GRK7A_DANRE
ID GRK7A_DANRE Reviewed; 549 AA.
AC Q49HM9; Q1XHL8;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Rhodopsin kinase grk7a;
DE EC=2.7.11.14 {ECO:0000269|PubMed:16787417};
DE AltName: Full=G protein-coupled receptor kinase 7-1;
DE AltName: Full=G-protein-coupled receptor kinase 7A;
DE Flags: Precursor;
GN Name=grk7a; Synonyms=grk7-1; ORFNames=dkeyp-13a3.1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16039565; DOI=10.1016/j.neuron.2005.06.010;
RA Rinner O., Makhankov Y.V., Biehlmaier O., Neuhauss S.C.;
RT "Knockdown of cone-specific kinase GRK7 in larval zebrafish leads to
RT impaired cone response recovery and delayed dark adaptation.";
RL Neuron 47:231-242(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=16787417; DOI=10.1111/j.1471-4159.2006.03920.x;
RA Wada Y., Sugiyama J., Okano T., Fukada Y.;
RT "GRK1 and GRK7: unique cellular distribution and widely different
RT activities of opsin phosphorylation in the zebrafish rods and cones.";
RL J. Neurochem. 98:824-837(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Retina-specific kinase involved in the shutoff of the
CC photoresponse and adaptation to changing light conditions via cone
CC opsin phosphorylation, including rhodopsin (RHO).
CC {ECO:0000269|PubMed:16039565}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[rhodopsin] = ADP + H(+) + O-phospho-L-
CC threonyl-[rhodopsin]; Xref=Rhea:RHEA:56552, Rhea:RHEA-COMP:14596,
CC Rhea:RHEA-COMP:14597, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.14; Evidence={ECO:0000269|PubMed:16787417};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[rhodopsin] = ADP + H(+) + O-phospho-L-seryl-
CC [rhodopsin]; Xref=Rhea:RHEA:23356, Rhea:RHEA-COMP:14594, Rhea:RHEA-
CC COMP:14595, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.14;
CC Evidence={ECO:0000269|PubMed:16787417};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.4 uM for rhodopsin {ECO:0000269|PubMed:16787417};
CC Vmax=773 nmol/min/mg enzyme {ECO:0000269|PubMed:16787417};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8WMV0}; Lipid-
CC anchor {ECO:0000250|UniProtKB:Q8WMV0}.
CC -!- PTM: Phosphorylation at Ser-33 is regulated by light and activated by
CC cAMP. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Impaired cone response recovery and delayed dark
CC adaptation. {ECO:0000269|PubMed:16039565}.
CC -!- MISCELLANEOUS: Although the protein is present in a diversity of
CC vertebrates ranging from bony fish to mammals, the mouse and rat
CC orthologous proteins do not exist.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. GPRK subfamily. {ECO:0000305}.
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DR EMBL; AY900004; AAX69081.1; -; mRNA.
DR EMBL; AB212995; BAE92858.1; -; mRNA.
DR EMBL; CR377211; CAQ13370.1; -; Genomic_DNA.
DR EMBL; BC163587; AAI63587.1; -; mRNA.
DR RefSeq; NP_001027011.2; NM_001031841.3.
DR AlphaFoldDB; Q49HM9; -.
DR SMR; Q49HM9; -.
DR STRING; 7955.ENSDARP00000091060; -.
DR PaxDb; Q49HM9; -.
DR PRIDE; Q49HM9; -.
DR Ensembl; ENSDART00000100287; ENSDARP00000091060; ENSDARG00000020602.
DR GeneID; 566120; -.
DR KEGG; dre:566120; -.
DR CTD; 566120; -.
DR ZFIN; ZDB-GENE-050824-1; grk7a.
DR eggNOG; KOG0986; Eukaryota.
DR GeneTree; ENSGT00940000160511; -.
DR HOGENOM; CLU_000288_63_41_1; -.
DR InParanoid; Q49HM9; -.
DR OMA; VFEMQPV; -.
DR OrthoDB; 1104340at2759; -.
DR PhylomeDB; Q49HM9; -.
DR TreeFam; TF313940; -.
DR BRENDA; 2.7.11.14; 928.
DR Reactome; R-DRE-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR SABIO-RK; Q49HM9; -.
DR PRO; PR:Q49HM9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 2.
DR Bgee; ENSDARG00000020602; Expressed in retina and 9 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004703; F:G protein-coupled receptor kinase activity; IEA:InterPro.
DR GO; GO:0009881; F:photoreceptor activity; IMP:ZFIN.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0050254; F:rhodopsin kinase activity; IDA:ZFIN.
DR GO; GO:0036368; P:cone photoresponse recovery; IMP:ZFIN.
DR GO; GO:0007603; P:phototransduction, visible light; IMP:ZFIN.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0009966; P:regulation of signal transduction; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; IMP:ZFIN.
DR Gene3D; 1.10.167.10; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR000239; GPCR_kinase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00615; RGS; 1.
DR PRINTS; PR00717; GPCRKINASE.
DR SMART; SM00315; RGS; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50132; RGS; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Phosphoprotein; Prenylation; Reference proteome;
KW Sensory transduction; Serine/threonine-protein kinase; Transferase; Vision.
FT CHAIN 1..546
FT /note="Rhodopsin kinase grk7a"
FT /id="PRO_0000412812"
FT PROPEP 547..549
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000412813"
FT DOMAIN 53..171
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT DOMAIN 186..449
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 450..515
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 522..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 311
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 192..200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 546
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 546
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000255"
FT CONFLICT 80
FT /note="T -> I (in Ref. 1; AAX69081)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="F -> I (in Ref. 1; AAX69081)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 549 AA; 62232 MW; 3F76C291F8BC9716 CRC64;
MCDMGGLDNL VANTAYLKAQ GGDDKEMKKR RRSLSLPKPE QCASLRTSLD KDFESLCEKQ
PIGKKLFRQY LSQGGPECTT AAEFLDDLNE WELSESAARD KARTNIINKF CKEGSKSSLT
FLTGDVATKC KAVSDKDFEE VMGQVKTATK EFLKGKPFTE YQASPFFDKF LQWKEYEKQP
ISEKYFYEFR TLGKGGFGEV CAVQVKNTGQ MYACKKLCKK RLKKKHGEKM ALLEKKILER
VNSLFIVSLA YAYDTKTHLC LVMSLMNGGD LKYHIYNIGE KGIEMDRIIY YTAQIATGIL
HLHDMDIVYR DMKPENVLLD SQGQCRLSDL GLAVEIAVGK TISQKAGTGA YMAPEILNET
PYRTSVDWWA LGCSIYEMVA GYTPFKGPDA KKEKVEKEEV QRRILNEEPK FEHKNFDAAT
IDIIKQFLKK KIDERLGCKN DDPRKHEWFK SINFARLEAG LIDPPWVPKP NVVYAKDTGD
IAEFSEIKGI EFDAKDDKFF KEFSTGAVSI AWQQEMIDTG LFDELSDPNR KESSGGSDDD
KKSGTCTLL
