GRK7_PIG
ID GRK7_PIG Reviewed; 553 AA.
AC Q8WP15;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, 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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=11717351; DOI=10.1523/jneurosci.21-23-09175.2001;
RA Weiss E.R., Ducceschi M.H., Horner T.J., Li A., Craft C.M., Osawa S.;
RT "Species-specific differences in expression of G-protein-coupled receptor
RT kinase (GRK) 7 and GRK1 in mammalian cone photoreceptor cells: implications
RT for cone cell phototransduction.";
RL J. Neurosci. 21:9175-9184(2001).
RN [2]
RP PHOSPHORYLATION AT SER-36.
RX PubMed=18803695; DOI=10.1111/j.1471-4159.2008.05691.x;
RA Osawa S., Jo R., Weiss E.R.;
RT "Phosphorylation of GRK7 by PKA in cone photoreceptor cells is regulated by
RT light.";
RL J. Neurochem. 107:1314-1324(2008).
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:0000250|UniProtKB:Q8WMV0}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8WMV0}; Lipid-
CC anchor {ECO:0000250|UniProtKB:Q8WMV0}.
CC -!- PTM: Autophosphorylated in vitro at Ser-490 (By similarity).
CC Phosphorylation at Ser-36 is regulated by light and activated by cAMP.
CC {ECO:0000250, ECO:0000269|PubMed:18803695}.
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; AF282270; AAL33881.1; -; mRNA.
DR RefSeq; NP_999212.1; NM_214047.1.
DR RefSeq; XP_013837535.1; XM_013982081.1.
DR AlphaFoldDB; Q8WP15; -.
DR SMR; Q8WP15; -.
DR STRING; 9823.ENSSSCP00000012443; -.
DR iPTMnet; Q8WP15; -.
DR PaxDb; Q8WP15; -.
DR PeptideAtlas; Q8WP15; -.
DR PRIDE; Q8WP15; -.
DR Ensembl; ENSSSCT00000012780; ENSSSCP00000012443; ENSSSCG00000011675.
DR Ensembl; ENSSSCT00005038990; ENSSSCP00005023950; ENSSSCG00005024558.
DR Ensembl; ENSSSCT00015006654; ENSSSCP00015002743; ENSSSCG00015004956.
DR Ensembl; ENSSSCT00025076955; ENSSSCP00025033347; ENSSSCG00025056254.
DR Ensembl; ENSSSCT00035106501; ENSSSCP00035045890; ENSSSCG00035078026.
DR Ensembl; ENSSSCT00040007048; ENSSSCP00040002796; ENSSSCG00040005326.
DR Ensembl; ENSSSCT00045052245; ENSSSCP00045036343; ENSSSCG00045030654.
DR Ensembl; ENSSSCT00050021081; ENSSSCP00050008793; ENSSSCG00050015584.
DR Ensembl; ENSSSCT00055051399; ENSSSCP00055041084; ENSSSCG00055026023.
DR Ensembl; ENSSSCT00065020048; ENSSSCP00065008159; ENSSSCG00065015051.
DR Ensembl; ENSSSCT00070014972; ENSSSCP00070012391; ENSSSCG00070007747.
DR GeneID; 397114; -.
DR KEGG; ssc:397114; -.
DR CTD; 131890; -.
DR VGNC; VGNC:88699; GRK7.
DR eggNOG; KOG0986; Eukaryota.
DR GeneTree; ENSGT00940000160511; -.
DR HOGENOM; CLU_000288_63_41_1; -.
DR InParanoid; Q8WP15; -.
DR OMA; VFEMQPV; -.
DR OrthoDB; 1104340at2759; -.
DR TreeFam; TF313940; -.
DR Reactome; R-SSC-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Proteomes; UP000008227; Chromosome 13.
DR Proteomes; UP000314985; Chromosome 13.
DR Bgee; ENSSSCG00000011675; Expressed in oocyte and 17 other tissues.
DR Genevisible; Q8WP15; SS.
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:0004703; F:G protein-coupled receptor kinase activity; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0050254; F:rhodopsin kinase activity; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
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 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..550
FT /note="Rhodopsin kinase GRK7"
FT /id="PRO_0000024334"
FT PROPEP 551..553
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000024335"
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:0000269|PubMed:18803695"
FT MOD_RES 550
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 550
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 553 AA; 62299 MW; 9BAD6E91BF31D33E CRC64;
MVDMGGLDNL IANTAYLQAR KTSDADSKEL QRRRRSLMLP GPQSCEQLRQ AMPADFNSLC
EQQPIGRRLF RDFLATVPAY QEAMGFLEEV QSWELAEEGP AKGSTLQALV ATCAVAPNPG
QPHSFLSPAL VTKCQAATTD EERASLVEQA KAEAMAFLQD QPFREFLVSP FYDKFLQWKV
FEMQPVSDKY FEEFRVLGKG GFGEVCAVQV KNTGKMYACK KLDKKRLKKK SGEKMALSEK
EILEKVSSPF VVSLAYAFES KSHLCLVMSL MNGGDLKFHI YSVGERGLDM NRVIFYSAQM
TCGVLHLHSL GIVYRDLKPE NVLLDDLGNC RLSDLGLAVQ IQDGKPVTQR AGTNGYMAPE
ILMEKASYSY PVDWFAMGCS IYEMVAGRTP FKDYKEKISK EDLKQRTLKE EVRFQHQSFT
EEAKDICRLF LAKTPEQRLG SREKSDDPRK HHFFKTINFP RLEAGLVDPP FVPDPSVVYA
KDVDEIEDFS EVRGVEFDDK DKQFFQRFAT GAVPIAWQEE IIETGLFEEL NDPNRPAGCG
EGNSSRSGVC LLL
