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   24-JAN-2024, entry version 127.
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; 9823-ENSSSCP00000012443; -.
DR   PeptideAtlas; Q8WP15; -.
DR   Ensembl; ENSSSCT00000012780.2; ENSSSCP00000012443.1; ENSSSCG00000011675.3.
DR   Ensembl; ENSSSCT00005038990.1; ENSSSCP00005023950.1; ENSSSCG00005024558.1.
DR   Ensembl; ENSSSCT00015006654.1; ENSSSCP00015002743.1; ENSSSCG00015004956.1.
DR   Ensembl; ENSSSCT00025076955.1; ENSSSCP00025033347.1; ENSSSCG00025056254.1.
DR   Ensembl; ENSSSCT00035106501.1; ENSSSCP00035045890.1; ENSSSCG00035078026.1.
DR   Ensembl; ENSSSCT00040007048.1; ENSSSCP00040002796.1; ENSSSCG00040005326.1.
DR   Ensembl; ENSSSCT00045052245.1; ENSSSCP00045036343.1; ENSSSCG00045030654.1.
DR   Ensembl; ENSSSCT00050021081.1; ENSSSCP00050008793.1; ENSSSCG00050015584.1.
DR   Ensembl; ENSSSCT00055051399.1; ENSSSCP00055041084.1; ENSSSCG00055026023.1.
DR   Ensembl; ENSSSCT00065020048.1; ENSSSCP00065008159.1; ENSSSCG00065015051.1.
DR   Ensembl; ENSSSCT00070014972.1; ENSSSCP00070012391.1; ENSSSCG00070007747.1.
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; YFTEFRV; -.
DR   OrthoDB; 2906348at2759; -.
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   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; Unplaced.
DR   Bgee; ENSSSCG00000011675; Expressed in oocyte and 17 other cell types or tissues.
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; 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.
DR   Genevisible; Q8WP15; SS.
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
//