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P32866 (GPRK2_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
G protein-coupled receptor kinase 2

EC=2.7.11.16
Gene names
Name:Gprk2
Synonyms:Gprk-2
ORF Names:CG17998
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length714 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Catalytic activity

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

Subcellular location

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

Tissue specificity

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. Ref.1

Developmental stage

Expressed both maternally and zygotically. Ref.1

Disruption phenotype

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. Ref.1

Sequence similarities

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. GPRK subfamily.

Contains 1 AGC-kinase C-terminal domain.

Contains 1 protein kinase domain.

Contains 2 RGS domains.

Sequence caution

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

The sequence AAK93373.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processDifferentiation
Oogenesis
   Cellular componentMembrane
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapical constriction involved in gastrulation

Inferred from mutant phenotype PubMed 24026125. Source: FlyBase

defense response to Gram-positive bacterium

Inferred from mutant phenotype PubMed 20421637. Source: FlyBase

imaginal disc-derived wing vein specification

Inferred from mutant phenotype PubMed 19850026. Source: FlyBase

negative regulation of smoothened signaling pathway

Inferred from genetic interaction PubMed 22096079. Source: FlyBase

oogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of cAMP-mediated signaling

Inferred from genetic interaction PubMed 22096079. Source: FlyBase

protein phosphorylation

Inferred from sequence or structural similarity Ref.6. Source: FlyBase

regulation of Toll signaling pathway

Inferred from genetic interaction PubMed 20421637. Source: FlyBase

regulation of antimicrobial peptide biosynthetic process

Inferred from mutant phenotype PubMed 20421637. Source: FlyBase

regulation of smoothened signaling pathway

Inferred from direct assay PubMed 19850026. Source: FlyBase

signal transduction

Inferred from sequence or structural similarity Ref.6. Source: FlyBase

smoothened signaling pathway

Inferred from mutant phenotype PubMed 17483466. Source: FlyBase

termination of G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from direct assay Ref.1. Source: FlyBase

plasma membrane

Inferred from direct assay Ref.1. Source: FlyBase

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

G-protein coupled receptor kinase activity

Inferred from mutant phenotype Ref.1. Source: FlyBase

protein serine/threonine kinase activity

Non-traceable author statement PubMed 10908587. Source: FlyBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 714714G protein-coupled receptor kinase 2
PRO_0000085966

Regions

Domain53 – 174122RGS 1
Domain177 – 294118RGS 2
Domain309 – 574266Protein kinase
Domain577 – 64266AGC-kinase C-terminal
Nucleotide binding315 – 3239ATP By similarity
Region1 – 308308N-terminal
Compositional bias139 – 17032Asn-rich

Sites

Active site4351Proton acceptor By similarity
Binding site3381ATP By similarity

Amino acid modifications

Modified residue6121Phosphoserine Ref.7
Modified residue6131Phosphothreonine Ref.7

Experimental info

Sequence conflict701F → C in AAB61467. Ref.1
Sequence conflict2061S → N in AAA28589. Ref.6
Sequence conflict2321P → H in AAB61467. Ref.1
Sequence conflict2321P → H in AAA28589. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P32866 [UniParc].

Last modified April 14, 2009. Version 3.
Checksum: 103F853BC74CFD80

FASTA71480,686
        10         20         30         40         50         60 
MELENIVANT VYLKAREGGS DSNKGKSKKW RKILQFPHIS QCINLKDKLD ISYGYVIDQQ 

        70         80         90        100        110        120 
PIGRELFRLF CENKRPVYFR YITFLDEVVK YEIEYISNRI FIGHDIGRRF LDVEAQLELR 

       130        140        150        160        170        180 
NGSGGDALDA ETQEELLLNS SNANPTETAE TEHCNNTTAN NCNNINNSNN SQHSSDINHK 

       190        200        210        220        230        240 
KLDTRNHNGD DATGNGSSHQ DDGDESVKCQ EGHDDAEKGG GGEGGGGGKC VPVGGYPDEL 

       250        260        270        280        290        300 
VLDVLNDDLI AQVRNKLNSG GKDIFAQCVN AVKAFLAGEP FREFESSMYF HRYLQWKWLE 

       310        320        330        340        350        360 
AQPITYKTFR MYRVLGKGGF GEVCACQVRA TGKMYACKKL EKKRIKKRKG ESMVLIEKQI 

       370        380        390        400        410        420 
LQKINSPFVV NLAYAYETKD ALCLVLTIMN GGDLKFHIYN MGGEPGFELE RARFYAAEVA 

       430        440        450        460        470        480 
CGLQHLHKQG IVYRDCKPEN ILLDDHGHVR ISDLGLAVEI PEGEMVRGRV GTVGYMAPEV 

       490        500        510        520        530        540 
IDNEKYAFSP DWFSFGCLLY EMIEGQAPFR MRKEKVKREE VDRRVKEDPE KYSSKFNDEA 

       550        560        570        580        590        600 
KSMCQQLLAK SIKQRLGCRN GRMGGQDVMA HPFFHSTQLN WRRLEAGMLE PPFVPDPHAV 

       610        620        630        640        650        660 
YAKDVLDIEQ FSTVKGVNID ESDTNFYTKF NTGSVSISWQ NEMMETECFR ELNVFGPEEC 

       670        680        690        700        710 
PTPDLQINAA PEPDKAGCFP FRRKKKQPAR TQPIPIPEHL LTTSHSVSST TVES 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
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]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRB41615.
RefSeqNP_001263143.1. NM_001276214.1.
NP_476867.1. NM_057519.4.
UniGeneDm.4430.

3D structure databases

ProteinModelPortalP32866.
SMRP32866. Positions 2-681.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid71932. 2 interactions.
MINTMINT-822642.

Proteomic databases

PaxDbP32866.
PRIDEP32866.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0085788; FBpp0085149; FBgn0261988.
GeneID49045.
KEGGdme:Dmel_CG17998.

Organism-specific databases

CTD49045.
FlyBaseFBgn0261988. Gprk2.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00730000110512.
InParanoidQ960P0.
KOK08291.
OMAEMMETEC.
OrthoDBEOG7V1FQK.
PhylomeDBP32866.

Enzyme and pathway databases

BRENDA2.7.11.15. 1994.
SignaLinkP32866.

Gene expression databases

BgeeP32866.

Family and domain databases

InterProIPR000961. 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]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSPR00717. GPCRKINASE.
SMARTSM00315. RGS. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF48097. SSF48097. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS50132. RGS. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGprk2. drosophila.
GenomeRNAi49045.
NextBio839614.
PROP32866.

Entry information

Entry nameGPRK2_DROME
AccessionPrimary (citable) accession number: P32866
Secondary accession number(s): A9UN94, Q960P0, Q9V9X6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: April 14, 2009
Last modified: April 16, 2014
This is version 125 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase