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Entry version 165 (22 Apr 2020)
Sequence version 3 (23 Jan 2007)
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Protein

Recoverin

Gene

RCVRN

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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:1672047, PubMed:1672637, PubMed:8392055, PubMed:16675451, PubMed:21299498, PubMed:12686556, PubMed:17015448). 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).By similarity7 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi74Calcium 1Combined sources1 Publication1
Metal bindingi76Calcium 1Combined sources1 Publication1
Metal bindingi78Calcium 1Combined sources1 Publication1
Metal bindingi80Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi85Calcium 1Combined sources1 Publication1
Metal bindingi110Calcium 2Combined sources8 Publications1
Metal bindingi112Calcium 2Combined sources8 Publications1
Metal bindingi114Calcium 2Combined sources7 Publications1
Metal bindingi116Calcium 2; via carbonyl oxygenCombined sources8 Publications1
Metal bindingi121Calcium 2Combined sources7 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) of the calcium-binding region(s) within the protein. One common calcium-binding motif is the EF-hand, but other calcium-binding motifs also exist.<p><a href='/help/ca_bind' target='_top'>More...</a></p>Calcium bindingi74 – 851; low affinity1 PublicationAdd BLAST12
Calcium bindingi110 – 1212; high affinity1 PublicationAdd BLAST12

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processSensory transduction, Vision
LigandCalcium, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-BTA-2514859 Inactivation, recovery and regulation of the phototransduction cascade

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Recoverin
Alternative name(s):
p26
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:RCVRN
Synonyms:RCV1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBos taurus (Bovine)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9913 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaArtiodactylaRuminantiaPecoraBovidaeBovinaeBos
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000009136 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 19

Organism-specific databases

Vertebrate Gene Nomenclature Database

More...
VGNCi
VGNC:33838 RCVRN

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell projection, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi39C → A: Increases calcium binding affinity at EF-hand 3 domain; induces co-operative calcium binding in non-myristoylated protein. 1 Publication1
Mutagenesisi39C → D: Reduces binding affinity for calcium at both EF-hand 2 and EF-hand 3 domains. Abolishes interaction with GRK1. 1 Publication1
Mutagenesisi40P → A: Reduces calcium binding affinity. 1 Publication1
Mutagenesisi85E → Q: Abolishes binding of calcium to EF-hand 2 domain. Abolishes calcium-dependent inhibition of GRK1. 2 Publications1
Mutagenesisi153E → A: No effect on calcium binding to EF-hand 2 and EF-hand 3 domains. No effect on interaction with GRK1. 1 Publication1
Mutagenesisi185 – 202Missing : Decrease in thermostability. 1 PublicationAdd BLAST18
Mutagenesisi187 – 202Missing : Decrease in thermostability. 1 PublicationAdd BLAST16
Mutagenesisi188 – 202Missing : Decrease in thermostability. 1 PublicationAdd BLAST15
Mutagenesisi189 – 202Missing : Reduces calcium binding affinity. Reduces interaction with GRK1. Reduces inhibition of GRK1 activity. 1 PublicationAdd BLAST14
Mutagenesisi190P → G: Reduces interaction with GRK1. 1 Publication1
Mutagenesisi191 – 202Missing : Reduces calcium binding affinity to EF-hand 3 domain. Reduces interaction with GRK1. 2 PublicationsAdd BLAST12
Mutagenesisi191Q → A: Reduces inhibition of GRK1 activity. 1 Publication1
Mutagenesisi192K → A: Reduces interaction with GRK1. Reduces inhibition of GRK1 activity. 1 Publication1
Mutagenesisi193 – 202Missing : Reduces calcium binding affinity. Reduces interaction with GRK1. 1 Publication10
Mutagenesisi193V → G: Reduces interaction with GRK1. 1 Publication1
Mutagenesisi197 – 202Missing : Reduces interaction with GRK1. 1 Publication6

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved5 Publications
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000737582 – 202RecoverinAdd BLAST201

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi2N-myristoyl glycine3 Publications1
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei39Cysteine sulfenic acid (-SOH)2 Publications1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi39Interchain, redox-active1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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:1386601, PubMed:1454850, PubMed:11980481, PubMed:12686556). 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).5 Publications
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.1 Publication

Keywords - PTMi

Disulfide bond, Lipoprotein, Myristate, Oxidation

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P21457

PRoteomics IDEntifications database

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PRIDEi
P21457

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P21457

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in the retina (at protein level) (PubMed:1672047, PubMed:1672637, PubMed:25772009). Expressed in the pineal gland (at protein level) (PubMed:1672047).3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSBTAG00000025088 Expressed in testis and 4 other tissues

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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).

