RECO_MOUSE
ID RECO_MOUSE Reviewed; 202 AA.
AC P34057;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Recoverin;
DE AltName: Full=23 kDa photoreceptor cell-specific protein;
DE AltName: Full=Cancer-associated retinopathy protein;
DE Short=Protein CAR;
GN Name=Rcvrn; Synonyms=Rcv1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Retina;
RX PubMed=1386025; DOI=10.1016/0014-5793(92)80433-h;
RA McGinnis J.F., Stepanik P.L., Baehr W., Subbaraya I., Lerious V.;
RT "Cloning and sequencing of the 23 kDa mouse photoreceptor cell-specific
RT protein.";
RL FEBS Lett. 302:172-176(1992).
RN [2]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15961391; DOI=10.1074/jbc.m501789200;
RA Strissel K.J., Lishko P.V., Trieu L.H., Kennedy M.J., Hurley J.B.,
RA Arshavsky V.Y.;
RT "Recoverin undergoes light-dependent intracellular translocation in rod
RT photoreceptors.";
RL J. Biol. Chem. 280:29250-29255(2005).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15882641; DOI=10.1016/j.neuron.2005.04.006;
RA Sampath A.P., Strissel K.J., Elias R., Arshavsky V.Y., McGinnis J.F.,
RA Chen J., Kawamura S., Rieke F., Hurley J.B.;
RT "Recoverin improves rod-mediated vision by enhancing signal transmission in
RT the mouse retina.";
RL Neuron 46:413-420(2005).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25673692; DOI=10.1074/jbc.m115.639591;
RA Sakurai K., Chen J., Khani S.C., Kefalov V.J.;
RT "Regulation of mammalian cone phototransduction by recoverin and rhodopsin
RT kinase.";
RL J. Biol. Chem. 290:9239-9250(2015).
RN [5]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=28151698; DOI=10.1369/0022155416689675;
RA Zalis M.C., Johansson S., Englund-Johansson U.;
RT "Immunocytochemical Profiling of Cultured Mouse Primary Retinal Cells.";
RL J. Histochem. Cytochem. 65:223-239(2017).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29435986; DOI=10.1113/jp275779;
RA Morshedian A., Woodruff M.L., Fain G.L.;
RT "Role of recoverin in rod photoreceptor light adaptation.";
RL J. Physiol. (Lond.) 596:1513-1526(2018).
CC -!- FUNCTION: Acts as a calcium sensor and regulates phototransduction of
CC cone and rod photoreceptor cells (By similarity). Modulates light
CC sensitivity of cone photoreceptor in dark and dim conditions
CC (PubMed:25673692). In response to high Ca(2+) levels induced by low
CC light levels, prolongs RHO/rhodopsin activation in rod photoreceptor
CC cells by binding to and inhibiting GRK1-mediated phosphorylation of
CC RHO/rhodopsin (By similarity). Plays a role in scotopic vision/enhances
CC vision in dim light by enhancing signal transfer between rod
CC photoreceptors and rod bipolar cells (PubMed:15882641). Improves rod
CC photoreceptor sensitivity in dim light and mediates response of rod
CC photoreceptors to facilitate detection of change and motion in bright
CC light (PubMed:29435986). {ECO:0000250|UniProtKB:P21457,
CC ECO:0000269|PubMed:15882641, ECO:0000269|PubMed:25673692,
CC ECO:0000269|PubMed:29435986}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Homodimerization
CC is caused by prolonged intense illumination (By similarity). May form a
CC complex composed of RHO, GRK1 and RCVRN in a Ca(2+)-dependent manner;
CC RCVRN prevents the interaction between GRK1 and RHO (By similarity).
CC Interacts (via C-terminus) with GRK1 (via N-terminus); the interaction
CC is Ca(2+)-dependent (By similarity). {ECO:0000250|UniProtKB:P21457}.
CC -!- SUBCELLULAR LOCATION: Photoreceptor inner segment
CC {ECO:0000269|PubMed:15882641, ECO:0000269|PubMed:15961391,
CC ECO:0000269|PubMed:28151698}. Cell projection, cilium, photoreceptor
CC outer segment {ECO:0000269|PubMed:15882641,
CC ECO:0000269|PubMed:15961391, ECO:0000269|PubMed:28151698}.
