ID   GPRK1_DROME             Reviewed;         700 AA.
AC   P32865; B5RJK1; Q4V555; Q7PLS9;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 2.
DT   24-JAN-2024, entry version 180.
DE   RecName: Full=G protein-coupled receptor kinase 1;
DE            EC=2.7.11.16;
GN   Name=Gprk1; Synonyms=Gprk-1; ORFNames=CG40129;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retina;
RX   PubMed=1662381; DOI=10.1073/pnas.88.24.11067;
RA   Cassill J.A., Whitney M., Joazeiro C.A., Becker A., Zuker C.S.;
RT   "Isolation of Drosophila genes encoding G protein-coupled receptor
RT   kinases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:11067-11070(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Carlson J.W., Booth B., Chavez C., Frise E., George R.A.,
RA   Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically phosphorylates the activated forms of G protein-
CC       coupled receptors. {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. GPRK subfamily. {ECO:0000305}.
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DR   EMBL; M80493; AAA28588.1; -; mRNA.
DR   EMBL; AE013599; EAA46156.2; -; Genomic_DNA.
DR   EMBL; BT022770; AAY55186.1; -; mRNA.
DR   EMBL; BT022801; AAY55217.1; -; mRNA.
DR   EMBL; BT044475; ACH92540.1; -; mRNA.
DR   PIR; A41615; A41615.
DR   RefSeq; NP_001036438.1; NM_001042973.3.
DR   RefSeq; NP_001163051.1; NM_001169580.2.
DR   RefSeq; NP_001286135.1; NM_001299206.1.
DR   AlphaFoldDB; P32865; -.
DR   SMR; P32865; -.
DR   BioGRID; 78138; 1.
DR   IntAct; P32865; 1.
DR   STRING; 7227.FBpp0311517; -.
DR   PaxDb; 7227-FBpp0110413; -.
DR   EnsemblMetazoa; FBtr0111121; FBpp0110413; FBgn0260798.
DR   EnsemblMetazoa; FBtr0302242; FBpp0291451; FBgn0260798.
DR   EnsemblMetazoa; FBtr0345363; FBpp0311517; FBgn0260798.
DR   GeneID; 3355013; -.
DR   KEGG; dme:Dmel_CG40129; -.
DR   AGR; FB:FBgn0260798; -.
DR   CTD; 3355013; -.
DR   FlyBase; FBgn0260798; Gprk1.
DR   VEuPathDB; VectorBase:FBgn0260798; -.
DR   eggNOG; KOG0986; Eukaryota.
DR   GeneTree; ENSGT00940000169024; -.
DR   HOGENOM; CLU_000288_63_41_1; -.
DR   InParanoid; P32865; -.
DR   OMA; KHFSLTI; -.
DR   OrthoDB; 3415459at2759; -.
DR   PhylomeDB; P32865; -.
DR   BRENDA; 2.7.11.14; 1994.
DR   Reactome; R-DME-111933; Calmodulin induced events.
DR   Reactome; R-DME-416476; G alpha (q) signalling events.
DR   Reactome; R-DME-418555; G alpha (s) signalling events.
DR   Reactome; R-DME-5635838; Activation of SMO.
DR   BioGRID-ORCS; 3355013; 1 hit in 3 CRISPR screens.
DR   ChiTaRS; Gprk1; fly.
DR   GenomeRNAi; 3355013; -.
DR   PRO; PR:P32865; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0260798; Expressed in wing disc and 21 other cell types or tissues.
DR   ExpressionAtlas; P32865; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
DR   GO; GO:0005886; C:plasma membrane; ISS:FlyBase.
DR   GO; GO:0005524; F:ATP binding; IMP:FlyBase.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; IPI:FlyBase.
DR   GO; GO:0004703; F:G protein-coupled receptor kinase activity; ISS:FlyBase.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IDA:FlyBase.
DR   GO; GO:0050254; F:rhodopsin kinase activity; IMP:FlyBase.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0016060; P:metarhodopsin inactivation; IMP:FlyBase.
DR   GO; GO:0007603; P:phototransduction, visible light; IMP:FlyBase.
DR   GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IGI:FlyBase.
DR   GO; GO:0006468; P:protein phosphorylation; IMP:FlyBase.
DR   GO; GO:0009966; P:regulation of signal transduction; IBA:GO_Central.
DR   CDD; cd01240; PH_GRK2_subgroup; 1.
DR   CDD; cd08747; RGS_GRK2_GRK3; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
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:SF18; G PROTEIN-COUPLED RECEPTOR KINASE; 1.
DR   PANTHER; PTHR24355; G PROTEIN-COUPLED RECEPTOR KINASE/RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00615; RGS; 1.
DR   PRINTS; PR00717; GPCRKINASE.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00315; RGS; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF50729; PH domain-like; 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; PS50003; PH_DOMAIN; 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; P32865; DM.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..700
FT                   /note="G protein-coupled receptor kinase 1"
FT                   /id="PRO_0000085965"
FT   DOMAIN          54..175
FT                   /note="RGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT   DOMAIN          191..454
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          455..522
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT   DOMAIN          557..657
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   REGION          1..190
FT                   /note="N-terminal"
FT   ACT_SITE        318
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         197..205
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         220
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CONFLICT        58
FT                   /note="I -> N (in Ref. 1; AAA28588)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        620
FT                   /note="N -> I (in Ref. 4; ACH92540)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   700 AA;  80566 MW;  44C6F3988A6A91CF CRC64;
     MADLEAVLAD VSYLMAMEKS KCTPAARASK KLNLPDPSVR SVMYKYLEKE GELNFHKIFN
     EVLGYLLFKD FCENDSEEPI QQLKFFEQIK LFEKTECYDE RKKMARDIYD NFIMEEMLSH
     TYEYSKHAVA SVQKYLLKNE VPVDLFEPYL EEIFTQLKGK PFKKFLESDK FTRFCQWKNL
     ELNIQLTMND FSVHRIIGRG GFGEVYGCRK ADTGKMYAMK CLDKKRIKMK QGEMLALNER
     NMLQAVSTGI DCPFIVCMTY AFHTPDKLCF ILDLMNGGDL HYHLSQHGIF SEDEMKFYAA
     EVILGLEHMH KRCIVYRDLK PANILLDENG HIRISDLGLA CDFSKKKPHA SVGTHGYMAP
     EVLSKGTSYD SCADWFSFGC MLYKLLKGHS PFRQHKTKDK LEIDKMTLTM NVELPESFSL
     ELKNLLEMLL QRDVSKRLGC MGNGADEVKM HNFFCGIDWH QVYIQKYTPP LVPPRGEVNA
     ADAFDIGSFD EEDTKGIKLN DADQDLYKMF SLTISERWQQ EVSETVFDTV NTETDKLEQK
     RKLKQKQHFD ADEKESDCIL HGYIKKLGGS FASLWQTKYA KLYPNRLELH SESGNNKPEL
     IFMDQVEDIS SDFILHKNEN CIQIRINDGT RDGRIILTNS DEIGLKEWSS SLRSAHKISQ
     DLLGSMAKKA GKIYGSERDV NKSMYIFGGN CSTKTSNGSN
//