GRK1_RAT
ID GRK1_RAT Reviewed; 564 AA.
AC Q63651;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Rhodopsin kinase GRK1;
DE Short=RK;
DE EC=2.7.11.14 {ECO:0000250|UniProtKB:Q9WVL4};
DE AltName: Full=G protein-coupled receptor kinase 1 {ECO:0000312|RGD:619712};
DE Flags: Precursor;
GN Name=Grk1 {ECO:0000312|RGD:619712}; Synonyms=Rhok;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Retina;
RX PubMed=9147475; DOI=10.1017/s0952523800011366;
RA Zhao X., Haeseleer F., Fariss R.N., Huang J., Baehr W., Milam A.H.,
RA Palczewski K.;
RT "Molecular cloning and localization of rhodopsin kinase in the mammalian
RT pineal.";
RL Vis. Neurosci. 14:225-232(1997).
RN [2]
RP TISSUE SPECIFICITY.
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 [3]
RP PROTEIN SEQUENCE OF 20-31, IDENTIFICATION BY MASS SPECTROMETRY,
RP PHOSPHORYLATION AT SER-21, AND TISSUE SPECIFICITY.
RX PubMed=21504899; DOI=10.1074/jbc.m111.230904;
RA Osawa S., Jo R., Xiong Y., Reidel B., Tserentsoodol N., Arshavsky V.Y.,
RA Iuvone P.M., Weiss E.R.;
RT "Phosphorylation of G protein-coupled receptor kinase 1 (GRK1) is regulated
RT by light but independent of phototransduction in rod photoreceptors.";
RL J. Biol. Chem. 286:20923-20929(2011).
CC -!- FUNCTION: Retina-specific kinase involved in the signal turnoff via
CC phosphorylation of rhodopsin (RHO), the G protein- coupled receptor
CC that initiates the phototransduction cascade (By similarity). This
CC rapid desensitization is essential for scotopic vision and permits
CC rapid adaptation to changes in illumination (By similarity). May play a
CC role in the maintenance of the outer nuclear layer in the retina (By
CC similarity). {ECO:0000250|UniProtKB:Q9WVL4}.
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:Q9WVL4};
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:Q9WVL4};
CC -!- ACTIVITY REGULATION: Inhibited by RCVRN, which prevents the interaction
CC between GRK1 and RHO (By similarity). Inhibition is calcium-dependent
CC (By similarity). {ECO:0000250|UniProtKB:P28327}.
CC -!- SUBUNIT: Interacts (via N-terminus) with RCVRN (via C-terminus); the
CC interaction is Ca(2+)-dependent (By similarity). Interacts (when
CC prenylated) with PDE6D; this promotes release from membranes (By
CC similarity). May form a complex composed of RHO, GRK1 and RCVRN in a
CC Ca(2+)-dependent manner; RCVRN prevents the interaction between GRK1
CC and RHO (By similarity). {ECO:0000250|UniProtKB:P28327}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P28327}; Lipid-
CC anchor {ECO:0000250|UniProtKB:P28327}. Cell projection, cilium,
CC photoreceptor outer segment {ECO:0000250|UniProtKB:Q9WVL4}.
CC Note=Subcellular location is not affected by light or dark conditions.
CC {ECO:0000250|UniProtKB:Q9WVL4}.
CC -!- TISSUE SPECIFICITY: Detected in retina (at protein level)
CC (PubMed:21504899). Retina-specific. Expressed in rod and cone
CC photoreceptor cells. {ECO:0000269|PubMed:11717351,
CC ECO:0000269|PubMed:21504899}.
CC -!- PTM: Autophosphorylated, Ser-21 is a minor site of autophosphorylation
CC compared to Ser-491 and Thr-492 (By similarity). Phosphorylation at
CC Ser-21 is regulated by light and activated by cAMP. {ECO:0000250,
CC ECO:0000269|PubMed:21504899}.
CC -!- PTM: Farnesylation is required for full activity.
CC {ECO:0000250|UniProtKB:P28327}.
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; U63971; AAB05930.1; -; mRNA.
DR RefSeq; NP_112358.1; NM_031096.1.
DR AlphaFoldDB; Q63651; -.
DR SMR; Q63651; -.
DR STRING; 10116.ENSRNOP00000024999; -.
