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Rhodopsin kinase (RK) (EC 2.7.11.14) (G protein-coupled receptor kinase 1)

 RK_RAT                  Reviewed;         564 AA.
Q63651;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
23-MAY-2018, entry version 141.
RecName: Full=Rhodopsin kinase;
Short=RK;
EC=2.7.11.14 {ECO:0000250|UniProtKB:Q9WVL4};
AltName: Full=G protein-coupled receptor kinase 1 {ECO:0000312|RGD:619712};
Flags: Precursor;
Name=Grk1 {ECO:0000312|RGD:619712}; Synonyms=Rhok;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Retina;
PubMed=9147475;
Zhao X., Haeseleer F., Fariss R.N., Huang J., Baehr W., Milam A.H.,
Palczewski K.;
"Molecular cloning and localization of rhodopsin kinase in the
mammalian pineal.";
Vis. Neurosci. 14:225-232(1997).
[2]
TISSUE SPECIFICITY.
PubMed=11717351;
Weiss E.R., Ducceschi M.H., Horner T.J., Li A., Craft C.M., Osawa S.;
"Species-specific differences in expression of G-protein-coupled
receptor kinase (GRK) 7 and GRK1 in mammalian cone photoreceptor
cells: implications for cone cell phototransduction.";
J. Neurosci. 21:9175-9184(2001).
[3]
PROTEIN SEQUENCE OF 20-31, IDENTIFICATION BY MASS SPECTROMETRY,
PHOSPHORYLATION AT SER-21, AND TISSUE SPECIFICITY.
PubMed=21504899; DOI=10.1074/jbc.M111.230904;
Osawa S., Jo R., Xiong Y., Reidel B., Tserentsoodol N.,
Arshavsky V.Y., Iuvone P.M., Weiss E.R.;
"Phosphorylation of G protein-coupled receptor kinase 1 (GRK1) is
regulated by light but independent of phototransduction in rod
photoreceptors.";
J. Biol. Chem. 286:20923-20929(2011).
-!- FUNCTION: Retina-specific kinase involved in the signal turnoff
via phosphorylation of rhodopsin (RHO), the G protein- coupled
receptor that initiates the phototransduction cascade. This rapid
desensitization is essential for scotopic vision and permits rapid
adaptation to changes in illumination.
{ECO:0000250|UniProtKB:Q9WVL4}.
-!- CATALYTIC ACTIVITY: ATP + [rhodopsin] = ADP + [rhodopsin]
phosphate. {ECO:0000250|UniProtKB:Q9WVL4}.
-!- SUBUNIT: Interacts (when prenylated) with PDE6D; this promotes
release from membranes. {ECO:0000250|UniProtKB:P28327}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P28327};
Lipid-anchor {ECO:0000250|UniProtKB:P28327}.
-!- TISSUE SPECIFICITY: Detected in retina (at protein level)
(PubMed:21504899). Retina-specific. Expressed in rod and cone
photoreceptor cells. {ECO:0000269|PubMed:11717351,
ECO:0000269|PubMed:21504899}.
-!- PTM: Autophosphorylated, Ser-21 is a minor site of
autophosphorylation compared to Ser-491 and Thr-492 (By
similarity). Phosphorylation at Ser-21 is regulated by light and
activated by cAMP. {ECO:0000250, ECO:0000269|PubMed:21504899}.
-!- PTM: Farnesylation is required for full activity.
{ECO:0000250|UniProtKB:P28327}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. GPRK subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U63971; AAB05930.1; -; mRNA.
RefSeq; NP_112358.1; NM_031096.1.
UniGene; Rn.10548; -.
ProteinModelPortal; Q63651; -.
SMR; Q63651; -.
STRING; 10116.ENSRNOP00000024999; -.
iPTMnet; Q63651; -.
PhosphoSitePlus; Q63651; -.
PaxDb; Q63651; -.
PRIDE; Q63651; -.
GeneID; 81760; -.
KEGG; rno:81760; -.
UCSC; RGD:619712; rat.
CTD; 6011; -.
RGD; 619712; Grk1.
eggNOG; KOG0986; Eukaryota.
eggNOG; ENOG410YRQZ; LUCA.
HOGENOM; HOG000006742; -.
HOVERGEN; HBG004532; -.
InParanoid; Q63651; -.
KO; K00909; -.
PhylomeDB; Q63651; -.
BRENDA; 2.7.11.14; 5301.
PRO; PR:Q63651; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004703; F:G-protein coupled receptor kinase activity; IEA:InterPro.
GO; GO:0050254; F:rhodopsin kinase activity; IDA:RGD.
GO; GO:0046777; P:protein autophosphorylation; IDA:RGD.
GO; GO:0022400; P:regulation of rhodopsin mediated signaling pathway; ISS:UniProtKB.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0009416; P:response to light stimulus; IEP:RGD.
GO; GO:0016056; P:rhodopsin mediated signaling pathway; TAS:RGD.
GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
CDD; cd05608; STKc_GRK1; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR000239; GPCR_kinase.
InterPro; IPR032965; GRK1.
InterPro; IPR037716; GRK1_dom.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR016137; RGS.
InterPro; IPR036305; RGS_sf.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR24355:SF11; PTHR24355:SF11; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00615; RGS; 1.
PRINTS; PR00717; GPCRKINASE.
SMART; SM00315; RGS; 1.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF48097; SSF48097; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS50132; RGS; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Direct protein sequencing; Kinase;
Lipoprotein; Membrane; Methylation; Nucleotide-binding;
Phosphoprotein; Prenylation; Reference proteome; Sensory transduction;
Serine/threonine-protein kinase; Transferase; Vision.
CHAIN 1 561 Rhodopsin kinase.
/FTId=PRO_0000024379.
PROPEP 562 564 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000024380.
DOMAIN 58 175 RGS. {ECO:0000255|PROSITE-
ProRule:PRU00171}.
DOMAIN 190 455 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 456 521 AGC-kinase C-terminal.
NP_BIND 196 204 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 1 189 N-terminal.
REGION 456 564 C-terminal.
ACT_SITE 317 317 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 219 219 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 5 5 Phosphoserine.
{ECO:0000250|UniProtKB:P28327}.
MOD_RES 8 8 Phosphothreonine.
{ECO:0000250|UniProtKB:P28327}.
MOD_RES 21 21 Phosphoserine; by PKA and autocatalysis.
{ECO:0000305|PubMed:21504899}.
MOD_RES 491 491 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:P28327}.
MOD_RES 492 492 Phosphothreonine; by autocatalysis.
{ECO:0000250|UniProtKB:P28327}.
MOD_RES 561 561 Cysteine methyl ester.
{ECO:0000250|UniProtKB:P28327}.
LIPID 561 561 S-farnesyl cysteine.
{ECO:0000250|UniProtKB:P28327}.
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


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