GRK7_ICTTR
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 03-AUG-2022, entry version 115.
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 PRIDE; Q9Z2G7; -.
DR GeneID; 101975039; -.
DR CTD; 131890; -.
DR eggNOG; KOG0986; Eukaryota.
DR InParanoid; Q9Z2G7; -.
DR OrthoDB; 1104340at2759; -.
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: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; 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..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