CC Photoreceptor outer segment membrane {ECO:0000250|UniProtKB:P21457};
CC Lipid-anchor {ECO:0000250|UniProtKB:P21457}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P21457}. Perikaryon
CC {ECO:0000269|PubMed:28151698}. Note=Primarily expressed in the inner
CC segments of light-adapted rod photoreceptors, approximately 10% of
CC which translocates from photoreceptor outer segments upon light
CC stimulation (PubMed:15961391). Targeting of myristoylated protein to
CC rod photoreceptor outer segments is calcium dependent (By similarity).
CC {ECO:0000250|UniProtKB:P21457, ECO:0000269|PubMed:15961391}.
CC -!- TISSUE SPECIFICITY: Expressed in rod photoreceptors in the retina (at
CC protein level). {ECO:0000269|PubMed:1386025,
CC ECO:0000269|PubMed:15882641, ECO:0000269|PubMed:15961391}.
CC -!- DEVELOPMENTAL STAGE: At postnatal day 11 abundantly expressed in the
CC retina outer plexiform layer, outer nuclear layer, and outer limiting
CC membrane, with weak expression in the inner nuclear layer and inner
CC plexiform layer (PubMed:28151698). At postnatal day 22 abundantly
CC expressed in the retina inner nuclear layer, outer plexiform layer,
CC outer nuclear layer, outer limiting membrane, outer segment, and inner
CC segment (PubMed:28151698). {ECO:0000269|PubMed:28151698}.
CC -!- DOMAIN: EF-hand 2 and EF-hand 3 domains are the low-affinity and the
CC high-affinity calcium binding sites, respectively. EF-hand 1 and EF-
CC hand 4 domains do not bind calcium due to substitutions that disrupt
CC their respective Ca(2+) binding loops. The cooperative binding of
CC calcium to the EF-hand 2 domain following EF-hand 3 domain calcium
CC binding requires myristoylation (By similarity). Calcium binding to the
CC 2 EF-hand domains induces exposure of the myristoyl group through a
CC protein conformation change, this process known as the calcium-
CC myristoyl switch facilitates binding to photoreceptor cell membranes
CC (By similarity). {ECO:0000250|UniProtKB:P21457}.
CC -!- PTM: The N-terminal glycine is linked to one of four different types of
CC acyl groups. The most abundant is myristoleate (14:1), but 14:0, 14:2,
CC and 12:0 acyl residues are also present (By similarity). The Ca(2+)
CC induced exposure of the myristoyl group, known as the calcium-myristoyl
CC switch, promotes RCVRN binding to the photoreceptor cell membranes only
CC when intracellular Ca(2+) concentration is high (By similarity).
CC {ECO:0000250|UniProtKB:P21457}.
CC -!- PTM: Oxidation on Cys-39 occurs in response to prolonged intense
CC illumination and results in the formation of disulfide homodimers, and
CC to a lesser extent disulfide-linked heterodimers.
CC {ECO:0000250|UniProtKB:P21457}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice exhibit reduced scotopic vision
CC acuity, however do not show rod photoreceptor degeneration
CC (PubMed:15882641). Rod photoreceptors have a higher visual response
CC threshold resulting in a 4-fold enhancement in sensitivity to low light
CC intensity, with no change in pupil size (PubMed:15882641). Dark adapted
CC rod photoreceptors have a reduced recovery time following stimulus, a
CC reduced adaption time to background light and sustained photoreceptor
CC signaling response following stimulus (PubMed:29435986). Rod
CC photoreceptors have an increased sensitivity to stimulus in saturating
CC background conditions (PubMed:29435986). Mice show a decrease in
CC response, sensitivity and photoreceptor recovery to light stimulus in
CC dark-adapted cone photoreceptors (PubMed:25673692). Rcvrn, Guca1a, and
CC Guca1b triple knockout mice have a sustained photoreceptor signaling
CC response following stimulus during light response in rod photoreceptors
CC (PubMed:29435986). {ECO:0000269|PubMed:15882641,
CC ECO:0000269|PubMed:25673692, ECO:0000269|PubMed:29435986}.
CC -!- SIMILARITY: Belongs to the recoverin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X66196; CAA46958.1; -; mRNA.
DR CCDS; CCDS24859.1; -.
DR PIR; S21155; S21155.
DR RefSeq; NP_033064.1; NM_009038.2.
DR AlphaFoldDB; P34057; -.
DR SMR; P34057; -.
