P23696 (PP2A_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein phosphatase PP2A
EC=3.1.3.16

Alternative name(s):
Protein microtubule star

Gene names

Name:	mts
Synonyms:	PP2A, Pp2A-28D
ORF Names:	CG7109

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	309 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	A phosphoprotein + H2O = a protein + phosphate.
Cofactor	Binds 1 iron ion per subunit By similarity. Binds 1 manganese ion per subunit By similarity.
Sequence similarities	Belongs to the PPP phosphatase family. PP-2A subfamily.

Ontologies

Keywords
Ligand	Iron Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	R7 cell fate commitment Inferred from genetic interaction PubMed 8595878. Source: FlyBase actin filament organization Inferred from mutant phenotype PubMed 14527345. Source: FlyBase asymmetric neuroblast division Inferred from genetic interaction PubMed 19690050. Source: FlyBase canonical Wnt receptor signaling pathway Inferred from mutant phenotype PubMed 19556239. Source: FlyBase cell adhesion Inferred from mutant phenotype PubMed 14527345. Source: FlyBase centrosome duplication Inferred from mutant phenotype PubMed 20818332. Source: FlyBase chromosome segregation Inferred from mutant phenotype PubMed 17306545. Source: FlyBase establishment of epithelial cell polarity Inferred from expression pattern PubMed 19690050. Source: FlyBase mitosis Inferred from mutant phenotype PubMed 9004035. Source: FlyBase mitotic cell cycle Inferred from mutant phenotype PubMed 17306545. Source: FlyBase negative regulation of neuroblast proliferation Inferred from mutant phenotype PubMed 19502489. Source: FlyBase oogenesis Inferred from mutant phenotype PubMed 8595878. Source: FlyBase phagocytosis, engulfment Inferred from mutant phenotype PubMed 16336044. Source: FlyBase positive regulation of smoothened signaling pathway Inferred from genetic interaction PubMed 18245841. Source: FlyBase protein dephosphorylation Inferred from mutant phenotype PubMed 9004035. Source: FlyBase regulation of cell shape Inferred from mutant phenotype PubMed 14527345. Source: FlyBase response to light stimulus Inferred from genetic interaction PubMed 18256265. Source: FlyBase spindle assembly Inferred from mutant phenotype PubMed 17306545. Source: FlyBase
Cellular_component	centriole Inferred from direct assay PubMed 18798690. Source: FlyBase protein phosphatase type 2A complex Inferred from sequence or structural similarity PubMed 1320961. Source: FlyBase
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphatase regulator activity Inferred from direct assay PubMed 18256265. Source: FlyBase protein serine/threonine phosphatase activity Inferred from mutant phenotype PubMed 9004035. Source: FlyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 309	309	Serine/threonine-protein phosphatase PP2A		PRO_0000058850
Sites
	Active site	118	1	Proton donor By similarity
	Metal binding	57	1	Iron By similarity
	Metal binding	59	1	Iron By similarity
	Metal binding	85	1	Iron By similarity
	Metal binding	85	1	Manganese By similarity
	Metal binding	117	1	Manganese By similarity
	Metal binding	167	1	Manganese By similarity
	Metal binding	241	1	Manganese By similarity

Sequences

	Sequence		Length	Mass (Da)
	P23696 [UniParc]. Last modified November 1, 1991. Version 1. Checksum: 6F1E2486A514FBAF	FASTA	309	35,469
	10 20 30 40 50 60 MEDKATTKDL DQWIEQLNEC NQLTETQVRT LCDKAKEILS KESNVQEVKC PVTVCGDVHG 70 80 90 100 110 120 QFHDLMELFR IGGKSPDTNY LFMGDYVDRG YYSVETVTLL VALKVRYRER ITILRGNHES 130 140 150 160 170 180 RQITQVYGFY DECLRKYGNA NVWKYFTDLF DYLPLTALVD GQIFCLHGGL SPSIDSLDHI 190 200 210 220 230 240 RALDRLQEVP HEGPMCDLLW SDPDDRGGWG ISPRGAGYTF GQDISETFNN TNGLTLVSRA 250 260 270 280 290 300 HQLVMEGYNW CHDRNVVTIF SAPNYCYRCG NQAALMELDD SLKFSFLQFD PAPRRGEPHV TRRTPDYFL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The structure of protein phosphatase 2A is as highly conserved as that of protein phosphatase 1." Orgad S., Brewis N.D., Alphey L., Axton J.M., Dudai Y., Cohen P.T.W. FEBS Lett. 275:44-48(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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]	"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] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[4]	"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]. Strain: Berkeley. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X55199 mRNA. Translation: CAA38984.1. X78577 mRNA. Translation: CAA55315.1. AE014134 Genomic DNA. Translation: AAF52567.2. AY058571 mRNA. Translation: AAL13800.1.
PIR	S12961.
RefSeq	NP_476805.1. NM_057457.3.
UniGene	Dm.4245.
3D structure databases
ProteinModelPortal	P23696.
SMR	P23696. Positions 7-293.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-17814N.
IntAct	P23696. 4 interactions.
MINT	MINT-333628.
STRING	7227.FBpp0079148.
Proteomic databases
PaxDb	P23696.
PRIDE	P23696.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0079525; FBpp0079148; FBgn0004177.
GeneID	45959.
KEGG	dme:Dmel_CG7109.
Organism-specific databases
CTD	45959.
FlyBase	FBgn0004177. mts.
Phylogenomic databases
eggNOG	COG0639.
GeneTree	ENSGT00550000074618.
InParanoid	P23696.
KO	K04382.
OMA	TFNHANR.
OrthoDB	EOG4FXPQ4.
PhylomeDB	P23696.
Enzyme and pathway databases
SignaLink	P23696.
Gene expression databases
Bgee	P23696.
GermOnline	CG7109. Drosophila melanogaster.
Family and domain databases
InterPro	IPR004843. Metallo_PEstase_dom. IPR006186. Ser/Thr-sp_prot-phosphatase. [Graphical view]
Pfam	PF00149. Metallophos. 1 hit. [Graphical view]
PRINTS	PR00114. STPHPHTASE.
SMART	SM00156. PP2Ac. 1 hit. [Graphical view]
PROSITE	PS00125. SER_THR_PHOSPHATASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	mts. drosophila.
GenomeRNAi	45959.
NextBio	838521.

Entry information

Entry name

PP2A_DROME

Accession

Primary (citable) accession number: P23696
Secondary accession number(s): Q9VLW4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1991
Last modified:	May 29, 2013
This is version 120 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project