P08100 · OPSD_HUMAN
- ProteinRhodopsin
- GeneRHO
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids348 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Photoreceptor required for image-forming vision at low light intensity (PubMed:7846071, PubMed:8107847).
Required for photoreceptor cell viability after birth (PubMed:12566452, PubMed:2215617).
Light-induced isomerization of the chromophore 11-cis-retinal to all-trans-retinal triggers a conformational change that activates signaling via G-proteins (PubMed:26200343, PubMed:28524165, PubMed:28753425, PubMed:8107847).
Subsequent receptor phosphorylation mediates displacement of the bound G-protein alpha subunit by the arrestin SAG and terminates signaling (PubMed:26200343, PubMed:28524165).
Required for photoreceptor cell viability after birth (PubMed:12566452, PubMed:2215617).
Light-induced isomerization of the chromophore 11-cis-retinal to all-trans-retinal triggers a conformational change that activates signaling via G-proteins (PubMed:26200343, PubMed:28524165, PubMed:28753425, PubMed:8107847).
Subsequent receptor phosphorylation mediates displacement of the bound G-protein alpha subunit by the arrestin SAG and terminates signaling (PubMed:26200343, PubMed:28524165).
Features
Showing features for site, binding site.
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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Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameRhodopsin
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP08100
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Multi-pass membrane protein
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.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-36 | Extracellular | ||||
Sequence: MNGTEGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQ | ||||||
Transmembrane | 37-61 | Helical; Name=1 | ||||
Sequence: FSMLAAYMFLLIVLGFPINFLTLYV | ||||||
Topological domain | 62-73 | Cytoplasmic | ||||
Sequence: TVQHKKLRTPLN | ||||||
Transmembrane | 74-96 | Helical; Name=2 | ||||
Sequence: YILLNLAVADLFMVLGGFTSTLY | ||||||
Topological domain | 97-110 | Extracellular | ||||
Sequence: TSLHGYFVFGPTGC | ||||||
Transmembrane | 111-133 | Helical; Name=3 | ||||
Sequence: NLEGFFATLGGEIALWSLVVLAI | ||||||
Topological domain | 134-152 | Cytoplasmic | ||||
Sequence: ERYVVVCKPMSNFRFGENH | ||||||
Transmembrane | 153-173 | Helical; Name=4 | ||||
Sequence: AIMGVAFTWVMALACAAPPLA | ||||||
Topological domain | 174-202 | Extracellular | ||||
Sequence: GWSRYIPEGLQCSCGIDYYTLKPEVNNES | ||||||
Transmembrane | 203-224 | Helical; Name=5 | ||||
Sequence: FVIYMFVVHFTIPMIIIFFCYG | ||||||
Topological domain | 225-252 | Cytoplasmic | ||||
Sequence: QLVFTVKEAAAQQQESATTQKAEKEVTR | ||||||
Transmembrane | 253-274 | Helical; Name=6 | ||||
Sequence: MVIIMVIAFLICWVPYASVAFY | ||||||
Topological domain | 275-284 | Extracellular | ||||
Sequence: IFTHQGSNFG | ||||||
Transmembrane | 285-309 | Helical; Name=7 | ||||
Sequence: PIFMTIPAFFAKSAAIYNPVIYIMM | ||||||
Topological domain | 310-348 | Cytoplasmic | ||||
Sequence: NKQFRNCMLTTICCGKNPLGDDEASATVSKTETSQVAPA |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Retinitis pigmentosa 4 (RP4)
- Note
- DescriptionA 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.
- See alsoMIM:613731
Natural variants in RP4
Night blindness, congenital stationary, autosomal dominant 1 (CSNBAD1)
- Note
- DescriptionA non-progressive retinal disorder characterized by impaired night vision, often associated with nystagmus and myopia.
