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Q49HM9

- GRK7A_DANRE

UniProt

Q49HM9 - GRK7A_DANRE

Protein

G-protein-coupled receptor kinase 7A

Gene

grk7a

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 2 (21 Sep 2011)
      Previous versions | rss
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    Functioni

    Retina-specific kinase involved in the shutoff of the photoresponse and adaptation to changing light conditions via cone opsin phosphorylation, including rhodopsin (RHO).1 Publication

    Catalytic activityi

    ATP + [G-protein-coupled receptor] = ADP + [G-protein-coupled receptor] phosphate.1 Publication
    ATP + [rhodopsin] = ADP + [rhodopsin] phosphate.1 Publication

    Kineticsi

    1. KM=4.4 µM for rhodopsin1 Publication

    Vmax=773 nmol/min/mg enzyme1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei215 – 2151ATPPROSITE-ProRule annotation
    Active sitei311 – 3111Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi192 – 2009ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. G-protein coupled receptor kinase activity Source: UniProtKB-EC
    3. photoreceptor activity Source: ZFIN
    4. rhodopsin kinase activity Source: ZFIN

    GO - Biological processi

    1. phototransduction, visible light Source: ZFIN
    2. termination of G-protein coupled receptor signaling pathway Source: InterPro
    3. visual perception Source: ZFIN

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Sensory transduction, Vision

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.14. 96826.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    G-protein-coupled receptor kinase 7A (EC:2.7.11.14, EC:2.7.11.16)
    Alternative name(s):
    G protein-coupled receptor kinase 7-1
    Gene namesi
    Name:grk7a
    Synonyms:grk7-1
    ORF Names:dkeyp-13a3.1
    OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
    Taxonomic identifieri7955 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
    ProteomesiUP000000437: Chromosome 2

    Organism-specific databases

    ZFINiZDB-GENE-050824-1. grk7a.

    Subcellular locationi

    Membrane By similarity; Lipid-anchor By similarity

    GO - Cellular componenti

    1. membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Impaired cone response recovery and delayed dark adaptation.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 546546G-protein-coupled receptor kinase 7APRO_0000412812Add
    BLAST
    Propeptidei547 – 5493Removed in mature formBy similarityPRO_0000412813

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei33 – 331PhosphoserineBy similarity
    Modified residuei546 – 5461Cysteine methyl esterSequence Analysis
    Lipidationi546 – 5461S-geranylgeranyl cysteineSequence Analysis

    Post-translational modificationi

    Phosphorylation at Ser-33 is regulated by light and activated by cAMP.By similarity

    Keywords - PTMi

    Lipoprotein, Methylation, Phosphoprotein, Prenylation

    Expressioni

    Gene expression databases

    BgeeiQ49HM9.

    Interactioni

    Protein-protein interaction databases

    STRINGi7955.ENSDARP00000091060.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini53 – 171119RGSPROSITE-ProRule annotationAdd
    BLAST
    Domaini186 – 449264Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini450 – 51566AGC-kinase C-terminalAdd
    BLAST

    Sequence similaritiesi

    Contains 1 AGC-kinase C-terminal domain.Curated
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 RGS domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00730000110751.
    HOGENOMiHOG000006742.
    HOVERGENiHBG004532.
    KOiK00909.
    OMAiAYAFESK.
    OrthoDBiEOG7V1FQK.
    TreeFamiTF313940.