6 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei192Interaction with GRK11 Publication1

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
P21457

Protein interaction database and analysis system

More...
IntActi
P21457, 4 interactors

Molecular INTeraction database

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MINTi
P21457

STRING: functional protein association networks

More...
STRINGi
9913.ENSBTAP00000034949

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1202
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P21457

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P21457

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini24 – 59EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini61 – 96EF-hand 2PROSITE-ProRule annotationAdd BLAST36
Domaini97 – 132EF-hand 3PROSITE-ProRule annotationAdd BLAST36
Domaini147 – 182EF-hand 4PROSITE-ProRule annotationAdd BLAST36

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni189 – 192Interaction with GRK11 Publication4
Regioni191 – 202Modulates EF-hand 3 domain calcium binding affinity1 PublicationAdd BLAST12

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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).2 Publications5 Publications

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the recoverin family.Curated

Keywords - Domaini

Redox-active center, Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0044 Eukaryota
COG5126 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000159441

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_072366_1_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P21457

KEGG Orthology (KO)

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KOi
K13764

Identification of Orthologs from Complete Genome Data

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OMAi
TWYQSFL

Database of Orthologous Groups

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OrthoDBi
1271942at2759

TreeFam database of animal gene trees

More...
TreeFami
TF300009

Family and domain databases

Conserved Domains Database

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CDDi
cd00051 EFh, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011992 EF-hand-dom_pair
IPR018247 EF_Hand_1_Ca_BS
IPR002048 EF_hand_dom
IPR028846 Recoverin

The PANTHER Classification System

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PANTHERi
PTHR23055 PTHR23055, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF13499 EF-hand_7, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00054 EFh, 2 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47473 SSF47473, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00018 EF_HAND_1, 2 hits
PS50222 EF_HAND_2, 4 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P21457-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGNSKSGALS KEILEELQLN TKFTEEELSS WYQSFLKECP SGRITRQEFQ
60 70 80 90 100
TIYSKFFPEA DPKAYAQHVF RSFDANSDGT LDFKEYVIAL HMTSAGKTNQ
110 120 130 140 150
KLEWAFSLYD VDGNGTISKN EVLEIVTAIF KMISPEDTKH LPEDENTPEK
160 170 180 190 200
RAEKIWGFFG KKDDDKLTEK EFIEGTLANK EILRLIQFEP QKVKEKLKEK

KL
Length:202
Mass (Da):23,333
Last modified:January 23, 2007 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i75504DEBE8288BA8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti19L → Q AA sequence (PubMed:1672637).Curated1
Sequence conflicti21T → N AA sequence (PubMed:1672637).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M95858 mRNA Translation: AAB59256.1
X63322 mRNA Translation: CAA44928.1

Protein sequence database of the Protein Information Resource

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PIRi
A46129

NCBI Reference Sequences

More...
RefSeqi
NP_776590.1, NM_174165.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSBTAT00000035069; ENSBTAP00000034949; ENSBTAG00000025088

Database of genes from NCBI RefSeq genomes

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GeneIDi
281447

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bta:281447

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95858 mRNA Translation: AAB59256.1
X63322 mRNA Translation: CAA44928.1
PIRiA46129
RefSeqiNP_776590.1, NM_174165.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IKUNMR-A2-202[»]
1JSANMR-A2-202[»]
1LA3NMR-A2-202[»]
1OMRX-ray1.50A2-202[»]
1OMVX-ray1.90A2-202[»]
1RECX-ray1.90A2-202[»]
2HETX-ray3.00A/B/C/D2-190[»]
2I94NMR-A1-202[»]
4M2OX-ray1.50A2-197[»]
4M2PX-ray1.45A2-202[»]
4M2QX-ray1.90A2-202[»]
4MLWX-ray1.45A2-202[»]
4YI8X-ray1.20A2-202[»]
4YI9X-ray1.35A2-202[»]
SMRiP21457
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

ELMiP21457
IntActiP21457, 4 interactors
MINTiP21457
STRINGi9913.ENSBTAP00000034949

PTM databases

iPTMnetiP21457

Proteomic databases

PaxDbiP21457
PRIDEiP21457

Genome annotation databases

EnsembliENSBTAT00000035069; ENSBTAP00000034949; ENSBTAG00000025088
GeneIDi281447
KEGGibta:281447

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
5957
VGNCiVGNC:33838 RCVRN

Phylogenomic databases

eggNOGiKOG0044 Eukaryota
COG5126 LUCA
GeneTreeiENSGT00940000159441
HOGENOMiCLU_072366_1_0_1
InParanoidiP21457
KOiK13764
OMAiTWYQSFL
OrthoDBi1271942at2759
TreeFamiTF300009

Enzyme and pathway databases

ReactomeiR-BTA-2514859 Inactivation, recovery and regulation of the phototransduction cascade

Miscellaneous databases

EvolutionaryTraceiP21457

Gene expression databases

BgeeiENSBTAG00000025088 Expressed in testis and 4 other tissues

Family and domain databases

CDDicd00051 EFh, 2 hits
InterProiView protein in InterPro
IPR011992 EF-hand-dom_pair
IPR018247 EF_Hand_1_Ca_BS
IPR002048 EF_hand_dom
IPR028846 Recoverin
PANTHERiPTHR23055 PTHR23055, 1 hit
PfamiView protein in Pfam
PF13499 EF-hand_7, 1 hit
SMARTiView protein in SMART
SM00054 EFh, 2 hits
SUPFAMiSSF47473 SSF47473, 1 hit
PROSITEiView protein in PROSITE
PS00018 EF_HAND_1, 2 hits
PS50222 EF_HAND_2, 4 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRECO_BOVIN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P21457
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: April 22, 2020
This is version 165 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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