ID   GRK7_ICTTR              Reviewed;         548 AA.
AC   Q9Z2G7;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-NOV-2023, entry version 119.
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   Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS   tridecemlineatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Ictidomys.
OX   NCBI_TaxID=43179;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND AUTOPHOSPHORYLATION.
RC   TISSUE=Retina;
RX   PubMed=9852166;
RA   Weiss E.R., Raman D., Shirakawa S., Ducceschi M.S., Bertram P.T., Wong F.,
RA   Kraft T.W., Osawa S.;
RT   "The cloning of GRK7, a candidate cone opsin kinase, from cone- and rod-
RT   dominant mammalian retinas.";
RL   Mol. Vis. 4:27-27(1998).
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-34.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts (when prenylated) with PDE6D; this promotes release
CC       from membranes. {ECO:0000250|UniProtKB:Q8WMV0}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8WMV0}; Lipid-
CC       anchor {ECO:0000250|UniProtKB:Q8WMV0}.
CC   -!- TISSUE SPECIFICITY: Retina. Cones and rod.
CC       {ECO:0000269|PubMed:9852166}.
CC   -!- PTM: Autophosphorylated. Phosphorylation at Ser-34 is regulated by
CC       light and activated by cAMP (By similarity). {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; AF063016; AAC95001.1; -; mRNA.
DR   RefSeq; NP_001269199.1; NM_001282270.1.
DR   AlphaFoldDB; Q9Z2G7; -.
DR   SMR; Q9Z2G7; -.
DR   STRING; 43179.ENSSTOP00000020054; -.
DR   GeneID; 101975039; -.
DR   CTD; 131890; -.
DR   eggNOG; KOG0986; Eukaryota.
DR   InParanoid; Q9Z2G7; -.
DR   OrthoDB; 2906348at2759; -.
DR   Proteomes; UP000005215; Unassembled WGS sequence.
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:0007165; P:signal transduction; IEA:InterPro.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
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: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; 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..545
FT                   /note="Rhodopsin kinase GRK7"
FT                   /id="PRO_0000024336"
FT   PROPEP          546..548
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000024337"
FT   DOMAIN          54..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          523..548
FT                   /note="Disordered"
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         34
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WTQ7"
FT   MOD_RES         545
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000255"
FT   LIPID           545
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   548 AA;  61993 MW;  092C5BFA5A42A200 CRC64;
     MDMGGLDNLI ANTAYLQARK TDSDSRELQR RRRSLALPGP QGCAELRQSL SPHFHSLCEQ
     QPIGRRLFRD FLATVPKYSQ AVAFLEDVQN WELAEEGPAK TSTLQQLAAT CARDPGPQSF
     LSQDLATKCR AASTDEERKT LVEQAKAETM SFLQEQPFQD FLASPFYDRF LQWKLFEMQP
     VSDKYFTEFR VLGKGGFGEV CAVQVRNTGK MYACKKLDKK RLKKKGGEKM ALLEKEILEK
     VNSPFIVSLA YAFESKTHLC LVMSLMNGGD LKFHIYNVGT RGLAMSRVIF YTAQMTCGVL
     HLHGLGIVYR DLKPENVLLD DLGNCRLSDL GLAVEVQDDK PITQRAGTNG YMAPEILMDK
     ASYSYPVDWF AMGCSIYEMV AGRTPFKDFK EKVSKEDLKE RTMKDEVAFH HENFTEETKD
     ICRLFLAKKP EQRLGSREKA DDPRKHPFFQ TVNFPRLEAG LVEPPFVPDP SVVYAKDVDE
     IDDFSEVRGV EFDDKDKQFF QRFSTGAVPV AWQEEIIETG LFEELNDPNR PSGDGKGDSS
     KSGVCLLL
//