DR iPTMnet; Q63651; -.
DR PhosphoSitePlus; Q63651; -.
DR PaxDb; Q63651; -.
DR GeneID; 81760; -.
DR KEGG; rno:81760; -.
DR UCSC; RGD:619712; rat.
DR CTD; 6011; -.
DR RGD; 619712; Grk1.
DR eggNOG; KOG0986; Eukaryota.
DR InParanoid; Q63651; -.
DR OrthoDB; 1104340at2759; -.
DR PhylomeDB; Q63651; -.
DR BRENDA; 2.7.11.14; 5301.
DR Reactome; R-RNO-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR PRO; PR:Q63651; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001750; C:photoreceptor outer segment; ISO:RGD.
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; IDA:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0008594; P:photoreceptor cell morphogenesis; ISO:RGD.
DR GO; GO:0042327; P:positive regulation of phosphorylation; ISO:RGD.
DR GO; GO:0060060; P:post-embryonic retina morphogenesis in camera-type eye; ISO:RGD.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:RGD.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0022400; P:regulation of rhodopsin mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0009966; P:regulation of signal transduction; IBA:GO_Central.
DR GO; GO:0009416; P:response to light stimulus; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0016056; P:rhodopsin mediated signaling pathway; TAS:RGD.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd05608; STKc_GRK1; 1.
DR Gene3D; 1.10.167.10; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR000239; GPCR_kinase.
DR InterPro; IPR032965; GRK1.
DR InterPro; IPR037716; GRK1_dom.
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:SF11; PTHR24355:SF11; 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; 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; Cell projection; Direct protein sequencing; Kinase;
KW Lipoprotein; Membrane; Methylation; Nucleotide-binding; Phosphoprotein;
KW Prenylation; Reference proteome; Sensory transduction;
KW Serine/threonine-protein kinase; Transferase; Vision.
FT CHAIN 1..561
FT /note="Rhodopsin kinase GRK1"
FT /id="PRO_0000024379"
FT PROPEP 562..564
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000024380"
FT DOMAIN 58..175
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT DOMAIN 190..455
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 456..521
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 1..189
FT /note="N-terminal"
FT REGION 1..15
FT /note="Interaction with RCVRN"
FT /evidence="ECO:0000250|UniProtKB:P28327"
FT REGION 456..564
FT /note="C-terminal"
FT ACT_SITE 317
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 196..204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28327"
FT MOD_RES 8
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P28327"
FT MOD_RES 21
FT /note="Phosphoserine; by PKA and autocatalysis"
FT /evidence="ECO:0000305|PubMed:21504899"
FT MOD_RES 491
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P28327"
FT MOD_RES 492
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P28327"
FT MOD_RES 561
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P28327"
FT LIPID 561
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P28327"
SQ SEQUENCE 564 AA; 63769 MW; 17E05784E6D1ED00 CRC64;
MDFGSLETVV ANSAFIAARG SFDGSSTPSS RDKKYLAKLR LPPLSKCEGL RDSISLEFDN
LCSEQPIGKR LFQQFLKTDE RHVPALELWK DIEDYDTADD DLRPQKAQAI LAEYLDPQGT
LFCNFLDQGM VARVKEGPTG SQDGLFQPLL QATLEHLSQG PFQEYLGSLY FLRFLQWKWL
EAQPIGEDWF LDFRVLGKGG FGEVSACQMK ATGKMYACKK LNKKRLKKRK GYQGAIVEKR
ILAKVHSRFI VSLAYAFETK TDLCLVMTIM NGGDVRYHIY NVDEENPGFP EPRAIYYTAQ
IISGLEHLHQ RRIVYRDLKP ENVLLDNDGN IRISDLGLAV ELKEGQNKTK GYAGTPGFMA
PELLRGEEYD FSVDYFALGV TLYEMIAARG PFRARGEKVE NKELKQRIIS EPVKYPEKFS
QASKDFCEQL LEKDPEKRLG FRDGTCDALR ANVLFKDISW RQLEAGMLIP PFIPDSRTVY
AKNIQDVGAF STVKGVVFDK ADTEFFQEFA SGNCSIPWQE EMIETGFFGD LNVWRPDGQM
PDDMKGITVE EAAPTAKSGM CLIS
