ID GRK1_CAEEL Reviewed; 642 AA.
AC Q09537;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 27-MAR-2024, entry version 158.
DE RecName: Full=G protein-coupled receptor kinase 1;
DE EC=2.7.11.16;
GN Name=grk-1; ORFNames=F19C6.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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; Z48006; CAA88047.1; -; Genomic_DNA.
DR PIR; T21112; T21112.
DR RefSeq; NP_509676.1; NM_077275.4.
DR AlphaFoldDB; Q09537; -.
DR SMR; Q09537; -.
DR BioGRID; 46127; 1.
DR STRING; 6239.F19C6.1.1; -.
DR iPTMnet; Q09537; -.
DR EPD; Q09537; -.
DR PaxDb; 6239-F19C6-1; -.
DR PeptideAtlas; Q09537; -.
DR EnsemblMetazoa; F19C6.1.1; F19C6.1.1; WBGene00001708.
DR GeneID; 181212; -.
DR KEGG; cel:CELE_F19C6.1; -.
DR UCSC; F19C6.1; c. elegans.
DR AGR; WB:WBGene00001708; -.
DR WormBase; F19C6.1; CE01554; WBGene00001708; grk-1.
DR eggNOG; KOG0986; Eukaryota.
DR GeneTree; ENSGT00940000167881; -.
DR HOGENOM; CLU_000288_63_41_1; -.
DR InParanoid; Q09537; -.
DR OMA; ISWQTEM; -.
DR OrthoDB; 2906348at2759; -.
DR PhylomeDB; Q09537; -.
DR PRO; PR:Q09537; -.
DR Proteomes; UP000001940; Chromosome X.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 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:SF28; G PROTEIN-COUPLED RECEPTOR KINASE 2; 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.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..642
FT /note="G protein-coupled receptor kinase 1"
FT /id="PRO_0000086840"
FT DOMAIN 52..188
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT DOMAIN 203..470
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 480..545
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 1..202
FT /note="N-terminal"
FT REGION 612..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 328
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 209..217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 642 AA; 73778 MW; D2A72CBB364793EA CRC64;
MEIENIVANT VYIKARESGG QKKGKSKKWK NYLQFPHYTE CLPLKTEIEV TYAFVVEKQP
IGKLLFHEFC QATNSQYHQC CQFLTKVEEY ETSDDDGQSR RDLASSIVSL LHSKPEDNPS
GSQDEQEFWC SFLSDEVIST CITTADSATH DDEPRSDIFT EPYRLTCQYL TDAPFKEFAE
SMYFHRFLQW KWLEKRPVDK HTFRLYRVLG KGGFGEVCAC QVRASGKMYA LKKLEKKRVK
KRHAETLSLN EKQILQRINS PFVVSLAYAY ETKDALCLVL TLMNGGDLKF HLYNLMPGGF
DEKRVQFYAA EITLGLQHLH SERILYRDLK PENILLDDFG HVRISDLGLA VEIKDNEPIK
GRVGTVGYMA PEIVKNERYS YGVDWWGVGC LIYEMIEGKA PFRQRKEKVK REEVERRVRE
DQEKYSEKFS EAARTLCRGL LHKEPGFRLG CRRVGRPEDG AEEIRAHPFF NTADTVTGRE
PVPWKKMEAG KVTPPFCPDP RAVYAKDVLD IEQFSTVKGV RLDATDTQFY GKFNTGCVSI
PWQSEMIETE CFAELNTFHD EDGNVMWNLR PDGINMDERR NGTSKPGFFS RLFRKKNIEV
TKSLHDLSHL GVEQQQPPKT STQTPAVRSS RAASASGRTL VI
//
