2AAA_DROME
ID 2AAA_DROME Reviewed; 591 AA.
AC P36179; A4V0F7; Q2MGK6; Q5BI19; Q9VLN3;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Serine/threonine-protein phosphatase PP2A 65 kDa regulatory subunit;
DE AltName: Full=PR65;
DE AltName: Full=Protein phosphatase PP2A regulatory subunit A;
GN Name=Pp2A-29B; ORFNames=CG17291;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=1320961; DOI=10.1091/mbc.3.3.287;
RA Mayer-Jaekel R.E., Baumgartner S., Bilbe G., Ohkura H., Glover D.M.,
RA Hemmings B.A.;
RT "Molecular cloning and developmental expression of the catalytic and 65-kDa
RT regulatory subunits of protein phosphatase 2A in Drosophila.";
RL Mol. Biol. Cell 3:287-298(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The PR65 subunit of protein phosphatase 2A serves as a
CC scaffolding molecule to coordinate the assembly of the catalytic
CC subunit and a variable regulatory B subunit. {ECO:0000250}.
CC -!- SUBUNIT: PP2A exists in several trimeric forms, all of which consist of
CC a core composed of a catalytic subunit associated with a 65 kDa
CC regulatory subunit (PR65) (subunit A). The core complex associates with
CC a third, variable subunit (subunit B), which confers distinct
CC properties to the holoenzyme.
CC -!- TISSUE SPECIFICITY: Expression varies in tissues throughout
CC development. Highly distributed expression in early embryos. In late
CC embryonal development, found at high levels in nervous system and
CC gonads. In third instar larvae, found in brain, imaginal disks and
CC salivary glands. {ECO:0000269|PubMed:1320961}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expressed at lower levels in larvae and adult.
CC {ECO:0000269|PubMed:1320961}.
CC -!- DOMAIN: Each HEAT repeat appears to consist of two alpha helices joined
CC by a hydrophilic region, the intrarepeat loop. The repeat units may be
CC arranged laterally to form a rod-like structure.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX33553.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; M86442; AAA28304.1; -; mRNA.
DR EMBL; AE014134; AAF52650.2; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66587.1; -; Genomic_DNA.
DR EMBL; BT021405; AAX33553.1; ALT_SEQ; mRNA.
DR PIR; A43767; A43767.
DR RefSeq; NP_001027225.1; NM_001032054.3.
DR RefSeq; NP_001027226.1; NM_001032055.3.
DR RefSeq; NP_001027227.1; NM_001032056.3.
DR AlphaFoldDB; P36179; -.
DR SMR; P36179; -.
DR BioGRID; 77789; 82.
DR IntAct; P36179; 12.
DR STRING; 7227.FBpp0297239; -.
DR PaxDb; P36179; -.
DR PRIDE; P36179; -.
DR EnsemblMetazoa; FBtr0005088; FBpp0099974; FBgn0260439.
DR EnsemblMetazoa; FBtr0100533; FBpp0099975; FBgn0260439.
DR EnsemblMetazoa; FBtr0100535; FBpp0293227; FBgn0260439.
DR GeneID; 2768940; -.
DR KEGG; dme:Dmel_CG17291; -.
DR CTD; 2768940; -.
DR FlyBase; FBgn0260439; Pp2A-29B.
DR VEuPathDB; VectorBase:FBgn0260439; -.
DR eggNOG; KOG0211; Eukaryota.
DR GeneTree; ENSGT00950000183066; -.
DR HOGENOM; CLU_015533_2_1_1; -.
DR InParanoid; P36179; -.
DR OMA; SSLCMSW; -.
DR PhylomeDB; P36179; -.
DR Reactome; R-DME-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR Reactome; R-DME-1295596; Spry regulation of FGF signaling.
DR Reactome; R-DME-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-DME-196299; Beta-catenin phosphorylation cascade.
DR Reactome; R-DME-198753; ERK/MAPK targets.
DR Reactome; R-DME-202670; ERKs are inactivated.
DR Reactome; R-DME-209155; Phosphorylation of AXN and APC.
DR Reactome; R-DME-209190; Phosphorylation of CI.
DR Reactome; R-DME-209214; Phosphorylation of SMO.
DR Reactome; R-DME-209360; Ubiquitination and proteolysis of phosphorylated CI.
DR Reactome; R-DME-209396; Phosphorylation of ARM.
DR Reactome; R-DME-209413; Assembly of the 'destruction complex'.
