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   24-JAN-2024, entry version 156.
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   iPTMnet; O70291; -.
DR   PhosphoSitePlus; O70291; -.
DR   MaxQB; O70291; -.
DR   PaxDb; 10090-ENSMUSP00000001112; -.
DR   PeptideAtlas; O70291; -.
DR   ProteomicsDB; 271165; -.
DR   Antibodypedia; 3832; 301 antibodies from 29 providers.
DR   DNASU; 14772; -.
DR   Ensembl; ENSMUST00000001112.14; ENSMUSP00000001112.8; ENSMUSG00000052783.17.
DR   GeneID; 14772; -.
DR   KEGG; mmu:14772; -.
DR   UCSC; uc008xcz.1; mouse.
DR   AGR; MGI:95801; -.
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; PFRPDPN; -.
DR   OrthoDB; 2906348at2759; -.
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 80 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 85 other cell types or tissues.
DR   ExpressionAtlas; O70291; baseline and differential.
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: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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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   CDD; cd05605; STKc_GRK4_like; 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:SF14; G PROTEIN-COUPLED RECEPTOR KINASE 4; 1.
DR   PANTHER; PTHR24355; G PROTEIN-COUPLED RECEPTOR KINASE/RIBOSOMAL PROTEIN S6 KINASE; 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; 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; O70291; MM.
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
//