GRK4_MOUSE
ID GRK4_MOUSE Reviewed; 574 AA.
AC O70291; Q3V151;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=G protein-coupled receptor kinase 4;
DE EC=2.7.11.16;
DE AltName: Full=G protein-coupled receptor kinase GRK4;
GN Name=Grk4; Synonyms=Gprk2l;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10506199; DOI=10.1074/jbc.274.41.29381;
RA Premont R.T., Macrae A.D., Aparicio S.A., Kendall H.E., Welch J.E.,
RA Lefkowitz R.J.;
RT "The GRK4 subfamily of G protein-coupled receptor kinases. Alternative
RT splicing, gene organization, and sequence conservation.";
RL J. Biol. Chem. 274:29381-29389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Specifically phosphorylates the activated forms of G protein-
CC coupled receptors.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[G-protein-coupled receptor] + ATP = [G-protein-coupled
CC receptor]-phosphate + ADP + H(+); Xref=Rhea:RHEA:12008, Rhea:RHEA-
CC COMP:11260, Rhea:RHEA-COMP:11261, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546,
CC ChEBI:CHEBI:456216; EC=2.7.11.16;
CC -!- ACTIVITY REGULATION: Inhibited by heparin. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with DRD3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cell cortex {ECO:0000250}.
CC -!- PTM: Palmitoylated. {ECO:0000250}.
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; AF040745; AAC09266.1; -; mRNA.
DR EMBL; AK132685; BAE21301.1; -; mRNA.
DR EMBL; CH466524; EDL37466.1; -; Genomic_DNA.
DR EMBL; BC150691; AAI50692.1; -; mRNA.
DR CCDS; CCDS19219.1; -.
DR RefSeq; NP_001074212.1; NM_001080743.1.
DR RefSeq; NP_062370.2; NM_019497.2.
DR AlphaFoldDB; O70291; -.
DR SMR; O70291; -.
DR STRING; 10090.ENSMUSP00000001112; -.
DR PhosphoSitePlus; O70291; -.
DR MaxQB; O70291; -.
DR PaxDb; O70291; -.
DR PeptideAtlas; O70291; -.
DR PRIDE; O70291; -.
DR ProteomicsDB; 271165; -.
DR Antibodypedia; 3832; 281 antibodies from 29 providers.
DR DNASU; 14772; -.
DR Ensembl; ENSMUST00000001112; ENSMUSP00000001112; ENSMUSG00000052783.
DR GeneID; 14772; -.
DR KEGG; mmu:14772; -.
DR UCSC; uc008xcz.1; mouse.
DR CTD; 2868; -.
DR MGI; MGI:95801; Grk4.
DR VEuPathDB; HostDB:ENSMUSG00000052783; -.
DR eggNOG; KOG0986; Eukaryota.
DR GeneTree; ENSGT00940000160151; -.
DR HOGENOM; CLU_000288_63_41_1; -.
DR InParanoid; O70291; -.
DR OMA; EVCFKSD; -.
DR OrthoDB; 1104340at2759; -.
DR PhylomeDB; O70291; -.
DR TreeFam; TF313940; -.
DR Reactome; R-MMU-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR BioGRID-ORCS; 14772; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Grk4; mouse.
DR PRO; PR:O70291; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; O70291; protein.
DR Bgee; ENSMUSG00000052783; Expressed in spermatid and 83 other tissues.
DR ExpressionAtlas; O70291; baseline and differential.
DR Genevisible; O70291; MM.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004703; F:G protein-coupled receptor kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0050254; F:rhodopsin kinase activity; ISO:MGI.
DR GO; GO:0002029; P:desensitization of G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0002031; P:G protein-coupled receptor internalization; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:0031623; P:receptor internalization; ISO:MGI.
DR GO; GO:0009966; P:regulation of signal transduction; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
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; 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 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cytoplasm; Kinase; Lipoprotein;
KW Nucleotide-binding; Palmitate; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..574
FT /note="G protein-coupled receptor kinase 4"
FT /id="PRO_0000085968"
FT DOMAIN 51..171
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT DOMAIN 186..448
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 449..514
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 1..153
FT /note="N-terminal"
FT ACT_SITE 311
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 192..200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P32298"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70507"
FT CONFLICT 6
FT /note="F -> M (in Ref. 1; AAC09266)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 574 AA; 66928 MW; 7D7D6F46C9C044B6 CRC64;
MELENFVANN LLLKARLGFN KQTGRSKKWR ELLKFPPVSM CTELRWSIEK DFSSLCDKQP
IGRLLFRQFC DTKPDLKRCI EFLDAVAEYE VTIEEEQREF GLAIFSRFFK EKSEVPLPEI
PPDIVKECKW NLKQNSPSQN VFEECAGIVC KYLSETPFEE YQESTYFNRF LQWKWLERRP
VTKNTFRQYR VLGKGGFGEV CACQVRATGK MYACKKLEKK RIKKRKGEAM ALNEKRILEK
LHSRFVVSLA YTYETKDALC LVLTIMNGGD LKYHIYNLGD PGFEEPRAVF YAAELCCGLE
DLQRKRIVYR DLKPENILLD DHGHIRISDL GLAMEVPEGE MVRGRVGTVG YMAPEIINHE
KYTFSPDWWG LGCLIYEMIA GHSPFRKYKE KVNREELERR VKNETEEYSE RFSEDAKSIC
SMLLIKDPSK RLGCQRDGVS AVKQHPIFKD INFSRLEANM LDPPFIPDPQ AIYCRNILDI
GQFSVVKGVN LDTNDEIFYA EFATGSVTIP WQNEMIESGC FKDLNENEDD LSSLEKYKMC
SSILRPKRNF FRRLFRRTGC LNIALSEERE PTEH
