GRK7B_XENLA
ID GRK7B_XENLA Reviewed; 550 AA.
AC B6CZ18;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Rhodopsin kinase grk7-b;
DE EC=2.7.11.14 {ECO:0000250|UniProtKB:Q8WTQ7};
DE AltName: Full=G protein-coupled receptor kinase 7B;
DE Flags: Precursor;
GN Name=grk7-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND PHOSPHORYLATION AT
RP SER-36.
RX PubMed=18803695; DOI=10.1111/j.1471-4159.2008.05691.x;
RA Osawa S., Jo R., Weiss E.R.;
RT "Phosphorylation of GRK7 by PKA in cone photoreceptor cells is regulated by
RT light.";
RL J. Neurochem. 107:1314-1324(2008).
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:0000250|UniProtKB:Q8WTQ7}.
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:0000250|UniProtKB:Q8WTQ7};
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:0000250|UniProtKB:Q8WTQ7};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8WMV0}; Lipid-
CC anchor {ECO:0000250|UniProtKB:Q8WMV0}.
CC -!- TISSUE SPECIFICITY: Retina, cones. {ECO:0000269|PubMed:18803695}.
CC -!- PTM: Autophosphorylated in vitro at Ser-487 (By similarity).
CC Phosphorylation at Ser-36 is regulated by light and activated by cAMP.
CC {ECO:0000250, ECO:0000269|PubMed:18803695}.
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; EU621674; ACF28431.1; -; mRNA.
DR RefSeq; NP_001131052.1; NM_001137580.1.
DR AlphaFoldDB; B6CZ18; -.
DR SMR; B6CZ18; -.
DR iPTMnet; B6CZ18; -.
DR GeneID; 100192359; -.
DR KEGG; xla:100192359; -.
DR CTD; 100192359; -.
DR Xenbase; XB-GENE-6252064; grk7.S.
DR OMA; LDAKGQC; -.
DR OrthoDB; 1104340at2759; -.
DR Proteomes; UP000186698; Chromosome 5S.
DR Bgee; 100192359; Expressed in camera-type eye and 2 other tissues.
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:0050254; F:rhodopsin kinase activity; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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; 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; 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..547
FT /note="Rhodopsin kinase grk7-b"
FT /id="PRO_0000412818"
FT PROPEP 548..550
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000412819"
FT DOMAIN 57..174
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT DOMAIN 189..451
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 452..517
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 22..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 314
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 195..203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18803695"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 547
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 547
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 550 AA; 62493 MW; 86F610D8275855CF CRC64;
MCDMGGLDNL IANTAYLQAR KSSEGDAKEL QKRRKSLSLP PPDVSRNEVK ETITLDYQSI
CVEQPIGQRL FKDFLATVPE YKLAEDFLEE VKEWELEEGS AKEQLMEKLV SRRFKEPAEG
SLNFLGKDLS SRIQQAQSKD MPELILLAKD SGNAFLMDAP FQDFQNSPFY DRFLQWKAFE
RQPINQKYFY EFRILGKGGF GEVCAIQVKN TGQMYACKKL DKKRLKKKNG EKMALLEKEI
LEKVHSPFIV SLAYAYETKT HLCLVMSLMN GGDLKFHIYN VGDKGVEIKR VIFYSAQICC
GILHLHSLKI VYRDMKPENV LLDDHGNCRL SDLGLAVKVK EGKAITQRAG TNGYMAPEIL
TDEDYSYPVD WFAMGCSIFE MIAAYTPFRD PKEKTSKEEL KRKTLEDEVV FPLPTFTEEA
KDICRLFLAK KPQNRLGSRT NDDDPRKHAF FKSINFQRLE AGMVDPPFVP DPSVVYAKDI
SDIADFSEVK GIEFDDKDAK LFKRFSTGAV PISWQKEIID TGLFDELNDP SREVTGGGNS
GEKSGVCSIL
