GRK7_BOVIN
ID GRK7_BOVIN Reviewed; 552 AA.
AC Q8WMV0;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Rhodopsin kinase GRK7;
DE EC=2.7.11.14 {ECO:0000250|UniProtKB:Q8WTQ7};
DE AltName: Full=G protein-coupled receptor kinase 7;
DE AltName: Full=G protein-coupled receptor kinase GRK7;
DE Flags: Precursor;
GN Name=GRK7;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhang K., Chen J.K.C., Baehr W.;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP INTERACTION WITH PDE6D.
RX PubMed=14561760; DOI=10.1074/jbc.m306559200;
RA Zhang H., Liu X.H., Zhang K., Chen C.K., Frederick J.M., Prestwich G.D.,
RA Baehr W.;
RT "Photoreceptor cGMP phosphodiesterase delta subunit (PDEdelta) functions as
RT a prenyl-binding protein.";
RL J. Biol. Chem. 279:407-413(2004).
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:0000250|UniProtKB:Q8WTQ7}.
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:0000250|UniProtKB:Q8WTQ7};
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:0000250|UniProtKB:Q8WTQ7};
CC -!- ACTIVITY REGULATION: Inhibited by phosphorylation of Ser-36.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts (when prenylated) with PDE6D; this promotes release
CC from membranes. {ECO:0000269|PubMed:14561760}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:14561760}; Lipid-
CC anchor {ECO:0000305|PubMed:14561760}.
CC -!- PTM: Autophosphorylated in vitro at Ser-490. Phosphorylation at Ser-36
CC is regulated by light and activated by cAMP. {ECO:0000250}.
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; AY049726; AAL06241.1; -; mRNA.
DR RefSeq; NP_776757.1; NM_174332.3.
DR AlphaFoldDB; Q8WMV0; -.
DR SMR; Q8WMV0; -.
DR STRING; 9913.ENSBTAP00000029175; -.
DR PaxDb; Q8WMV0; -.
DR GeneID; 281802; -.
DR KEGG; bta:281802; -.
DR CTD; 131890; -.
DR eggNOG; KOG0986; Eukaryota.
DR InParanoid; Q8WMV0; -.
DR OrthoDB; 1104340at2759; -.
DR Proteomes; UP000009136; Unplaced.
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:0050254; F:rhodopsin kinase activity; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
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..549
FT /note="Rhodopsin kinase GRK7"
FT /id="PRO_0000274193"
FT PROPEP 550..552
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000274194"
FT DOMAIN 56..176
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT DOMAIN 191..454
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 455..520
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ACT_SITE 316
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 197..205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 36
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q8WTQ7"
FT MOD_RES 549
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 549
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 552 AA; 62125 MW; 6112CB3B9EB0376D CRC64;
MVDMGGLDNL IANTAYLQAR KSSDADSKEL QRRRRSLMLP GPQSCEQLRQ ALATDFHSLC
EQQPIGRRLF RDFLATVPAY QEARGFLEEV QSWELAEEGP AKGSALQGLV TTCAAAPVPG
RPHPFFSPAL VTKCQAATTD DDRASLVELA KAEVMAFLQD QPFREFLASP FYDKFLQWKV
FEMQPVSDKY FEEFRVLGKG GFGEVCAVQV KNTGKMYACK KLDKKRLKKK NGEKMALLEK
EILERVSSPF IVSLAYAFES KSHLCLVMSL MNGGDLKFHI YSVGEPGLDM SRVIFYSAQI
TCGVLHLHSL GIVYRDMKPE NVLLDDLGNC RLSDLGLAVQ IQDGKPITQR AGTNGYMAPE
ILMEKASYSY PVDWFAMGCS IYEMVAGRTP FRDYKEKVSK EDLKQRTLKE EVRFQHSNFT
EEAKDICRLF LAKTPEQRLG SREKSDDPRK HHFFKTINFP RLEAGLVEPP FVPDPSVVYA
KDINEIDDFS EVRGVEFDDN DKQFFQRFAT GAVPIAWQEE IIETGPFAEL NDPNRPAGCG
EGSSRSGVCL LL
