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   08-NOV-2023, entry version 123.
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; 9913-ENSBTAP00000029175; -.
DR   GeneID; 281802; -.
DR   KEGG; bta:281802; -.
DR   CTD; 131890; -.
DR   eggNOG; KOG0986; Eukaryota.
DR   InParanoid; Q8WMV0; -.
DR   OrthoDB; 2906348at2759; -.
DR   Proteomes; UP000009136; Unplaced.
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:0050254; F:rhodopsin kinase activity; ISS:UniProtKB.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009966; P:regulation of signal transduction; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   CDD; cd05607; STKc_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:SF12; RHODOPSIN KINASE GRK7; 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..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
//