to UV light.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Cellular Component | plasma membrane | |
Molecular Function | G protein-coupled photoreceptor activity | |
Biological Process | cellular response to light stimulus | |
Biological Process | detection of UV | |
Biological Process | G protein-coupled receptor signaling pathway | |
Biological Process | phototransduction | |
Biological Process | phototransduction, UV | |
Biological Process | visual perception |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameOpsin Rh4
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionP08255
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-53 | Extracellular | ||||
Sequence: MEPLCNASEPPLRPEARSSGNGDLQFLGWNVPPDQIQYIPEHWLTQLEPPASM | ||||||
Transmembrane | 54-78 | Helical; Name=1 | ||||
Sequence: HYMLGVFYIFLFCASTVGNGMVIWI | ||||||
Topological domain | 79-90 | Cytoplasmic | ||||
Sequence: FSTSKSLRTPSN | ||||||
Transmembrane | 91-111 | Helical; Name=2 | ||||
Sequence: MFVLNLAVFDLIMCLKAPIFI | ||||||
Topological domain | 112-127 | Extracellular | ||||
Sequence: YNSFHRGFALGNTWCQ | ||||||
Transmembrane | 128-148 | Helical; Name=3 | ||||
Sequence: IFASIGSYSGIGAGMTNAAIG | ||||||
Topological domain | 149-167 | Cytoplasmic | ||||
Sequence: YDRYNVITKPMNRNMTFTK | ||||||
Transmembrane | 168-192 | Helical; Name=4 | ||||
Sequence: AVIMNIIIWLYCTPWVVLPLTQFWD | ||||||
Topological domain | 193-216 | Extracellular | ||||
Sequence: RFVPEGYLTSCSFDYLSDNFDTRL | ||||||
Transmembrane | 217-244 | Helical; Name=5 | ||||
Sequence: FVGTIFFFSFVCPTLMILYYYSQIVGHV | ||||||
Topological domain | 245-280 | Cytoplasmic | ||||
Sequence: FSHEKALREQAKKMNVESLRSNVDKSKETAEIRIAK | ||||||
Transmembrane | 281-304 | Helical; Name=6 | ||||
Sequence: AAITICFLFFVSWTPYGVMSLIGA | ||||||
Topological domain | 305-312 | Extracellular | ||||
Sequence: FGDKSLLT | ||||||
Transmembrane | 313-337 | Helical; Name=7 | ||||
Sequence: PGATMIPACTCKLVACIDPFVYAIS | ||||||
Topological domain | 338-378 | Cytoplasmic | ||||
Sequence: HPRYRLELQKRCPWLGVNEKSGEISSAQSTTTQEQQQTTAA |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, glycosylation, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000197630 | 1-378 | Opsin Rh4 | |||
Sequence: MEPLCNASEPPLRPEARSSGNGDLQFLGWNVPPDQIQYIPEHWLTQLEPPASMHYMLGVFYIFLFCASTVGNGMVIWIFSTSKSLRTPSNMFVLNLAVFDLIMCLKAPIFIYNSFHRGFALGNTWCQIFASIGSYSGIGAGMTNAAIGYDRYNVITKPMNRNMTFTKAVIMNIIIWLYCTPWVVLPLTQFWDRFVPEGYLTSCSFDYLSDNFDTRLFVGTIFFFSFVCPTLMILYYYSQIVGHVFSHEKALREQAKKMNVESLRSNVDKSKETAEIRIAKAAITICFLFFVSWTPYGVMSLIGAFGDKSLLTPGATMIPACTCKLVACIDPFVYAISHPRYRLELQKRCPWLGVNEKSGEISSAQSTTTQEQQQTTAA | ||||||
Glycosylation | 6 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 126↔203 | |||||
Sequence: CQIFASIGSYSGIGAGMTNAAIGYDRYNVITKPMNRNMTFTKAVIMNIIIWLYCTPWVVLPLTQFWDRFVPEGYLTSC | ||||||
Modified residue | 324 | N6-(retinylidene)lysine | ||||
Sequence: K |
Post-translational modification
Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Length378
- Mass (Da)42,658
- Last updated2000-12-01 v2
- Checksum9A33C1E6F7BD11AD
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 111-112 | in Ref. 1; AAA28856 | ||||
Sequence: Missing | ||||||
Sequence conflict | 120 | in Ref. 1; AAA28856 | ||||
Sequence: A → AIY | ||||||
Sequence conflict | 313 | in Ref. 1; AAA28856 | ||||
Sequence: P → Q |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M17730 EMBL· GenBank· DDBJ | AAA28856.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M17719 EMBL· GenBank· DDBJ | AAA28856.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014296 EMBL· GenBank· DDBJ | AAF49400.1 EMBL· GenBank· DDBJ | Genomic DNA |