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P32866

- GPRK2_DROME

UniProt

P32866 - GPRK2_DROME

Protein

G protein-coupled receptor kinase 2

Gene

Gprk2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 3 (14 Apr 2009)
      Previous versions | rss
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    Functioni

    Specifically phosphorylates the activated forms of G protein-coupled receptors By similarity. Required during oogenesis and embryogenesis; component of a signaling pathway that functions during egg chamber maturation.By similarity1 Publication

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei338 – 3381ATPPROSITE-ProRule annotation
    Active sitei435 – 4351Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi315 – 3239ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. G-protein coupled receptor kinase activity Source: FlyBase
    3. protein serine/threonine kinase activity Source: FlyBase

    GO - Biological processi

    1. apical constriction involved in gastrulation Source: FlyBase
    2. defense response to Gram-positive bacterium Source: FlyBase
    3. imaginal disc-derived wing vein specification Source: FlyBase
    4. negative regulation of smoothened signaling pathway Source: FlyBase
    5. oogenesis Source: UniProtKB-KW
    6. positive regulation of cAMP-mediated signaling Source: FlyBase
    7. protein phosphorylation Source: FlyBase
    8. regulation of antimicrobial peptide biosynthetic process Source: FlyBase
    9. regulation of smoothened signaling pathway Source: FlyBase
    10. regulation of Toll signaling pathway Source: FlyBase
    11. signal transduction Source: FlyBase
    12. smoothened signaling pathway Source: FlyBase
    13. termination of G-protein coupled receptor signaling pathway Source: InterPro

    Keywords - Molecular functioni

    Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Differentiation, Oogenesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.15. 1994.
    SignaLinkiP32866.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    G protein-coupled receptor kinase 2 (EC:2.7.11.16)
    Gene namesi
    Name:Gprk2
    Synonyms:Gprk-2
    ORF Names:CG17998
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0261988. Gprk2.

    Subcellular locationi

    Membrane 1 Publication
    Note: Associated with nurse cell and oocyte plasma membranes during much of oogenesis.

    GO - Cellular componenti

    1. cytoplasm Source: FlyBase
    2. plasma membrane Source: FlyBase

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Adult females show severely reduced number of egg chambers and the small germarium in ovarioles. The rare eggs that become fertilized display gross defects in embryogenesis exhibiting fusion of adjacent segments and holes in the dorsal and ventral cuticle.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 714714G protein-coupled receptor kinase 2PRO_0000085966Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei612 – 6121Phosphoserine1 Publication
    Modified residuei613 – 6131Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP32866.
    PRIDEiP32866.

    Expressioni

    Tissue specificityi

    Expressed in all larval tissues and in adult ovaries. Larval CNS staining is localized to axons projecting to the optic lobes and the mushroom bodies, in the longitudinal connectives, and in cell bodies and nerves of the ring gland corpus allatum. Adult CNS staining is detectable only in cell bodies and processes associated with the ellipsoid body of the central complex and portions of the mushroom bodies. In the wing disk, expression is confined to a stripe that parallels the anterior/posterior boundary of the wing blade and the hinge region, and weak expression in the prospective notum.1 Publication

    Developmental stagei

    Expressed both maternally and zygotically.1 Publication

    Gene expression databases

    BgeeiP32866.

    Interactioni

    Protein-protein interaction databases

    BioGridi71932. 2 interactions.
    MINTiMINT-822642.

    Structurei

    3D structure databases

    ProteinModelPortaliP32866.
    SMRiP32866. Positions 2-677.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini53 – 174122RGS 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini177 – 294118RGS 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini309 – 574266Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini577 – 64266AGC-kinase C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 308308N-terminalAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi139 – 17032Asn-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 AGC-kinase C-terminal domain.Curated
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 2 RGS domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00730000110512.
    InParanoidiQ960P0.
    KOiK08291.
    OMAiEMMETEC.
    OrthoDBiEOG7V1FQK.
    PhylomeDBiP32866.

    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.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    [Graphical view]
    PfamiPF00069. Pkinase. 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. 2 hits.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS50132. RGS. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P32866-1 [UniParc]FASTAAdd to Basket

