P21457 · RECO_BOVIN
- ProteinRecoverin
- GeneRCVRN
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids202 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Acts as a calcium sensor and regulates phototransduction of cone and rod photoreceptor cells (PubMed:1672047, PubMed:1672637).
Modulates light sensitivity of cone photoreceptor in dark and dim conditions (By similarity).
In response to high Ca2+ levels induced by low light levels, prolongs RHO/rhodopsin activation in rod photoreceptor cells by binding to and inhibiting GRK1-mediated phosphorylation of RHO/rhodopsin (PubMed:12686556, PubMed:16675451, PubMed:1672047, PubMed:1672637, PubMed:17015448, PubMed:21299498, PubMed:8392055).
Plays a role in scotopic vision/enhances vision in dim light by enhancing signal transfer between rod photoreceptors and rod bipolar cells (By similarity).
Improves rod photoreceptor sensitivity in dim light and mediates response of rod photoreceptors to facilitate detection of change and motion in bright light (By similarity).
Modulates light sensitivity of cone photoreceptor in dark and dim conditions (By similarity).
In response to high Ca2+ levels induced by low light levels, prolongs RHO/rhodopsin activation in rod photoreceptor cells by binding to and inhibiting GRK1-mediated phosphorylation of RHO/rhodopsin (PubMed:12686556, PubMed:16675451, PubMed:1672047, PubMed:1672637, PubMed:17015448, PubMed:21299498, PubMed:8392055).
Plays a role in scotopic vision/enhances vision in dim light by enhancing signal transfer between rod photoreceptors and rod bipolar cells (By similarity).
Improves rod photoreceptor sensitivity in dim light and mediates response of rod photoreceptors to facilitate detection of change and motion in bright light (By similarity).
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 74 | Ca2+ 1 (UniProtKB | ChEBI); low affinity | ||||
Sequence: D | ||||||
Binding site | 76 | Ca2+ 1 (UniProtKB | ChEBI); low affinity | ||||
Sequence: N | ||||||
Binding site | 78 | Ca2+ 1 (UniProtKB | ChEBI); low affinity | ||||
Sequence: D | ||||||
Binding site | 80 | Ca2+ 1 (UniProtKB | ChEBI); low affinity | ||||
Sequence: T | ||||||
Binding site | 85 | Ca2+ 1 (UniProtKB | ChEBI); low affinity | ||||
Sequence: E | ||||||
Binding site | 110 | Ca2+ 2 (UniProtKB | ChEBI); high affinity | ||||
Sequence: D | ||||||
Binding site | 112 | Ca2+ 2 (UniProtKB | ChEBI); high affinity | ||||
Sequence: D | ||||||
Binding site | 114 | Ca2+ 2 (UniProtKB | ChEBI); high affinity | ||||
Sequence: N | ||||||
Binding site | 116 | Ca2+ 2 (UniProtKB | ChEBI); high affinity | ||||
Sequence: T | ||||||
Binding site | 121 | Ca2+ 2 (UniProtKB | ChEBI); high affinity | ||||
Sequence: E | ||||||
Site | 192 | Interaction with GRK1 | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | membrane | |
Cellular Component | perikaryon | |
Cellular Component | photoreceptor inner segment | |
Cellular Component | photoreceptor outer segment | |
Molecular Function | calcium ion binding | |
Biological Process | phototransduction | |
Biological Process | regulation of calcium ion transport | |
Biological Process | visual perception |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRecoverin
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionP21457
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Photoreceptor outer segment membrane ; Lipid-anchor
Note: Primarily expressed in the inner segments of light-adapted rod photoreceptors, approximately 10% of which translocates from photoreceptor outer segments upon light stimulation (By similarity).
Targeting of myristoylated protein to rod photoreceptor outer segments is calcium dependent (PubMed:17015448).
Targeting of myristoylated protein to rod photoreceptor outer segments is calcium dependent (PubMed:17015448).