- See alsoMIM:610445
Natural variants in CSNBAD1
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_004783 | 90 | G>D | in CSNBAD1; constitutive activity in the absence of bound retinal; dbSNP:rs104893790 | |
VAR_004784 | 94 | T>I | in CSNBAD1; dbSNP:rs104893796 | |
VAR_004827 | 292 | A>E | in CSNBAD1; dbSNP:rs104893789 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_004765 | 4 | in RP4 | |||
Sequence: T → K | ||||||
Natural variant | VAR_004766 | 15 | in RP4; dbSNP:rs104893786 | |||
Sequence: N → S | ||||||
Natural variant | VAR_004767 | 17 | in RP4; dbSNP:rs104893769 | |||
Sequence: T → M | ||||||
Natural variant | VAR_004768 | 23 | in RP4; most common variant; impairs protein folding; leads to interaction with EDEM1 followed by degradation by the ERAD system; dbSNP:rs104893768 | |||
Sequence: P → H | ||||||
Natural variant | VAR_004769 | 23 | in RP4; dbSNP:rs104893768 | |||
Sequence: P → L | ||||||
Natural variant | VAR_004770 | 28 | in RP4; dbSNP:rs2108749184 | |||
Sequence: Q → H | ||||||
Natural variant | VAR_004771 | 40 | in RP4 | |||
Sequence: L → R | ||||||
Natural variant | VAR_004772 | 44 | in RP4; dbSNP:rs774336493 | |||
Sequence: M → T | ||||||
Natural variant | VAR_004773 | 45 | in RP4; dbSNP:rs104893770 | |||
Sequence: F → L | ||||||
Natural variant | VAR_004774 | 46 | in RP4; dbSNP:rs2084757073 | |||
Sequence: L → R | ||||||
Natural variant | VAR_004775 | 51 | in dbSNP:rs149079952 | |||
Sequence: G → A | ||||||
Natural variant | VAR_004776 | 51 | in RP4; dbSNP:rs104893792 | |||
Sequence: G → R | ||||||
Natural variant | VAR_004777 | 51 | in RP4; dbSNP:rs149079952 | |||
Sequence: G → V | ||||||
Natural variant | VAR_004778 | 53 | in RP4; dbSNP:rs28933395 | |||
Sequence: P → R | ||||||
Natural variant | VAR_004779 | 58 | in RP4; dbSNP:rs28933394 | |||
Sequence: T → R | ||||||
Natural variant | VAR_004780 | 68-71 | in RP4 | |||
Sequence: Missing | ||||||
Natural variant | VAR_004781 | 87 | in RP4; dbSNP:rs104893771 | |||
Sequence: V → D | ||||||
Natural variant | VAR_004782 | 89 | in RP4; dbSNP:rs104893772 | |||
Sequence: G → D | ||||||
Natural variant | VAR_004783 | 90 | in CSNBAD1; constitutive activity in the absence of bound retinal; dbSNP:rs104893790 | |||
Sequence: G → D | ||||||
Natural variant | VAR_004784 | 94 | in CSNBAD1; dbSNP:rs104893796 | |||
Sequence: T → I | ||||||
Natural variant | VAR_004785 | 104 | found in patients with pathologic myopia; uncertain significance; dbSNP:rs144317206 | |||
Sequence: V → I | ||||||
Natural variant | VAR_004786 | 106 | in RP4; dbSNP:rs104893773 | |||
Sequence: G → R | ||||||
Natural variant | VAR_004787 | 106 | in RP4; dbSNP:rs104893773 | |||
Sequence: G → W | ||||||
Natural variant | VAR_004788 | 109 | in RP4; dbSNP:rs1415160298 | |||
Sequence: G → R | ||||||
Natural variant | VAR_004789 | 110 | in RP4 | |||
Sequence: C → F | ||||||
Natural variant | VAR_004790 | 110 | in RP4; dbSNP:rs104893787 | |||
Sequence: C → Y | ||||||
Mutagenesis | 113 | Induces a conformation change that promotes interaction with GRK1 and SAG; when associated with Y-257. | ||||
Sequence: E → Q | ||||||
Natural variant | VAR_004791 | 114 | in RP4; dbSNP:rs104893788 | |||
Sequence: G → D | ||||||
Natural variant | VAR_004792 | 125 | in RP4 | |||
Sequence: L → R | ||||||
Natural variant | VAR_004793 | 127 | in RP4; dbSNP:rs2108749921 | |||
Sequence: S → F | ||||||
Natural variant | VAR_004794 | 131 | in RP4; dbSNP:rs1553781140 | |||
Sequence: L → P | ||||||
Natural variant | VAR_004795 | 135 | in RP4; dbSNP:rs104893775 | |||
Sequence: R → G | ||||||
Natural variant | VAR_004796 | 135 | in RP4; dbSNP:rs104893774 | |||
Sequence: R → L | ||||||
Natural variant | VAR_004797 | 135 | in RP4; dbSNP:rs104893775 | |||
Sequence: R → W | ||||||
Natural variant | VAR_004798 | 140 | in RP4; dbSNP:rs2084775122 | |||
Sequence: C → S | ||||||
Natural variant | VAR_004799 | 150 | in RP4; autosomal recessive; dbSNP:rs104893791 | |||
Sequence: E → K | ||||||
Natural variant | VAR_004800 | 164 | in RP4; dbSNP:rs104893793 | |||
Sequence: A → E | ||||||
Natural variant | VAR_004801 | 164 | in RP4; dbSNP:rs104893793 | |||
Sequence: A → V | ||||||
Natural variant | VAR_004802 | 167 | in RP4 | |||
Sequence: C → R | ||||||
