GRK7A_XENLA
ID GRK7A_XENLA Reviewed; 551 AA.
AC B6CZ17;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Rhodopsin kinase grk7-a;
DE EC=2.7.11.14 {ECO:0000250|UniProtKB:Q8WTQ7};
DE AltName: Full=G protein-coupled receptor kinase 7A;
DE Flags: Precursor;
GN Name=grk7-a;
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], AND PHOSPHORYLATION AT 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 -!- 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; EU621673; ACF28430.1; -; mRNA.
DR RefSeq; NP_001131051.1; NM_001137579.1.
DR AlphaFoldDB; B6CZ17; -.
DR SMR; B6CZ17; -.
DR iPTMnet; B6CZ17; -.
DR PRIDE; B6CZ17; -.
DR GeneID; 100192358; -.
DR KEGG; xla:100192358; -.
DR CTD; 100192358; -.
DR Xenbase; XB-GENE-6055238; grk7.L.
DR OMA; VFEMQPV; -.
DR OrthoDB; 1104340at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 100192358; Expressed in camera-type eye and 3 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..548
FT /note="Rhodopsin kinase grk7-a"
FT /id="PRO_0000412816"
FT PROPEP 549..551
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000412817"
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 529..551
FT /note="Disordered"
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 548
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 548
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 551 AA; 62693 MW; 87140A98514D7022 CRC64;
MCDMGGLDNL IANTAYLQAR KNSEGDVKEL QKRRKSLSLP STDVSRKEIK ETITLDYQSI
CVEQPIGQRL FRDFLGTVSE YKLAEEFLEE VKEWELEEGS AKEQLMEKLV SRRFKEPAEG
SLNFLGKDLS SRIQQAQSKD MPELILLAKD AGNAFLMDAP FQDFQNSPFY DRFLQWKAFE
RQPINQKYFY EFRILGKGGF GEVCAIQVKN TGQMYACKKL DKKRLKKKNG EKMALLEKEI
LEKVHSPFIV SLAYAYETKT HLCLVMSLMN GGDLKFHIYN IGEKGIEIKR VIFYSAQICC
GILHLHSLKI LYRDMKPENV LLDDNGNCRL SDLGLAVKVK EGKPITQRAG TNGYMAPEIL
TDVDYSYPVD WFAMGCSIYE MIAGHTPFRD PKEKTSKEEV KRKTIEDEVV FQHPVFTEEA
KDICRLFLAK KPQNRLGSRT NDDDPRKHAF FKSINFQRLE AGMVDPPFVP DPSVVYAKDI
SDIADFSEVK GIEFDDKDSK FFKRFATGAI PISWQKEIID TGLFDELNDP SREATGGGGN
SGEKSGVCSI L