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 39 | Increases calcium binding affinity at EF-hand 3 domain; induces co-operative calcium binding in non-myristoylated protein. | ||||
Sequence: C → A | ||||||
Mutagenesis | 39 | Reduces binding affinity for calcium at both EF-hand 2 and EF-hand 3 domains. Abolishes interaction with GRK1. | ||||
Sequence: C → D | ||||||
Mutagenesis | 40 | Reduces calcium binding affinity. | ||||
Sequence: P → A | ||||||
Mutagenesis | 85 | Abolishes binding of calcium to EF-hand 2 domain. Abolishes calcium-dependent inhibition of GRK1. | ||||
Sequence: E → Q | ||||||
Mutagenesis | 153 | No effect on calcium binding to EF-hand 2 and EF-hand 3 domains. No effect on interaction with GRK1. | ||||
Sequence: E → A | ||||||
Mutagenesis | 185-202 | Decrease in thermostability. | ||||
Sequence: Missing | ||||||
Mutagenesis | 187-202 | Decrease in thermostability. | ||||
Sequence: Missing | ||||||
Mutagenesis | 188-202 | Decrease in thermostability. | ||||
Sequence: Missing | ||||||
Mutagenesis | 189-202 | Reduces calcium binding affinity. Reduces interaction with GRK1. Reduces inhibition of GRK1 activity. | ||||
Sequence: Missing | ||||||
Mutagenesis | 190 | Reduces interaction with GRK1. | ||||
Sequence: P → G | ||||||
Mutagenesis | 191 | Reduces inhibition of GRK1 activity. | ||||
Sequence: Q → A | ||||||
Mutagenesis | 191-202 | Reduces calcium binding affinity to EF-hand 3 domain. Reduces interaction with GRK1. | ||||
Sequence: Missing | ||||||
Mutagenesis | 192 | Reduces interaction with GRK1. Reduces inhibition of GRK1 activity. | ||||
Sequence: K → A | ||||||
Mutagenesis | 193 | Reduces interaction with GRK1. | ||||
Sequence: V → G | ||||||
Mutagenesis | 193-202 | Reduces calcium binding affinity. Reduces interaction with GRK1. | ||||
Sequence: Missing | ||||||
Mutagenesis | 197-202 | Reduces interaction with GRK1. | ||||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 10 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for initiator methionine, lipidation, chain, modified residue, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Lipidation | 2 | N-myristoyl glycine | ||||
Sequence: G | ||||||
Chain | PRO_0000073758 | 2-202 | Recoverin | |||
Sequence: GNSKSGALSKEILEELQLNTKFTEEELSSWYQSFLKECPSGRITRQEFQTIYSKFFPEADPKAYAQHVFRSFDANSDGTLDFKEYVIALHMTSAGKTNQKLEWAFSLYDVDGNGTISKNEVLEIVTAIFKMISPEDTKHLPEDENTPEKRAEKIWGFFGKKDDDKLTEKEFIEGTLANKEILRLIQFEPQKVKEKLKEKKL | ||||||
Modified residue | 39 | Cysteine sulfenic acid (-SOH) | ||||
Sequence: C | ||||||
Disulfide bond | 39 | Interchain, redox-active | ||||
Sequence: C |
Post-translational modification
The N-terminal glycine is linked to one of four different types of acyl groups. The most abundant is myristoleate (14:1), but 14:0, 14:2, and 12:0 acyl residues are also present (PubMed:11980481, PubMed:12686556, PubMed:1386601, PubMed:1454850).
The Ca2+ induced exposure of the myristoyl group, known as the calcium-myristoyl switch, promotes RCVRN binding to the photoreceptor cell membranes only when intracellular Ca2+ concentration is high (PubMed:7630423).
The Ca2+ induced exposure of the myristoyl group, known as the calcium-myristoyl switch, promotes RCVRN binding to the photoreceptor cell membranes only when intracellular Ca2+ concentration is high (PubMed:7630423).
