GPRK1_DROME
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 03-AUG-2022, entry version 175.
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.FBpp0110413; -.
DR PaxDb; P32865; -.
DR PRIDE; P32865; -.
DR EnsemblMetazoa; FBtr0111121; FBpp0110413; FBgn0260798.
DR EnsemblMetazoa; FBtr0302242; FBpp0291451; FBgn0260798.
DR EnsemblMetazoa; FBtr0345363; FBpp0311517; FBgn0260798.
DR GeneID; 3355013; -.
DR KEGG; dme:Dmel_CG40129; -.
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; 1104340at2759; -.
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 tissues.
DR ExpressionAtlas; P32865; baseline and differential.
DR Genevisible; P32865; DM.
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:0004672; F:protein kinase activity; IBA:GO_Central.
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 Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 2.30.29.30; -; 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 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; SSF48097; SSF48097; 1.
DR SUPFAM; SSF56112; SSF56112; 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.
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
