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

 RK_BOVIN                Reviewed;         561 AA.
P28327;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
01-DEC-1992, sequence version 1.
12-SEP-2018, entry version 155.
RecName: Full=Rhodopsin kinase;
Short=RK;
EC=2.7.11.14 {ECO:0000269|PubMed:1527025, ECO:0000269|PubMed:1730692};
AltName: Full=G protein-coupled receptor kinase 1;
Flags: Precursor;
Name=GRK1; Synonyms=RHOK;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 268-297, AND TISSUE
SPECIFICITY.
TISSUE=Retina;
PubMed=1656454; DOI=10.1073/pnas.88.19.8715;
Lorenz W., Inglese J., Palczewski K., Onorato J.J., Caron M.G.,
Lefkowitz R.J.;
"The receptor kinase family: primary structure of rhodopsin kinase
reveals similarities to the beta-adrenergic receptor kinase.";
Proc. Natl. Acad. Sci. U.S.A. 88:8715-8719(1991).
[2]
ISOPRENYLATION AT CYS-558, METHYLATION AT CYS-558, MUTAGENESIS OF
CYS-558, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=1730692;
Inglese J., Glickman J.F., Lorenz W., Caron M.G., Lefkowitz R.J.;
"Isoprenylation of a protein kinase. Requirement of
farnesylation/alpha-carboxyl methylation for full enzymatic activity
of rhodopsin kinase.";
J. Biol. Chem. 267:1422-1425(1992).
[3]
PHOSPHORYLATION AT SER-21; SER-488 AND THR-489, PARTIAL PROTEIN
SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=1527025;
Palczewski K., Buczylko J., van Hooser P., Carr S.A., Huddleston M.J.,
Crabb J.W.;
"Identification of the autophosphorylation sites in rhodopsin
kinase.";
J. Biol. Chem. 267:18991-18998(1992).
[4]
INTERACTION WITH PDE6D, AND SUBCELLULAR LOCATION.
PubMed=14561760; DOI=10.1074/jbc.M306559200;
Zhang H., Liu X.H., Zhang K., Chen C.K., Frederick J.M.,
Prestwich G.D., Baehr W.;
"Photoreceptor cGMP phosphodiesterase delta subunit (PDEdelta)
functions as a prenyl-binding protein.";
J. Biol. Chem. 279:407-413(2004).
[5]
X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 1-535 IN COMPLEX WITH ATP,
AND PHOSPHORYLATION AT SER-5; THR-8; SER-21; SER-488 AND THR-489.
PubMed=18339619; DOI=10.1074/jbc.M708974200;
Singh P., Wang B., Maeda T., Palczewski K., Tesmer J.J.;
"Structures of rhodopsin kinase in different ligand states reveal key
elements involved in G protein-coupled receptor kinase activation.";
J. Biol. Chem. 283:14053-14062(2008).
-!- 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:0000303|PubMed:1656454, ECO:0000303|PubMed:1730692}.
-!- CATALYTIC ACTIVITY: ATP + [rhodopsin] = ADP + [rhodopsin]
phosphate. {ECO:0000269|PubMed:1527025,
ECO:0000269|PubMed:1730692}.
-!- ACTIVITY REGULATION: Inhibited by phosphorylation of Ser-21.
{ECO:0000250}.
-!- SUBUNIT: Interacts (when prenylated) with PDE6D; this promotes
release from membranes. {ECO:0000269|PubMed:14561760}.
-!- INTERACTION:
P21457:RCVRN; NbExp=2; IntAct=EBI-7865560, EBI-8592784;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:14561760,
ECO:0000269|PubMed:1527025, ECO:0000305|PubMed:1730692}; Lipid-
anchor {ECO:0000269|PubMed:14561760, ECO:0000305|PubMed:1730692}.
-!- TISSUE SPECIFICITY: Rod outer segments of retina photoreceptor
cells (at protein level) (PubMed:1656454, PubMed:1730692,
PubMed:1527025). Retina (PubMed:1656454).
{ECO:0000269|PubMed:1527025, ECO:0000269|PubMed:1656454,
ECO:0000269|PubMed:1730692}.
-!- PTM: Autophosphorylated, Ser-21 is a minor site of
autophosphorylation compared to Ser-488 and Thr-489.
Phosphorylation at Ser-21 is regulated by light and activated by
cAMP (Probable). {ECO:0000305|PubMed:1527025,
ECO:0000305|PubMed:18339619}.
-!- PTM: Farnesylation is required for full activity.
{ECO:0000269|PubMed:1730692}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. GPRK subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M73836; AAA30752.1; -; mRNA.
PIR; A41365; A41365.
RefSeq; NP_776598.1; NM_174173.2.
UniGene; Bt.459; -.
PDB; 2I94; NMR; -; B=1-25.
PDB; 3C4W; X-ray; 2.70 A; A/B=1-535.
