GRK7B_DANRE
ID GRK7B_DANRE Reviewed; 548 AA.
AC Q1XHL7;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Rhodopsin kinase grk7-b;
DE EC=2.7.11.14 {ECO:0000269|PubMed:16787417};
DE AltName: Full=G protein-coupled receptor kinase 7-2;
DE AltName: Full=G protein-coupled receptor kinase 7B;
DE Flags: Precursor;
GN Name=grk7b; Synonyms=grk7-2;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=16787417; DOI=10.1111/j.1471-4159.2006.03920.x;
RA Wada Y., Sugiyama J., Okano T., Fukada Y.;
RT "GRK1 and GRK7: unique cellular distribution and widely different
RT activities of opsin phosphorylation in the zebrafish rods and cones.";
RL J. Neurochem. 98:824-837(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Retina-specific kinase involved in the shutoff of the
CC photoresponse and adaptation to changing light conditions via cone
CC opsin phosphorylation, including rhodopsin (RHO).
CC {ECO:0000269|PubMed:16787417}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[rhodopsin] = ADP + H(+) + O-phospho-L-
CC threonyl-[rhodopsin]; Xref=Rhea:RHEA:56552, Rhea:RHEA-COMP:14596,
CC Rhea:RHEA-COMP:14597, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.14; Evidence={ECO:0000269|PubMed:16787417};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[rhodopsin] = ADP + H(+) + O-phospho-L-seryl-
CC [rhodopsin]; Xref=Rhea:RHEA:23356, Rhea:RHEA-COMP:14594, Rhea:RHEA-
CC COMP:14595, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.14;
CC Evidence={ECO:0000269|PubMed:16787417};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8WMV0}; Lipid-
CC anchor {ECO:0000250|UniProtKB:Q8WMV0}.
CC -!- TISSUE SPECIFICITY: Expressed in the eyes (at protein level). Expressed
CC in the eyes, the pineal gland and in the brain.
CC {ECO:0000269|PubMed:16787417}.
CC -!- PTM: Phosphorylation at Ser-33 is regulated by light and activated by
CC cAMP. {ECO:0000250|UniProtKB:B6CZ18}.
CC -!- MISCELLANEOUS: Although the protein is present in a diversity of
CC vertebrates ranging from bony fish to mammals, the mouse and rat
CC orthologous proteins do not exist.
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; AB212996; BAE92859.1; -; mRNA.
DR EMBL; BC162212; AAI62212.1; -; mRNA.
DR EMBL; BC162221; AAI62221.1; -; mRNA.
DR AlphaFoldDB; Q1XHL7; -.
DR SMR; Q1XHL7; -.
DR STRING; 7955.ENSDARP00000072364; -.
DR PaxDb; Q1XHL7; -.
DR PRIDE; Q1XHL7; -.
DR Ensembl; ENSDART00000077898; ENSDARP00000072364; ENSDARG00000055534.
DR ZFIN; ZDB-GENE-030904-3; grk7b.
DR eggNOG; KOG0986; Eukaryota.
DR GeneTree; ENSGT00940000160511; -.
DR HOGENOM; CLU_000288_63_41_1; -.
DR InParanoid; Q1XHL7; -.
DR OMA; TLEDECQ; -.
DR PhylomeDB; Q1XHL7; -.
DR TreeFam; TF313940; -.
DR BRENDA; 2.7.11.14; 928.
DR PRO; PR:Q1XHL7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 18.
DR Bgee; ENSDARG00000055534; Expressed in retina and 13 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004703; F:G protein-coupled receptor kinase activity; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0050254; F:rhodopsin kinase activity; IDA:ZFIN.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0009966; P:regulation of signal transduction; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
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; 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 1: Evidence at protein level;
KW ATP-binding; Kinase; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Phosphoprotein; Prenylation; Reference proteome;
KW Sensory transduction; Serine/threonine-protein kinase; Transferase; Vision.
FT CHAIN 1..545
FT /note="Rhodopsin kinase grk7-b"
FT /id="PRO_0000412814"
FT PROPEP 546..548
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000412815"
FT DOMAIN 53..172
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT DOMAIN 187..446
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 447..512
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 520..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 312
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 193..201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 33
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:B6CZ18"
FT MOD_RES 545
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 545
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000255"
FT CONFLICT 47
FT /note="V -> A (in Ref. 1; BAE92859 and 2; AAI62212)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="N -> D (in Ref. 1; BAE92859 and 2; AAI62212/
FT AAI62221)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="R -> Q (in Ref. 1; BAE92859 and 2; AAI62212/
FT AAI62221)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="V -> A (in Ref. 1; BAE92859 and 2; AAI62212/
FT AAI62221)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 548 AA; 62609 MW; 939D0B13095FECF2 CRC64;
MSDMGGLKNL VANTDYLKAQ SLDEKEIKKR RCSLGLPHLG NCTDVRVSVS KGFEDICEQQ
PIGRACFRQF LSVSSPEYLA AAELLDELNC WNLAEAEAKE EARLNIINKF CKADSKSFLA
FLTEDEAEKC KAVSEKDFEE VMMGQVKEAT QKFLRGQPFE EYQTSLFFDR FVQWKKFEKQ
PITDKYFYEF RTLGKGGFGE VCGVQVKTTG QMYACKKLDK KRLKKKSGEK MALLEKKILE
MVNSLFIVNL AYAFDTKTHL CLVMTLMSGG DLKYHIFHVG EVGIEMERII HYTAQITSGI
LHLHSMDIVY RDMKPENVLL DCQGQCRLSD LGLAVELPNG KTTTQKAGTK GYMAPEILKQ
EPYRTSVDWW ALGCSIYEMV AGRVPFRDHK EKVAKEELLR RTLEDEVKFE HRNFDAPSKD
IISLFLKRNI EDRLGSNDDP RKHEFFKSIN FPRLEAGLIP PPWEPKANVV YAKDTGDIRE
FSDVKGVKFD ANDEKFFKEF STGVVPIAWQ QEMIDSGLFD ELSDPNRKES AAGLEDEEQQ
KSKSCTLL