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   27-MAR-2024, entry version 119.
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; 7955-ENSDARP00000091060; -.
DR   GeneID; 566120; -.
DR   KEGG; dre:566120; -.
DR   AGR; ZFIN:ZDB-GENE-050824-1; -.
DR   CTD; 566120; -.
DR   ZFIN; ZDB-GENE-050824-1; grk7a.
DR   eggNOG; KOG0986; Eukaryota.
DR   HOGENOM; CLU_000288_63_41_1; -.
DR   InParanoid; Q49HM9; -.
DR   OMA; YFTEFRV; -.
DR   OrthoDB; 2906348at2759; -.
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; Chromosome 2.
DR   Bgee; ENSDARG00000020602; Expressed in retina and 9 other cell types or 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:0009881; F:photoreceptor activity; IMP:ZFIN.
DR   GO; GO:0050254; F:rhodopsin kinase activity; IDA:ZFIN.
DR   GO; GO:0036368; P:cone photoresponse recovery; IMP:ZFIN.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0007603; P:phototransduction, visible light; IMP:ZFIN.
DR   GO; GO:0009966; P:regulation of signal transduction; IBA:GO_Central.
DR   GO; GO:0007601; P:visual perception; IMP:ZFIN.
DR   CDD; cd08749; RGS_GRK7; 1.
DR   Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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   PANTHER; PTHR24355; G PROTEIN-COUPLED RECEPTOR KINASE/RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   PANTHER; PTHR24355:SF32; RHODOPSIN KINASE GRK7A; 1.
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; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 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
//