PDB; 3C4X; X-ray; 2.90 A; A/B=1-535.
PDB; 3C4Y; X-ray; 7.51 A; A/B=1-535.
PDB; 3C4Z; X-ray; 1.84 A; A=1-535.
PDB; 3C50; X-ray; 2.60 A; A/B=1-535.
PDB; 3C51; X-ray; 3.55 A; A/B=1-535.
PDB; 3QC9; X-ray; 2.70 A; A/B/C/D=1-535.
PDB; 3T8O; X-ray; 2.50 A; A=1-535.
PDB; 4L9I; X-ray; 2.32 A; A/B=30-533.
PDB; 4PNI; X-ray; 1.85 A; A=1-561.
PDB; 4WBO; X-ray; 2.81 A; A/B/C/D=1-535.
PDBsum; 2I94; -.
PDBsum; 3C4W; -.
PDBsum; 3C4X; -.
PDBsum; 3C4Y; -.
PDBsum; 3C4Z; -.
PDBsum; 3C50; -.
PDBsum; 3C51; -.
PDBsum; 3QC9; -.
PDBsum; 3T8O; -.
PDBsum; 4L9I; -.
PDBsum; 4PNI; -.
PDBsum; 4WBO; -.
ProteinModelPortal; P28327; -.
SMR; P28327; -.
IntAct; P28327; 3.
MINT; P28327; -.
STRING; 9913.ENSBTAP00000042484; -.
ChEMBL; CHEMBL3879860; -.
iPTMnet; P28327; -.
PaxDb; P28327; -.
PRIDE; P28327; -.
Ensembl; ENSBTAT00000045068; ENSBTAP00000042484; ENSBTAG00000019963.
GeneID; 281457; -.
KEGG; bta:281457; -.
CTD; 6011; -.
VGNC; VGNC:29654; GRK1.
eggNOG; KOG0986; Eukaryota.
eggNOG; ENOG410YRQZ; LUCA.
GeneTree; ENSGT00860000133699; -.
HOGENOM; HOG000006742; -.
HOVERGEN; HBG004532; -.
InParanoid; P28327; -.
KO; K00909; -.
OMA; KSGMCLV; -.
OrthoDB; EOG091G062G; -.
TreeFam; TF313940; -.
BioCyc; MetaCyc:MONOMER-4461; -.
BRENDA; 2.7.11.14; 908.
Reactome; R-BTA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
SABIO-RK; P28327; -.
EvolutionaryTrace; P28327; -.
Proteomes; UP000009136; Chromosome 12.
GO; GO:0097381; C:photoreceptor disc membrane; TAS:Reactome.
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; ISS:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0022400; P:regulation of rhodopsin mediated signaling pathway; ISS:UniProtKB.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
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;
3D-structure; 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 1 558 Rhodopsin kinase.
/FTId=PRO_0000024373.
PROPEP 559 561 Removed in mature form.
/FTId=PRO_0000024374.
DOMAIN 58 172 RGS. {ECO:0000255|PROSITE-
ProRule:PRU00171}.
DOMAIN 187 452 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159,
ECO:0000269|PubMed:18339619}.
DOMAIN 453 518 AGC-kinase C-terminal.
NP_BIND 193 201 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159,
ECO:0000269|PubMed:18339619}.
NP_BIND 265 267 ATP. {ECO:0000269|PubMed:18339619}.
REGION 1 186 N-terminal.
REGION 453 561 C-terminal.
ACT_SITE 314 314 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 216 216 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 332 332 ATP. {ECO:0000269|PubMed:18339619}.
MOD_RES 5 5 Phosphoserine.
{ECO:0000269|PubMed:18339619}.
MOD_RES 8 8 Phosphothreonine.
{ECO:0000269|PubMed:18339619}.
MOD_RES 21 21 Phosphoserine; by PKA and autocatalysis.
{ECO:0000305|PubMed:1527025,
ECO:0000305|PubMed:18339619}.
MOD_RES 488 488 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:1527025,
ECO:0000269|PubMed:18339619}.
MOD_RES 489 489 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:1527025,
ECO:0000269|PubMed:18339619}.
MOD_RES 558 558 Cysteine methyl ester.
{ECO:0000269|PubMed:1730692}.
LIPID 558 558 S-farnesyl cysteine.
{ECO:0000269|PubMed:1730692}.
MUTAGEN 558 558 C->S: 75% decrease in enzymatic activity.
{ECO:0000269|PubMed:1730692}.
HELIX 13 17 {ECO:0000244|PDB:3C4W}.
HELIX 20 23 {ECO:0000244|PDB:3C4W}.
STRAND 25 27 {ECO:0000244|PDB:3C4W}.
HELIX 33 36 {ECO:0000244|PDB:3C4Z}.
HELIX 44 47 {ECO:0000244|PDB:3C4Z}.
HELIX 48 53 {ECO:0000244|PDB:3C4Z}.
