P21457 · RECO_BOVIN

  • Protein
    Recoverin
  • Gene
    RCVRN
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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).

Features

Showing features for binding site, site.

120220406080100120140160180200
TypeIDPosition(s)Description
Binding site74Ca2+ 1 (UniProtKB | ChEBI); low affinity
Binding site76Ca2+ 1 (UniProtKB | ChEBI); low affinity
Binding site78Ca2+ 1 (UniProtKB | ChEBI); low affinity
Binding site80Ca2+ 1 (UniProtKB | ChEBI); low affinity
Binding site85Ca2+ 1 (UniProtKB | ChEBI); low affinity
Binding site110Ca2+ 2 (UniProtKB | ChEBI); high affinity
Binding site112Ca2+ 2 (UniProtKB | ChEBI); high affinity
Binding site114Ca2+ 2 (UniProtKB | ChEBI); high affinity
Binding site116Ca2+ 2 (UniProtKB | ChEBI); high affinity
Binding site121Ca2+ 2 (UniProtKB | ChEBI); high affinity
Site192Interaction with GRK1

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentmembrane
Cellular Componentperikaryon
Cellular Componentphotoreceptor inner segment
Cellular Componentphotoreceptor outer segment
Molecular Functioncalcium ion binding
Biological Processphototransduction
Biological Processregulation of calcium ion transport
Biological Processvisual perception

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Recoverin
  • Alternative names
    • p26

Gene names

    • Name
      RCVRN
    • Synonyms
      RCV1

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos

Accessions

  • Primary accession
    P21457

Proteomes

Organism-specific databases

Subcellular Location

Photoreceptor outer segment membrane
; Lipid-anchor
Perikaryon
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).

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis39Increases calcium binding affinity at EF-hand 3 domain; induces co-operative calcium binding in non-myristoylated protein.
Mutagenesis39Reduces binding affinity for calcium at both EF-hand 2 and EF-hand 3 domains. Abolishes interaction with GRK1.
Mutagenesis40Reduces calcium binding affinity.
Mutagenesis85Abolishes binding of calcium to EF-hand 2 domain. Abolishes calcium-dependent inhibition of GRK1.
Mutagenesis153No effect on calcium binding to EF-hand 2 and EF-hand 3 domains. No effect on interaction with GRK1.
Mutagenesis185-202Decrease in thermostability.
Mutagenesis187-202Decrease in thermostability.
Mutagenesis188-202Decrease in thermostability.
Mutagenesis189-202Reduces calcium binding affinity. Reduces interaction with GRK1. Reduces inhibition of GRK1 activity.
Mutagenesis190Reduces interaction with GRK1.
Mutagenesis191Reduces inhibition of GRK1 activity.
Mutagenesis191-202Reduces calcium binding affinity to EF-hand 3 domain. Reduces interaction with GRK1.
Mutagenesis192Reduces interaction with GRK1. Reduces inhibition of GRK1 activity.
Mutagenesis193Reduces interaction with GRK1.
Mutagenesis193-202Reduces calcium binding affinity. Reduces interaction with GRK1.
Mutagenesis197-202Reduces interaction with GRK1.

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.

Go to variant viewer

PTM/Processing

Features

Showing features for initiator methionine, lipidation, chain, modified residue, disulfide bond.

TypeIDPosition(s)Description
Initiator methionine1Removed
Lipidation2N-myristoyl glycine
ChainPRO_00000737582-202Recoverin
Modified residue39Cysteine sulfenic acid (-SOH)
Disulfide bond39Interchain, redox-active

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).
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

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in the retina (at protein level) (PubMed:1672047, PubMed:1672637, PubMed:25772009).
Expressed in the pineal gland (at protein level) (PubMed:1672047).

Gene expression 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).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P21457GRK1 P283272EBI-8592784, EBI-7865560

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain24-59EF-hand 1
Domain61-96EF-hand 2
Domain97-132EF-hand 3
Domain147-182EF-hand 4
Region189-192Interaction with GRK1
Region191-202Modulates EF-hand 3 domain calcium binding affinity

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).

Sequence similarities

Belongs to the recoverin family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    202
  • Mass (Da)
    23,333
  • Last updated
    2007-01-23 v3
  • Checksum
    75504DEBE8288BA8
MGNSKSGALSKEILEELQLNTKFTEEELSSWYQSFLKECPSGRITRQEFQTIYSKFFPEADPKAYAQHVFRSFDANSDGTLDFKEYVIALHMTSAGKTNQKLEWAFSLYDVDGNGTISKNEVLEIVTAIFKMISPEDTKHLPEDENTPEKRAEKIWGFFGKKDDDKLTEKEFIEGTLANKEILRLIQFEPQKVKEKLKEKKL

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict19in Ref. 4; AA sequence
Sequence conflict21in Ref. 4; AA sequence

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M95858
EMBL· GenBank· DDBJ
AAB59256.1
EMBL· GenBank· DDBJ
mRNA
X63322
EMBL· GenBank· DDBJ
CAA44928.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp