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Protein

Recoverin

Gene

RCVRN

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Seems to be implicated in the pathway from retinal rod guanylate cyclase to rhodopsin. May be involved in the inhibition of the phosphorylation of rhodopsin in a calcium-dependent manner. The calcium-bound recoverin prolongs the photoresponse.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi74 – 85121; low affinityAdd
BLAST
Calcium bindingi110 – 121122; high affinityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Sensory transduction, Vision

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Recoverin
Alternative name(s):
p26
Gene namesi
Name:RCVRN
Synonyms:RCV1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 19

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 202201RecoverinPRO_0000073758Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication

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. Myristoylation is necessary for recoverin to bind photoreceptor membranes when the calcium concentration is greater than one micromolar.1 Publication

Keywords - PTMi

Lipoprotein, Myristate

Proteomic databases

PaxDbiP21457.
PRIDEiP21457.

Expressioni

Tissue specificityi

Retina and pineal gland.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
GRK1P283272EBI-8592784,EBI-7865560

Protein-protein interaction databases

IntActiP21457. 4 interactions.
MINTiMINT-1507490.
STRINGi9913.ENSBTAP00000034949.

Structurei

Secondary structure

1
202
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 2010Combined sources
Helixi25 – 3814Combined sources
Beta strandi42 – 454Combined sources
Helixi46 – 5611Combined sources
Beta strandi58 – 603Combined sources
Helixi63 – 7311Combined sources
Beta strandi78 – 814Combined sources
Helixi83 – 9412Combined sources
Helixi98 – 1003Combined sources
Helixi102 – 1098Combined sources
Beta strandi114 – 1174Combined sources
Helixi119 – 13012Combined sources
Helixi135 – 1384Combined sources
Beta strandi139 – 1413Combined sources
Helixi143 – 1453Combined sources
Helixi148 – 15811Combined sources
Beta strandi162 – 1643Combined sources
Beta strandi166 – 1683Combined sources
Helixi169 – 17810Combined sources
Helixi180 – 1867Combined sources
Helixi190 – 1967Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP21457.
SMRiP21457. Positions 2-191.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21457.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 5936EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini61 – 9636EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini97 – 13236EF-hand 3PROSITE-ProRule annotationAdd
BLAST
Domaini147 – 18236EF-hand 4PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the recoverin family.Curated
Contains 4 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0044. Eukaryota.
COG5126. LUCA.
GeneTreeiENSGT00760000118820.
HOGENOMiHOG000233019.
HOVERGENiHBG108179.
InParanoidiP21457.
KOiK13764.
OMAiKECPSGR.
OrthoDBiEOG7GJ6F3.
TreeFamiTF300009.

Family and domain databases

Gene3Di1.10.238.10. 3 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR028846. Recoverin.
[Graphical view]
PANTHERiPTHR23055. PTHR23055. 1 hit.
PfamiPF13499. EF-hand_7. 1 hit.
PF13833. EF-hand_8. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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
Checksum:i75504DEBE8288BA8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191L → Q AA sequence (PubMed:1672637).Curated
Sequence conflicti21 – 211T → N AA sequence (PubMed:1672637).Curated

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.
UniGeneiBt.56904.

Genome annotation databases

EnsembliENSBTAT00000035069; ENSBTAP00000034949; ENSBTAG00000025088.
GeneIDi281447.
KEGGibta:281447.

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.
UniGeneiBt.56904.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP21457.
SMRiP21457. Positions 2-191.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP21457. 4 interactions.
MINTiMINT-1507490.
STRINGi9913.ENSBTAP00000034949.

Proteomic databases

PaxDbiP21457.
PRIDEiP21457.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000035069; ENSBTAP00000034949; ENSBTAG00000025088.
GeneIDi281447.
KEGGibta:281447.

Organism-specific databases

CTDi5957.

Phylogenomic databases

eggNOGiKOG0044. Eukaryota.
COG5126. LUCA.
GeneTreeiENSGT00760000118820.
HOGENOMiHOG000233019.
HOVERGENiHBG108179.
InParanoidiP21457.
KOiK13764.
OMAiKECPSGR.
OrthoDBiEOG7GJ6F3.
TreeFamiTF300009.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP21457.

Family and domain databases

Gene3Di1.10.238.10. 3 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR028846. Recoverin.
[Graphical view]
PANTHERiPTHR23055. PTHR23055. 1 hit.
PfamiPF13499. EF-hand_7. 1 hit.
PF13833. EF-hand_8. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Recoverin: a calcium sensitive activator of retinal rod guanylate cyclase."
    Dizhoor A.M., Ray S., Kumar S., Niemi G., Spencer M., Brolley D., Walsh K.A., Philipov P.P., Hurley J.B., Stryer L.
    Science 251:915-918(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 6-195.
    Tissue: Retina.
  2. "P26-calcium binding protein from bovine retinal photoreceptor cells."
    Kutuzov M.A., Shmukler B.E., Suslov O.N., Dergachev A.E., Zargarov A.A., Abdulaev N.G.
    FEBS Lett. 293:21-24(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Retina.
  3. "Cloning, expression, and crystallization of recoverin, a calcium sensor in vision."
    Ray S., Zozulya S., Niemi G.A., Flaherty K.M., Brolley D., Dizhoor A.M., McKay D.B., Hurley J., Stryer L.
    Proc. Natl. Acad. Sci. U.S.A. 89:5705-5709(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Retina.
  4. "A 26 kd calcium binding protein from bovine rod outer segments as modulator of photoreceptor guanylate cyclase."
    Lambrecht H.G., Koch K.W.
    EMBO J. 10:793-798(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 18-36.
    Tissue: Retina.
  5. "The NH2 terminus of retinal recoverin is acylated by a small family of fatty acids."
    Dizhoor A.M., Ericsson L.H., Johnson R.S., Kumar S., Olshevskaya E., Zozulya S., Neubert T.A., Stryer L., Hurley J.B., Walsh K.A.
    J. Biol. Chem. 267:16033-16036(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: MYRISTOYLATION AT GLY-2.
  6. "Role of the acylated amino terminus of recoverin in Ca(2+)-dependent membrane interaction."
    Dizhoor A.M., Chen C.-K., Olshevskaya E., Sinelnikova V.V., Phillipov P., Hurley J.B.
    Science 259:829-832(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE OF MYRISTOYLATION.
  7. "Recoverin's role: conclusion withdrawn."
    Hurley J.B., Dizhoor A.M., Stryer L.
    Science 260:740-740(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: RETRACTION ON ORIGINAL PROPOSED FUNCTION.
  8. "Recoverin has S-modulin activity in frog rods."
    Kawamura S., Hisatomi O., Kayada S., Tokunaga F., Kuo C.-H.
    J. Biol. Chem. 268:14579-14582(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Three-dimensional structure of recoverin, a calcium sensor in vision."
    Flaherty K.M., Zozulya S., Stryer L., McKay D.B.
    Cell 75:709-716(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
  10. "Sequestration of the membrane-targeting myristoyl group of recoverin in the calcium-free state."
    Tanaka T., Ames J.B., Harvey T.S., Stryer L., Ikura M.
    Nature 376:444-446(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiRECO_BOVIN
AccessioniPrimary (citable) accession number: P21457
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 143 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Binds two calcium ions; one with high affinity, the other with low affinity.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.