DR Reactome; R-DME-209440; Recruitment of the 'destruction complex' to the receptor complex, the degradation of AXN and release of ARM.
DR Reactome; R-DME-209461; Ubiquitination and degradation of phosphorylated ARM.
DR Reactome; R-DME-2995383; Initiation of Nuclear Envelope (NE) Reformation.
DR Reactome; R-DME-432553; Phosphorylation of PER and TIM.
DR Reactome; R-DME-432620; Dephosphorylation of PER.
DR Reactome; R-DME-432626; Circadian Clock pathway.
DR Reactome; R-DME-69231; Cyclin D associated events in G1.
DR Reactome; R-DME-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-DME-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P36179; -.
DR BioGRID-ORCS; 2768940; 2 hits in 3 CRISPR screens.
DR GenomeRNAi; 2768940; -.
DR PRO; PR:P36179; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0260439; Expressed in wing disc and 20 other tissues.
DR ExpressionAtlas; P36179; baseline and differential.
DR Genevisible; P36179; DM.
DR GO; GO:0005814; C:centriole; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0090443; C:FAR/SIN/STRIPAK complex; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; ISS:FlyBase.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IMP:FlyBase.
DR GO; GO:0007099; P:centriole replication; IMP:FlyBase.
DR GO; GO:0007098; P:centrosome cycle; IMP:FlyBase.
DR GO; GO:0007059; P:chromosome segregation; IMP:FlyBase.
DR GO; GO:0035331; P:negative regulation of hippo signaling; IMP:FlyBase.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IMP:FlyBase.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:FlyBase.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:FlyBase.
DR GO; GO:0051225; P:spindle assembly; IMP:FlyBase.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR021133; HEAT_type_2.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 11.
PE 2: Evidence at transcript level;
KW Acetylation; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..591
FT /note="Serine/threonine-protein phosphatase PP2A 65 kDa
FT regulatory subunit"
FT /id="PRO_0000071408"
FT REPEAT 10..48
FT /note="HEAT 1"
FT REPEAT 49..86
FT /note="HEAT 2"
FT REPEAT 87..125
FT /note="HEAT 3"
FT REPEAT 126..163
FT /note="HEAT 4"
FT REPEAT 164..202
FT /note="HEAT 5"
FT REPEAT 203..241
FT /note="HEAT 6"
FT REPEAT 242..280
FT /note="HEAT 7"
FT REPEAT 281..323
FT /note="HEAT 8"
FT REPEAT 324..362
FT /note="HEAT 9"
FT REPEAT 363..401
FT /note="HEAT 10"
FT REPEAT 402..440
FT /note="HEAT 11"
FT REPEAT 441..479
FT /note="HEAT 12"
FT REPEAT 480..518
FT /note="HEAT 13"
FT REPEAT 519..557
FT /note="HEAT 14"
FT REPEAT 558..591
FT /note="HEAT 15"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250"
FT CONFLICT 232
FT /note="S -> T (in Ref. 1; AAA28304)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 591 AA; 65424 MW; 13948F39796662AC CRC64;
MAASDKSVDD SLYPIAVLID ELKNEDVQLR LNSIKKLSTI ALALGEERTR SELIPFLTET
IYDEDEVLLA LADQLGNFTS LVGGPEFAMY LIPPLESLAT VEETVVRDKA VESLRTVAAE
HSAQDLEIHV VPTLQRLVSG DWFTSRTSAC GLFSVCYPRV TQPVKAELRA NFRKLCQDET
PMVRRAAANK LGEFAKVVET EYLKSDLIPN FVQLAQDDQD SVRLLAVEAC VSIAQLLPQD
DVEHLVLPTL RQCASDSSWR VRYMVAEKFV DLQKAVGPEI TRVDLVPAFQ YLLKDAEAEV
RAAVATKVKD FCANLDKVNQ VQIILSSILP YVRDLVSDPN PHVKSALASV IMGLSPMLGA
YQTVEQLLPL FLIQLKDECP EVRLNIISNL DCVNDVIGIQ QLSQSLLPAI VELAEDSKWR
VRLAIIEYMP ALAGQLGQEF FDQKLRGLCM GWLNDHVYAI REAATLNMKK LVEQFGAPWA
EQAIIPMILV MSRNKNYLHR MTCLFCLNVL AEVCGTDITT KLLLPTVLLL AADPVANVRF
NVAKTLQKIS PFLEASVIDA QVKPTLDKLN TDTDVDVKHF AAQAIAGIAA A