Natural variant | VAR_004803 | 171 | in RP4; dbSNP:rs2084776162 | |||
Sequence: P → L | ||||||
Natural variant | VAR_004804 | 171 | in RP4; dbSNP:rs2084776162 | |||
Sequence: P → Q | ||||||
Natural variant | VAR_004805 | 171 | in RP4; dbSNP:rs104893794 | |||
Sequence: P → S | ||||||
Natural variant | VAR_004806 | 178 | in RP4; dbSNP:rs104893776 | |||
Sequence: Y → C | ||||||
Natural variant | VAR_004807 | 178 | in RP4 | |||
Sequence: Y → N | ||||||
Natural variant | VAR_068359 | 180 | in RP4; dbSNP:rs1560046837 | |||
Sequence: P → S | ||||||
Natural variant | VAR_004808 | 181 | in RP4; dbSNP:rs775557680 | |||
Sequence: E → K | ||||||
Natural variant | VAR_004809 | 182 | in RP4; dbSNP:rs104893780 | |||
Sequence: G → S | ||||||
Natural variant | VAR_004810 | 186 | in RP4 | |||
Sequence: S → P | ||||||
Natural variant | VAR_004811 | 188 | in RP4; dbSNP:rs1424131846 | |||
Sequence: G → E | ||||||
Natural variant | VAR_004812 | 188 | in RP4; dbSNP:rs527236100 | |||
Sequence: G → R | ||||||
Natural variant | VAR_004814 | 190 | in RP4; dbSNP:rs104893777 | |||
Sequence: D → G | ||||||
Natural variant | VAR_004813 | 190 | in RP4; dbSNP:rs104893779 | |||
Sequence: D → N | ||||||
Natural variant | VAR_004815 | 190 | in RP4; dbSNP:rs104893779 | |||
Sequence: D → Y | ||||||
Natural variant | VAR_004816 | 207 | in RP4; dbSNP:rs104893782 | |||
Sequence: M → R | ||||||
Natural variant | VAR_004817 | 209 | found in a patient with retinitis pigmentosa; uncertain significance; dbSNP:rs567288669 | |||
Sequence: V → M | ||||||
Natural variant | VAR_004818 | 211 | in RP4; dbSNP:rs28933993 | |||
Sequence: H → P | ||||||
Natural variant | VAR_004819 | 211 | in RP4; dbSNP:rs28933993 | |||
Sequence: H → R | ||||||
Natural variant | VAR_068360 | 214 | in RP4 | |||
Sequence: I → N | ||||||
Natural variant | VAR_004820 | 216 | in RP4; dbSNP:rs984572250 | |||
Sequence: M → K | ||||||
Natural variant | VAR_004821 | 220 | in RP4; dbSNP:rs766161322 | |||
Sequence: F → C | ||||||
Natural variant | VAR_004822 | 222 | in RP4 | |||
Sequence: C → R | ||||||
Natural variant | VAR_004823 | 255 | in RP4 | |||
Sequence: Missing | ||||||
Mutagenesis | 257 | Induces a conformation change that promotes interaction with GRK1 and SAG; when associated with Q-113. | ||||
Sequence: M → Y | ||||||
Natural variant | VAR_004824 | 264 | in RP4 | |||
Sequence: Missing | ||||||
Natural variant | VAR_004825 | 267 | in RP4; dbSNP:rs104893781 | |||
Sequence: P → L | ||||||
Natural variant | VAR_004826 | 267 | in RP4 | |||
Sequence: P → R | ||||||
Natural variant | VAR_004827 | 292 | in CSNBAD1; dbSNP:rs104893789 | |||
Sequence: A → E | ||||||
Natural variant | VAR_004828 | 296 | in RP4; dbSNP:rs29001653 | |||
Sequence: K → E | ||||||
Natural variant | VAR_004829 | 297 | in RP4; dbSNP:rs142285818 | |||
Sequence: S → R | ||||||
Mutagenesis | 336-338 | Loss of phosphorylation sites and decreased interaction with SAG; when associated with A-343. | ||||
Sequence: TVS → AVA | ||||||
Mutagenesis | 336-340 | Loss of phosphorylation sites and decreased interaction with SAG. | ||||
Sequence: TVSKT → AVAKA | ||||||
Natural variant | VAR_004830 | 342 | in RP4; dbSNP:rs183318466 | |||
Sequence: T → M | ||||||
Mutagenesis | 343 | Loss of phosphorylation sites and decreased interaction with SAG; when associated with 336-A--A-338. | ||||
Sequence: S → A | ||||||
Natural variant | VAR_004831 | 345 | in RP4; dbSNP:rs104893795 | |||
Sequence: V → L | ||||||
Natural variant | VAR_004832 | 345 | in RP4; dbSNP:rs104893795 | |||
Sequence: V → M | ||||||
Natural variant | VAR_004833 | 347 | in RP4 | |||
Sequence: P → A | ||||||
Natural variant | VAR_004834 | 347 | in RP4; common variant; dbSNP:rs29001566 | |||
Sequence: P → L | ||||||
Natural variant | VAR_004835 | 347 | in RP4; dbSNP:rs29001566 | |||
Sequence: P → Q | ||||||
Natural variant | VAR_004836 | 347 | in RP4; dbSNP:rs29001566 | |||
Sequence: P → R | ||||||
Natural variant | VAR_004837 | 347 | in RP4; dbSNP:rs29001637 | |||
Sequence: P → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 582 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue, chain, glycosylation, disulfide bond, lipidation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000197677 | 1-348 | Rhodopsin | |||
