RECO_CANLF
ID RECO_CANLF Reviewed; 202 AA.
AC Q8MIH6;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Recoverin;
GN Name=RCVRN; Synonyms=RCV1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-3 AND HIS-202.
RX PubMed=12447165;
RA Dekomien G., Epplen J.T.;
RT "The canine recoverin (RCV1) gene: a candidate gene for generalized
RT progressive retinal atrophy.";
RL Mol. Vis. 8:436-441(2002).
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 (By
CC similarity). In response to high Ca(2+) levels induced by low light
CC levels, prolongs RHO/rhodopsin activation in rod photoreceptor cells by
CC 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 (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:P21457,
CC ECO:0000250|UniProtKB:P34057}.
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:0000250|UniProtKB:P34057}. Cell projection, cilium, photoreceptor
CC outer segment {ECO:0000250|UniProtKB:P34057}. Photoreceptor outer
CC segment membrane {ECO:0000250|UniProtKB:P21457}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P21457}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P21457}. Perikaryon
CC {ECO:0000250|UniProtKB:P34057}. 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 (By similarity). Targeting of myristoylated protein to rod
CC photoreceptor outer segments is calcium dependent (By similarity).
CC {ECO:0000250|UniProtKB:P21457, ECO:0000250|UniProtKB:P34057}.
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 -!- SIMILARITY: Belongs to the recoverin family. {ECO:0000305}.
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DR EMBL; AJ414401; CAC91741.1; -; Genomic_DNA.
DR RefSeq; NP_001014303.1; NM_001014281.1.
DR AlphaFoldDB; Q8MIH6; -.
DR SMR; Q8MIH6; -.
DR STRING; 9612.ENSCAFP00000025716; -.
DR PaxDb; Q8MIH6; -.
DR Ensembl; ENSCAFT00030001999; ENSCAFP00030001771; ENSCAFG00030001151.
DR Ensembl; ENSCAFT00845003222; ENSCAFP00845002556; ENSCAFG00845001836.
DR GeneID; 489500; -.
DR KEGG; cfa:489500; -.
DR CTD; 5957; -.
DR VEuPathDB; HostDB:ENSCAFG00845001836; -.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000159441; -.
DR InParanoid; Q8MIH6; -.
DR OrthoDB; 1271942at2759; -.
DR Proteomes; UP000002254; Chromosome 5.
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; IEA:Ensembl.
DR GO; GO:0007602; P:phototransduction; IEA:Ensembl.
DR GO; GO:0051924; P:regulation of calcium ion transport; IEA:Ensembl.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd00051; EFh; 1.
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 3: Inferred from homology;
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_0000289578"
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="high 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="high 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="high 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="high 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"
FT VARIANT 3
FT /note="N -> K"
FT /evidence="ECO:0000269|PubMed:12447165"
FT VARIANT 202
FT /note="P -> H"
FT /evidence="ECO:0000269|PubMed:12447165"
SQ SEQUENCE 202 AA; 23282 MW; DFC46116CE0B6245 CRC64;
MGNSKSGALS KEILEELQLN TKFTEEELCS WYQSFLKECP SGRITKQEFQ SIYSKFFPEA
DPKAYAQHVF RSFDANSDGT LDFKEYVIAL HMTSAGKTNQ KLEWAFSLYD VDGNGAISKS
EVLEIVMAIF KMISPEDVKQ LPEDENTPEK RAEKIWGFFG KKDDDKLTEE EFIEGTLANK
EILRLIQFEP RKVKEKLKEK KP
