P32866 (GPRK2_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
G protein-coupled receptor kinase 2
EC=2.7.11.16

Gene names

Name:	Gprk2
Synonyms:	Gprk-2
ORF Names:	CG17998

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	714 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Differentiation Oogenesis
Cellular component	Membrane
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW oogenesis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW G-protein coupled receptor kinase activity Inferred from electronic annotation. Source: EC signal transducer activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 714	714	G protein-coupled receptor kinase 2		PRO_0000085966
Regions
	Domain	53 – 174	122	RGS 1
	Domain	177 – 294	118	RGS 2
	Domain	309 – 574	266	Protein kinase
	Domain	577 – 642	66	AGC-kinase C-terminal
	Nucleotide binding	315 – 323	9	ATP By similarity
	Region	1 – 308	308	N-terminal
	Compositional bias	139 – 170	32	Asn-rich
Sites
	Active site	435	1	Proton acceptor By similarity
	Binding site	338	1	ATP By similarity
Amino acid modifications
	Modified residue	612	1	Phosphoserine Ref.7
	Modified residue	613	1	Phosphothreonine Ref.7
Experimental info
	Sequence conflict	70	1	F → C in AAB61467. Ref.1
	Sequence conflict	206	1	S → N in AAA28589. Ref.6
	Sequence conflict	232	1	P → H in AAB61467. Ref.1
	Sequence conflict	232	1	P → H in AAA28589. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P32866 [UniParc]. Last modified April 14, 2009. Version 3. Checksum: 103F853BC74CFD80	FASTA	714	80,686
	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

References

	« Hide 'large scale' referencesShow '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: 9217001] [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: 10731132] [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. , 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: 12537572] [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: 12537569] [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: 1662381] [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: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-612 AND THR-613, 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.
PIR	B41615.
RefSeq	NP_476867.1. NM_057519.3.
UniGene	Dm.4430.
3D structure databases
ProteinModelPortal	P32866.
SMR	P32866. Positions 2-681.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-822642.
STRING	P32866.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0085788; FBpp0085149; FBgn0261988.
GeneID	49045.
KEGG	dme:Dmel_CG17998.
Organism-specific databases
CTD	49045.
FlyBase	FBgn0261988. Gprk2.
Phylogenomic databases
eggNOG	inNOG07455.
GeneTree	EMGT00050000001096.
InParanoid	P32866.
OMA	NFYTKFN.
OrthoDB	EOG4H44JT.
PhylomeDB	P32866.
Enzyme and pathway databases
BRENDA	2.7.11.15. 1994.
Gene expression databases
ArrayExpress	P32866.
Bgee	P32866.
GermOnline	CG17998. Drosophila melanogaster.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR000239. GPCR_kinase. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR000342. Regulat_G_prot_signal. IPR016137. Regulat_G_prot_signal_superfam. IPR017442. Se/Thr_kinase-like_dom. IPR002290. Ser/Thr_kinase_dom. [Graphical view]
KO	K08291.
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
PRINTS	PR00717. GPCRKINASE.
SMART	SM00315. RGS. 1 hit. SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit. SSF48097. Regulat_G_prot_signal_superfam. 1 hit.
PROSITE	PS51285. AGC_KINASE_CTER. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. False negative. PS50132. RGS. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	839614.

Entry information

Entry name

GPRK2_DROME

Accession

Primary (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:	January 25, 2012
This is version 107 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project