Sequence: MNGTEGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQFSMLAAYMFLLIVLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADLFMVLGGFTSTLYTSLHGYFVFGPTGCNLEGFFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMALACAAPPLAGWSRYIPEGLQCSCGIDYYTLKPEVNNESFVIYMFVVHFTIPMIIIFFCYGQLVFTVKEAAAQQQESATTQKAEKEVTRMVIIMVIAFLICWVPYASVAFYIFTHQGSNFGPIFMTIPAFFAKSAAIYNPVIYIMMNKQFRNCMLTTICCGKNPLGDDEASATVSKTETSQVAPA | ||||||
Glycosylation | 2 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 15 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 110↔187 | |||||
Sequence: CNLEGFFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMALACAAPPLAGWSRYIPEGLQCSC | ||||||
Modified residue | 296 | N6-(retinylidene)lysine | ||||
Sequence: K | ||||||
Lipidation | 322 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Lipidation | 323 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Modified residue | 334 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 336 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 338 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 340 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 342 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 343 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
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).
After activation by light, phosphorylated by GRK1 (in vitro) (PubMed:28524165).
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 (PubMed:12566452).
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Homodimer (By similarity).
May form a complex composed of RHO, GRK1 and RCVRN in a Ca2+-dependent manner; RCVRN prevents the interaction between GRK1 and RHO (By similarity).
Interacts with GRK1 (PubMed:28524165).
Interacts (phosphorylated form) with SAG (PubMed:26200343, PubMed:28524165, PubMed:28753425).
Interacts with GNAT1 (PubMed:26200343).
Interacts with GNAT3. SAG and G-proteins compete for a common binding site (PubMed:26200343).
Interacts with PRCD; the interaction promotes PRCD stability (By similarity).
Forms a complex with ASAP1 and ARF4. Forms a complex with ASAP1, RAB11A, Rabin8/RAB3IP, ARF4 and RAB11FIP3; the complex regulates Golgi-to-cilia rhodopsin/RHO transport in photoreceptors (By similarity).
May form a complex composed of RHO, GRK1 and RCVRN in a Ca2+-dependent manner; RCVRN prevents the interaction between GRK1 and RHO (By similarity).
Interacts with GRK1 (PubMed:28524165).
Interacts (phosphorylated form) with SAG (PubMed:26200343, PubMed:28524165, PubMed:28753425).
Interacts with GNAT1 (PubMed:26200343).
Interacts with GNAT3. SAG and G-proteins compete for a common binding site (PubMed:26200343).
Interacts with PRCD; the interaction promotes PRCD stability (By similarity).
Forms a complex with ASAP1 and ARF4. Forms a complex with ASAP1, RAB11A, Rabin8/RAB3IP, ARF4 and RAB11FIP3; the complex regulates Golgi-to-cilia rhodopsin/RHO transport in photoreceptors (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P08100 | CD79A P11912 | 3 | EBI-1394177, EBI-7797864 | |
BINARY | P08100 | ZFYVE9 O95405 | 2 | EBI-1394177, EBI-296817 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for motif, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 134-136 | 'Ionic lock' involved in activated form stabilization | ||||
Sequence: ERY | ||||||
Region | 330-348 | Interaction with SAG | ||||
Sequence: DDEASATVSKTETSQVAPA |
Sequence similarities
Belongs to the G-protein coupled receptor 1 family. Opsin subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Protein family/group databases
Sequence
- Sequence statusComplete
- Length348
- Mass (Da)38,893
- Last updated1988-08-01 v1
- Checksum6F4F6FCBA34265B2
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U49742 EMBL· GenBank· DDBJ | AAC31763.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB065668 EMBL· GenBank· DDBJ | BAC05894.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BX537381 EMBL· GenBank· DDBJ | CAD97623.1 EMBL· GenBank· DDBJ | mRNA | ||
BC112104 EMBL· GenBank· DDBJ | AAI12105.1 EMBL· GenBank· DDBJ | mRNA | ||
BC112106 EMBL· GenBank· DDBJ | AAI12107.1 EMBL· GenBank· DDBJ | mRNA | ||
U16824 EMBL· GenBank· DDBJ | AAA97436.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
S81166 EMBL· GenBank· DDBJ | AAB35906.1 EMBL· GenBank· DDBJ | Genomic DNA |