HELIX 58 62 {ECO:0000244|PDB:3C4Z}.
HELIX 66 78 {ECO:0000244|PDB:3C4Z}.
HELIX 80 82 {ECO:0000244|PDB:3C4Z}.
HELIX 83 96 {ECO:0000244|PDB:3C4Z}.
TURN 100 102 {ECO:0000244|PDB:3C4Z}.
HELIX 103 114 {ECO:0000244|PDB:3C4Z}.
STRAND 116 119 {ECO:0000244|PDB:3QC9}.
HELIX 128 135 {ECO:0000244|PDB:3C4Z}.
TURN 140 143 {ECO:0000244|PDB:4PNI}.
HELIX 144 154 {ECO:0000244|PDB:3C4Z}.
HELIX 157 163 {ECO:0000244|PDB:3C4Z}.
HELIX 166 178 {ECO:0000244|PDB:3C4Z}.
HELIX 184 186 {ECO:0000244|PDB:3C4Z}.
STRAND 187 195 {ECO:0000244|PDB:3C4Z}.
STRAND 197 206 {ECO:0000244|PDB:3C4Z}.
TURN 207 209 {ECO:0000244|PDB:3C4Z}.
STRAND 212 219 {ECO:0000244|PDB:3C4Z}.
HELIX 220 225 {ECO:0000244|PDB:3C4Z}.
HELIX 229 241 {ECO:0000244|PDB:3C4Z}.
STRAND 250 255 {ECO:0000244|PDB:3C4Z}.
STRAND 257 264 {ECO:0000244|PDB:3C4Z}.
STRAND 269 271 {ECO:0000244|PDB:3C4W}.
HELIX 272 277 {ECO:0000244|PDB:3C4Z}.
STRAND 278 283 {ECO:0000244|PDB:4PNI}.
HELIX 288 307 {ECO:0000244|PDB:3C4Z}.
HELIX 317 319 {ECO:0000244|PDB:3C4Z}.
STRAND 320 322 {ECO:0000244|PDB:3C4Z}.
STRAND 328 330 {ECO:0000244|PDB:3C4Z}.
HELIX 333 335 {ECO:0000244|PDB:4PNI}.
TURN 353 355 {ECO:0000244|PDB:3C4Z}.
HELIX 358 361 {ECO:0000244|PDB:3C4Z}.
HELIX 369 384 {ECO:0000244|PDB:3C4Z}.
STRAND 385 387 {ECO:0000244|PDB:3T8O}.
STRAND 388 390 {ECO:0000244|PDB:4L9I}.
HELIX 398 407 {ECO:0000244|PDB:3C4Z}.
HELIX 418 427 {ECO:0000244|PDB:3C4Z}.
HELIX 432 434 {ECO:0000244|PDB:3C4Z}.
HELIX 444 447 {ECO:0000244|PDB:3C4Z}.
HELIX 450 452 {ECO:0000244|PDB:3C4Z}.
HELIX 457 461 {ECO:0000244|PDB:3C4Z}.
STRAND 473 475 {ECO:0000244|PDB:3C4Z}.
HELIX 481 483 {ECO:0000244|PDB:4L9I}.
HELIX 497 506 {ECO:0000244|PDB:3C4Z}.
HELIX 512 521 {ECO:0000244|PDB:3C4Z}.
HELIX 524 528 {ECO:0000244|PDB:3C4Z}.
SEQUENCE 561 AA; 62934 MW; 1AC6FEC1B277DDD8 CRC64;
MDFGSLETVV ANSAFIAARG SFDASSGPAS RDRKYLARLK LPPLSKCEAL RESLDLGFEG
MCLEQPIGKR LFQQFLRTHE QHGPALQLWK DIEDYDTADD ALRPQKAQAL RAAYLEPQAQ
LFCSFLDAET VARARAGAGD GLFQPLLRAV LAHLGQAPFQ EFLDSLYFLR FLQWKWLEAQ
PMGEDWFLDF RVLGRGGFGE VFACQMKATG KLYACKKLNK KRLKKRKGYQ GAMVEKKILA
KVHSRFIVSL AYAFETKTDL CLVMTIMNGG DIRYHIYNVD EDNPGFQEPR AIFYTAQIVS
GLEHLHQRNI IYRDLKPENV LLDDDGNVRI SDLGLAVELK AGQTKTKGYA GTPGFMAPEL
LLGEEYDFSV DYFALGVTLY EMIAARGPFR ARGEKVENKE LKQRVLEQAV TYPDKFSPAS
KDFCEALLQK DPEKRLGFRD GSCDGLRTHP LFRDISWRQL EAGMLTPPFV PDSRTVYAKN
IQDVGAFSTV KGVAFEKADT EFFQEFASGT CPIPWQEEMI ETGVFGDLNV WRPDGQMPDD
MKGVSGQEAA PSSKSGMCVL S


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