Oxidation on Cys-39 occurs in response to prolonged intense illumination and results in the formation of disulfide homodimers, and to a lesser extent disulfide-linked heterodimers.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Homodimer; disulfide-linked (PubMed:25772009).
Homodimerization is caused by prolonged intense illumination (PubMed:25772009).
May form a complex composed of RHO, GRK1 and RCVRN in a Ca2+-dependent manner; RCVRN prevents the interaction between GRK1 and RHO (PubMed:17020884).
Interacts (via C-terminus) with GRK1 (via N-terminus); the interaction is Ca2+-dependent (PubMed:16675451, PubMed:21299498, PubMed:24189072, PubMed:26584024).
Homodimerization is caused by prolonged intense illumination (PubMed:25772009).
May form a complex composed of RHO, GRK1 and RCVRN in a Ca2+-dependent manner; RCVRN prevents the interaction between GRK1 and RHO (PubMed:17020884).
Interacts (via C-terminus) with GRK1 (via N-terminus); the interaction is Ca2+-dependent (PubMed:16675451, PubMed:21299498, PubMed:24189072, PubMed:26584024).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P21457 | GRK1 P28327 | 2 | EBI-8592784, EBI-7865560 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 24-59 | EF-hand 1 | ||||
Sequence: TEEELSSWYQSFLKECPSGRITRQEFQTIYSKFFPE | ||||||
Domain | 61-96 | EF-hand 2 | ||||
Sequence: DPKAYAQHVFRSFDANSDGTLDFKEYVIALHMTSAG | ||||||
Domain | 97-132 | EF-hand 3 | ||||
Sequence: KTNQKLEWAFSLYDVDGNGTISKNEVLEIVTAIFKM | ||||||
Domain | 147-182 | EF-hand 4 | ||||
Sequence: TPEKRAEKIWGFFGKKDDDKLTEKEFIEGTLANKEI | ||||||
Region | 189-192 | Interaction with GRK1 | ||||
Sequence: EPQK | ||||||
Region | 191-202 | Modulates EF-hand 3 domain calcium binding affinity | ||||
Sequence: QKVKEKLKEKKL |
Domain
EF-hand 2 and EF-hand 3 domains are the low-affinity and the high-affinity calcium binding sites, respectively (PubMed:11980481, PubMed:26584024).
EF-hand 1 and EF-hand 4 domains do not bind calcium due to substitutions that disrupt their respective Ca2+ binding loops (Probable). The cooperative binding of calcium to the EF-hand 2 domain following EF-hand 3 domain calcium binding requires myristoylation (PubMed:12686556, PubMed:24189072).
Calcium binding to the 2 EF-hand domains induces exposure of the myristoyl group through a protein conformation change, this process known as the calcium-myristoyl switch facilitates binding to photoreceptor cell membranes (PubMed:7630423).
EF-hand 1 and EF-hand 4 domains do not bind calcium due to substitutions that disrupt their respective Ca2+ binding loops (Probable). The cooperative binding of calcium to the EF-hand 2 domain following EF-hand 3 domain calcium binding requires myristoylation (PubMed:12686556, PubMed:24189072).
Calcium binding to the 2 EF-hand domains induces exposure of the myristoyl group through a protein conformation change, this process known as the calcium-myristoyl switch facilitates binding to photoreceptor cell membranes (PubMed:7630423).
Sequence similarities
Belongs to the recoverin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length202
- Mass (Da)23,333
- Last updated2007-01-23 v3
- Checksum75504DEBE8288BA8
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 19 | in Ref. 4; AA sequence | ||||
Sequence: L → Q | ||||||
Sequence conflict | 21 | in Ref. 4; AA sequence | ||||
Sequence: T → N |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M95858 EMBL· GenBank· DDBJ | AAB59256.1 EMBL· GenBank· DDBJ | mRNA | ||
X63322 EMBL· GenBank· DDBJ | CAA44928.1 EMBL· GenBank· DDBJ | mRNA |