    Family and domain databases

    InterProiIPR000961. AGC-kinase_C.
    IPR000239. GPCR_kinase.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR016137. Regulat_G_prot_signal_superfam.
    IPR000342. RGS_dom.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    PF00615. RGS. 1 hit.
    [Graphical view]
    PRINTSiPR00717. GPCRKINASE.
    SMARTiSM00315. RGS. 1 hit.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF48097. SSF48097. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS50132. RGS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q49HM9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MCDMGGLDNL VANTAYLKAQ GGDDKEMKKR RRSLSLPKPE QCASLRTSLD    50
    KDFESLCEKQ PIGKKLFRQY LSQGGPECTT AAEFLDDLNE WELSESAARD 100
    KARTNIINKF CKEGSKSSLT FLTGDVATKC KAVSDKDFEE VMGQVKTATK 150
    EFLKGKPFTE YQASPFFDKF LQWKEYEKQP ISEKYFYEFR TLGKGGFGEV 200
    CAVQVKNTGQ MYACKKLCKK RLKKKHGEKM ALLEKKILER VNSLFIVSLA 250
    YAYDTKTHLC LVMSLMNGGD LKYHIYNIGE KGIEMDRIIY YTAQIATGIL 300
    HLHDMDIVYR DMKPENVLLD SQGQCRLSDL GLAVEIAVGK TISQKAGTGA 350
    YMAPEILNET PYRTSVDWWA LGCSIYEMVA GYTPFKGPDA KKEKVEKEEV 400
    QRRILNEEPK FEHKNFDAAT IDIIKQFLKK KIDERLGCKN DDPRKHEWFK 450
    SINFARLEAG LIDPPWVPKP NVVYAKDTGD IAEFSEIKGI EFDAKDDKFF 500
    KEFSTGAVSI AWQQEMIDTG LFDELSDPNR KESSGGSDDD KKSGTCTLL 549
    Length:549
    Mass (Da):62,232
    Last modified:September 21, 2011 - v2
    Checksum:i3F76C291F8BC9716
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti80 – 801T → I in AAX69081. (PubMed:16039565)Curated
    Sequence conflicti385 – 3851F → I in AAX69081. (PubMed:16039565)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY900004 mRNA. Translation: AAX69081.1.
    AB212995 mRNA. Translation: BAE92858.1.
    CR377211 Genomic DNA. Translation: CAQ13370.1.
    BC163587 mRNA. Translation: AAI63587.1.
    RefSeqiNP_001027011.2. NM_001031841.3.
    UniGeneiDr.82672.

    Genome annotation databases

    EnsembliENSDART00000100287; ENSDARP00000091060; ENSDARG00000020602.
    GeneIDi566120.
    KEGGidre:566120.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY900004 mRNA. Translation: AAX69081.1 .
    AB212995 mRNA. Translation: BAE92858.1 .
    CR377211 Genomic DNA. Translation: CAQ13370.1 .
    BC163587 mRNA. Translation: AAI63587.1 .
    RefSeqi NP_001027011.2. NM_001031841.3.
    UniGenei Dr.82672.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 7955.ENSDARP00000091060.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSDART00000100287 ; ENSDARP00000091060 ; ENSDARG00000020602 .
    GeneIDi 566120.
    KEGGi dre:566120.

    Organism-specific databases

    CTDi 566120.
    ZFINi ZDB-GENE-050824-1. grk7a.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00730000110751.
    HOGENOMi HOG000006742.
    HOVERGENi HBG004532.
    KOi K00909.
    OMAi AYAFESK.
    OrthoDBi EOG7V1FQK.
    TreeFami TF313940.

    Enzyme and pathway databases

    BRENDAi 2.7.11.14. 96826.

    Miscellaneous databases

    NextBioi 20888040.
    PROi Q49HM9.

    Gene expression databases

    Bgeei Q49HM9.

    Family and domain databases

    InterProi IPR000961. AGC-kinase_C.
    IPR000239. GPCR_kinase.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR016137. Regulat_G_prot_signal_superfam.
    IPR000342. RGS_dom.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    PF00615. RGS. 1 hit.
    [Graphical view ]
    PRINTSi PR00717. GPCRKINASE.
    SMARTi SM00315. RGS. 1 hit.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48097. SSF48097. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS50132. RGS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Knockdown of cone-specific kinase GRK7 in larval zebrafish leads to impaired cone response recovery and delayed dark adaptation."
      Rinner O., Makhankov Y.V., Biehlmaier O., Neuhauss S.C.
      Neuron 47:231-242(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE.
    2. "GRK1 and GRK7: unique cellular distribution and widely different activities of opsin phosphorylation in the zebrafish rods and cones."
      Wada Y., Sugiyama J., Okano T., Fukada Y.
      J. Neurochem. 98:824-837(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
    3. "The zebrafish reference genome sequence and its relationship to the human genome."
      Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.
      , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
      Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Tuebingen.
    4. NIH - Zebrafish Gene Collection (ZGC) project
      Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

    Entry informationi

    Entry nameiGRK7A_DANRE
    AccessioniPrimary (citable) accession number: Q49HM9
    Secondary accession number(s): Q1XHL8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 21, 2011
    Last sequence update: September 21, 2011
    Last modified: October 1, 2014
    This is version 73 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Although the protein is present in a diversity of vertebrates ranging from bony fish to mammals, the mouse and rat orthologous proteins do not exist.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3