    « Hide

    MELENIVANT VYLKAREGGS DSNKGKSKKW RKILQFPHIS QCINLKDKLD    50
    ISYGYVIDQQ PIGRELFRLF CENKRPVYFR YITFLDEVVK YEIEYISNRI 100
    FIGHDIGRRF LDVEAQLELR NGSGGDALDA ETQEELLLNS SNANPTETAE 150
    TEHCNNTTAN NCNNINNSNN SQHSSDINHK KLDTRNHNGD DATGNGSSHQ 200
    DDGDESVKCQ EGHDDAEKGG GGEGGGGGKC VPVGGYPDEL VLDVLNDDLI 250
    AQVRNKLNSG GKDIFAQCVN AVKAFLAGEP FREFESSMYF HRYLQWKWLE 300
    AQPITYKTFR MYRVLGKGGF GEVCACQVRA TGKMYACKKL EKKRIKKRKG 350
    ESMVLIEKQI LQKINSPFVV NLAYAYETKD ALCLVLTIMN GGDLKFHIYN 400
    MGGEPGFELE RARFYAAEVA CGLQHLHKQG IVYRDCKPEN ILLDDHGHVR 450
    ISDLGLAVEI PEGEMVRGRV GTVGYMAPEV IDNEKYAFSP DWFSFGCLLY 500
    EMIEGQAPFR MRKEKVKREE VDRRVKEDPE KYSSKFNDEA KSMCQQLLAK 550
    SIKQRLGCRN GRMGGQDVMA HPFFHSTQLN WRRLEAGMLE PPFVPDPHAV 600
    YAKDVLDIEQ FSTVKGVNID ESDTNFYTKF NTGSVSISWQ NEMMETECFR 650
    ELNVFGPEEC PTPDLQINAA PEPDKAGCFP FRRKKKQPAR TQPIPIPEHL 700
    LTTSHSVSST TVES 714
    Length:714
    Mass (Da):80,686
    Last modified:April 14, 2009 - v3
    Checksum:i103F853BC74CFD80
    GO

    Sequence cautioni

    The sequence AAA28589.1 differs from that shown. Reason: Frameshift at position 279.
    The sequence AAK93373.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti70 – 701F → C in AAB61467. (PubMed:9217001)Curated
    Sequence conflicti206 – 2061S → N in AAA28589. (PubMed:1662381)Curated
    Sequence conflicti232 – 2321P → H in AAB61467. (PubMed:9217001)Curated
    Sequence conflicti232 – 2321P → H in AAA28589. (PubMed:1662381)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF004674 mRNA. Translation: AAB61467.1.
    AE014297 Genomic DNA. Translation: AAF57152.1.
    BT031258 mRNA. Translation: ABY20499.1.
    AY051949 mRNA. Translation: AAK93373.1. Different initiation.
    M80494 mRNA. Translation: AAA28589.1. Frameshift.
    PIRiB41615.
    RefSeqiNP_001263143.1. NM_001276214.1.
    NP_476867.1. NM_057519.4.
    UniGeneiDm.4430.

    Genome annotation databases

    EnsemblMetazoaiFBtr0085788; FBpp0085149; FBgn0261988.
    GeneIDi49045.
    KEGGidme:Dmel_CG17998.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF004674 mRNA. Translation: AAB61467.1 .
    AE014297 Genomic DNA. Translation: AAF57152.1 .
    BT031258 mRNA. Translation: ABY20499.1 .
    AY051949 mRNA. Translation: AAK93373.1 . Different initiation.
    M80494 mRNA. Translation: AAA28589.1 . Frameshift.
    PIRi B41615.
    RefSeqi NP_001263143.1. NM_001276214.1.
    NP_476867.1. NM_057519.4.
    UniGenei Dm.4430.

    3D structure databases

    ProteinModelPortali P32866.
    SMRi P32866. Positions 2-677.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 71932. 2 interactions.
    MINTi MINT-822642.

    Proteomic databases

    PaxDbi P32866.
    PRIDEi P32866.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0085788 ; FBpp0085149 ; FBgn0261988 .
    GeneIDi 49045.
    KEGGi dme:Dmel_CG17998.

    Organism-specific databases

    CTDi 49045.
    FlyBasei FBgn0261988. Gprk2.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00730000110512.
    InParanoidi Q960P0.
    KOi K08291.
    OMAi EMMETEC.
    OrthoDBi EOG7V1FQK.
    PhylomeDBi P32866.

    Enzyme and pathway databases

    BRENDAi 2.7.11.15. 1994.
    SignaLinki P32866.

    Miscellaneous databases

    ChiTaRSi Gprk2. drosophila.
    GenomeRNAii 49045.
    NextBioi 839614.
    PROi P32866.

    Gene expression databases

    Bgeei P32866.

    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.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    [Graphical view ]
    Pfami PF00069. Pkinase. 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. 2 hits.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS50132. RGS. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The Drosophila G-protein-coupled receptor kinase homologue Gprk2 is required for egg morphogenesis."
      Schneider L.E., Spradling A.C.
      Development 124:2591-2602(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
    2. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C., Celniker S.E.
      Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 112-714.
      Strain: Berkeley.
      Tissue: Embryo.
    6. "Isolation of Drosophila genes encoding G protein-coupled receptor kinases."
      Cassill J.A., Whitney M., Joazeiro C.A., Becker A., Zuker C.S.
      Proc. Natl. Acad. Sci. U.S.A. 88:11067-11070(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 201-714.
      Tissue: Retina.
    7. "Phosphoproteome analysis of Drosophila melanogaster embryos."
      Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
      J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-612 AND THR-613, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.

    Entry informationi

    Entry nameiGPRK2_DROME
    AccessioniPrimary (citable) accession number: P32866
    Secondary accession number(s): A9UN94, Q960P0, Q9V9X6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: April 14, 2009
    Last modified: October 1, 2014
    This is version 128 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3