DR STRING; 10090.ENSMUSP00000021290; -.
DR PhosphoSitePlus; P34057; -.
DR PaxDb; P34057; -.
DR PRIDE; P34057; -.
DR ProteomicsDB; 253194; -.
DR Antibodypedia; 12699; 509 antibodies from 33 providers.
DR Ensembl; ENSMUST00000021290; ENSMUSP00000021290; ENSMUSG00000020907.
DR GeneID; 19674; -.
DR KEGG; mmu:19674; -.
DR UCSC; uc007jmz.2; mouse.
DR CTD; 5957; -.
DR MGI; MGI:97883; Rcvrn.
DR VEuPathDB; HostDB:ENSMUSG00000020907; -.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000159441; -.
DR HOGENOM; CLU_072366_1_0_1; -.
DR InParanoid; P34057; -.
DR OMA; WEFFGKK; -.
DR PhylomeDB; P34057; -.
DR TreeFam; TF300009; -.
DR Reactome; R-MMU-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR BioGRID-ORCS; 19674; 2 hits in 71 CRISPR screens.
DR PRO; PR:P34057; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P34057; protein.
DR Bgee; ENSMUSG00000020907; Expressed in retinal neural layer and 40 other tissues.
DR ExpressionAtlas; P34057; baseline and differential.
DR Genevisible; P34057; MM.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:UniProtKB-SubCell.
DR GO; GO:0001750; C:photoreceptor outer segment; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IMP:MGI.
DR GO; GO:0007602; P:phototransduction; IMP:MGI.
DR GO; GO:0051924; P:regulation of calcium ion transport; IMP:MGI.
DR GO; GO:0007601; P:visual perception; IMP:MGI.
DR CDD; cd00051; EFh; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR028846; Recoverin.
DR PANTHER; PTHR23055; PTHR23055; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW Calcium; Cell projection; Disulfide bond; Lipoprotein; Membrane;
KW Metal-binding; Myristate; Oxidation; Redox-active center;
KW Reference proteome; Repeat; Sensory transduction; Vision.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P21457"
FT CHAIN 2..202
FT /note="Recoverin"
FT /id="PRO_0000073760"
FT DOMAIN 41..59
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 61..96
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 97..132
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 147..182
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 189..192
FT /note="Interaction with GRK1"
FT /evidence="ECO:0000250|UniProtKB:P21457"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="low affinity"
FT /evidence="ECO:0000250|UniProtKB:P21457,
FT ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="low affinity"
FT /evidence="ECO:0000250|UniProtKB:P21457,
FT ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="low affinity"
FT /evidence="ECO:0000250|UniProtKB:P21457,
FT ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="low affinity"
FT /evidence="ECO:0000250|UniProtKB:P21457,
FT ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="low affinity"
FT /evidence="ECO:0000250|UniProtKB:P21457,
FT ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 110
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="low affinity"
FT /evidence="ECO:0000250|UniProtKB:P21457,
FT ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 112
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="low affinity"
FT /evidence="ECO:0000250|UniProtKB:P21457,
FT ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 114
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="low affinity"
FT /evidence="ECO:0000250|UniProtKB:P21457,
FT ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="low affinity"
FT /evidence="ECO:0000250|UniProtKB:P21457,
FT ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 121
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="low affinity"
FT /evidence="ECO:0000250|UniProtKB:P21457,
FT ECO:0000255|PROSITE-ProRule:PRU00448"
FT SITE 192
FT /note="Interaction with GRK1"
FT /evidence="ECO:0000250|UniProtKB:P21457"
FT MOD_RES 39
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000250|UniProtKB:P21457"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT DISULFID 39
FT /note="Interchain, redox-active"
FT /evidence="ECO:0000250|UniProtKB:P21457"
SQ SEQUENCE 202 AA; 23407 MW; 2ED23893716D148C CRC64;
MGNSKSGALS KEILEELQLN TKFTEEELSA WYQSFLKECP SGRITRQEFE SIYSKFFPDS
DPKAYAQHVF RSFDANSDGT LDFKEYVIAL HMTTAGKPTQ KLEWAFSLYD VDGNGTISKN
EVLEIVMAIF KMIKPEDVKL LPDDENTPEK RAEKIWAFFG KKEDDKLTEE EFIEGTLANK
EILRLIQFEP QKVKERIKEK KQ
