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P32866

- GPRK2_DROME

UniProt

P32866 - GPRK2_DROME

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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

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. oocyte morphogenesis Source: FlyBase
  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
Complete GO annotation...

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.
ReactomeiREACT_212409. G alpha (q) signalling events.
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
Complete GO annotation...

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 2-111, 249-677.
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.
GeneTreeiENSGT00770000120493.
InParanoidiP32866.
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.
[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

        10         20         30         40         50
MELENIVANT VYLKAREGGS DSNKGKSKKW RKILQFPHIS QCINLKDKLD
60 70 80 90 100
ISYGYVIDQQ PIGRELFRLF CENKRPVYFR YITFLDEVVK YEIEYISNRI
110 120 130 140 150
FIGHDIGRRF LDVEAQLELR NGSGGDALDA ETQEELLLNS SNANPTETAE
160 170 180 190 200
TEHCNNTTAN NCNNINNSNN SQHSSDINHK KLDTRNHNGD DATGNGSSHQ
210 220 230 240 250
DDGDESVKCQ EGHDDAEKGG GGEGGGGGKC VPVGGYPDEL VLDVLNDDLI
260 270 280 290 300
AQVRNKLNSG GKDIFAQCVN AVKAFLAGEP FREFESSMYF HRYLQWKWLE
310 320 330 340 350
AQPITYKTFR MYRVLGKGGF GEVCACQVRA TGKMYACKKL EKKRIKKRKG
360 370 380 390 400
ESMVLIEKQI LQKINSPFVV NLAYAYETKD ALCLVLTIMN GGDLKFHIYN
410 420 430 440 450
MGGEPGFELE RARFYAAEVA CGLQHLHKQG IVYRDCKPEN ILLDDHGHVR
460 470 480 490 500
ISDLGLAVEI PEGEMVRGRV GTVGYMAPEV IDNEKYAFSP DWFSFGCLLY
510 520 530 540 550
EMIEGQAPFR MRKEKVKREE VDRRVKEDPE KYSSKFNDEA KSMCQQLLAK
560 570 580 590 600
SIKQRLGCRN GRMGGQDVMA HPFFHSTQLN WRRLEAGMLE PPFVPDPHAV
610 620 630 640 650
YAKDVLDIEQ FSTVKGVNID ESDTNFYTKF NTGSVSISWQ NEMMETECFR
660 670 680 690 700
ELNVFGPEEC PTPDLQINAA PEPDKAGCFP FRRKKKQPAR TQPIPIPEHL
710
LTTSHSVSST TVES
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. Curated
The sequence AAK93373.1 differs from that shown. Reason: Erroneous initiation. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 2-111, 249-677.
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 ENSGT00770000120493.
InParanoidi P32866.
KOi K08291.
OMAi EMMETEC.
OrthoDBi EOG7V1FQK.
PhylomeDBi P32866.

Enzyme and pathway databases

BRENDAi 2.7.11.15. 1994.
Reactomei REACT_212409. G alpha (q) signalling events.
SignaLinki P32866.

Miscellaneous databases

ChiTaRSi Gprk2. fly.
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.
[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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 130 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