2ABA_DROME
ID 2ABA_DROME Reviewed; 499 AA.
AC P36872; A4V2M9; A4V2N0; Q9VH21; Q9VH22;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Protein phosphatase PP2A 55 kDa regulatory subunit;
DE Short=PR55;
DE AltName: Full=Protein phosphatase PP2A regulatory subunit B;
DE AltName: Full=Protein twins;
GN Name=tws; Synonyms=aar, Pp2A-85F; ORFNames=CG6235;
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 [GENOMIC DNA / MRNA] (ISOFORMS A AND B).
RX PubMed=8382567; DOI=10.1016/0092-8674(93)90080-a;
RA Mayer-Jaekel R.E., Ohkura H., Gomes R., Sunkel C.E., Baumgartner S.,
RA Hemmings B.A., Glover D.M.;
RT "The 55 kd regulatory subunit of Drosophila protein phosphatase 2A is
RT required for anaphase.";
RL Cell 72:621-633(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RC STRAIN=Oregon-R; TISSUE=Eye imaginal disk;
RX PubMed=8383623; DOI=10.1101/gad.7.3.429;
RA Uemura T., Shiomi K., Togashi S., Takeichi M.;
RT "Mutation of twins encoding a regulator of protein phosphatase 2A leads to
RT pattern duplication in Drosophila imaginal discs.";
RL Genes Dev. 7:429-440(1993).
RN [3]
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 [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Could perform a substrate recognition function or could be
CC responsible for targeting the enzyme complex to the appropriate
CC subcellular compartment.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A; Synonyms=F;
CC IsoId=P36872-1; Sequence=Displayed;
CC Name=B; Synonyms=C, D, E, G, H;
CC IsoId=P36872-2; Sequence=VSP_005105, VSP_005106;
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B family.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1, Met-18, Met-33 or Met-44 is the
CC initiator. {ECO:0000305}.
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DR EMBL; D13004; BAA02367.1; -; mRNA.
DR EMBL; L07581; AAA99870.1; -; mRNA.
DR EMBL; L07583; AAA99871.1; -; mRNA.
DR EMBL; L07585; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L07586; AAB00371.1; -; Genomic_DNA.
DR EMBL; L12544; AAB00371.1; JOINED; Genomic_DNA.
DR EMBL; L07586; AAB00372.1; -; Genomic_DNA.
DR EMBL; L12544; AAB00372.1; JOINED; Genomic_DNA.
DR EMBL; AE014297; AAF54498.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF54499.3; -; Genomic_DNA.
DR EMBL; AE014297; AAN13455.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13456.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13457.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13458.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13459.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13460.1; -; Genomic_DNA.
DR EMBL; AY061152; AAL28700.1; -; mRNA.
DR PIR; A45778; A45778.
DR RefSeq; NP_001287269.1; NM_001300340.1. [P36872-1]
DR RefSeq; NP_476880.1; NM_057532.4. [P36872-1]
DR RefSeq; NP_476881.1; NM_057533.3. [P36872-2]
DR RefSeq; NP_599111.1; NM_134284.3. [P36872-2]
DR RefSeq; NP_599112.1; NM_134285.2. [P36872-2]
DR RefSeq; NP_599113.1; NM_134286.3. [P36872-2]
DR RefSeq; NP_731451.1; NM_169329.2. [P36872-1]
DR RefSeq; NP_731452.1; NM_169330.2. [P36872-2]
DR RefSeq; NP_731453.1; NM_169331.2. [P36872-2]
DR AlphaFoldDB; P36872; -.
DR SMR; P36872; -.
DR BioGRID; 71024; 36.
DR DIP; DIP-19897N; -.
DR IntAct; P36872; 32.
DR STRING; 7227.FBpp0081665; -.
DR PaxDb; P36872; -.
DR DNASU; 47877; -.
DR EnsemblMetazoa; FBtr0082186; FBpp0081664; FBgn0004889. [P36872-1]
DR EnsemblMetazoa; FBtr0082187; FBpp0081665; FBgn0004889. [P36872-1]
DR EnsemblMetazoa; FBtr0082188; FBpp0081666; FBgn0004889. [P36872-2]
DR EnsemblMetazoa; FBtr0082189; FBpp0081667; FBgn0004889. [P36872-2]
DR EnsemblMetazoa; FBtr0082190; FBpp0081668; FBgn0004889. [P36872-2]
DR EnsemblMetazoa; FBtr0082191; FBpp0081669; FBgn0004889. [P36872-2]
DR EnsemblMetazoa; FBtr0082192; FBpp0081670; FBgn0004889. [P36872-2]
DR EnsemblMetazoa; FBtr0082193; FBpp0081671; FBgn0004889. [P36872-2]
DR EnsemblMetazoa; FBtr0345177; FBpp0311386; FBgn0004889. [P36872-1]
DR GeneID; 47877; -.
DR KEGG; dme:Dmel_CG6235; -.
DR UCSC; CG6235-RC; d. melanogaster.
DR UCSC; CG6235-RF; d. melanogaster.
DR CTD; 47877; -.
DR FlyBase; FBgn0004889; tws.
DR VEuPathDB; VectorBase:FBgn0004889; -.
DR eggNOG; KOG1354; Eukaryota.
DR GeneTree; ENSGT00950000182864; -.
DR InParanoid; P36872; -.
DR OMA; HPISCNW; -.
DR PhylomeDB; P36872; -.
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-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; P36872; -.
DR BioGRID-ORCS; 47877; 1 hit in 3 CRISPR screens.
DR ChiTaRS; tws; fly.
DR GenomeRNAi; 47877; -.
DR PRO; PR:P36872; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0004889; Expressed in adult hindgut (Drosophila) and 31 other tissues.
DR ExpressionAtlas; P36872; baseline and differential.
DR Genevisible; P36872; DM.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; ISS:UniProtKB.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IMP:FlyBase.
DR GO; GO:0007098; P:centrosome cycle; IMP:FlyBase.
DR GO; GO:0007447; P:imaginal disc pattern formation; IMP:UniProtKB.
DR GO; GO:0045201; P:maintenance of neuroblast polarity; IMP:FlyBase.
DR GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0007406; P:negative regulation of neuroblast proliferation; IMP:FlyBase.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:FlyBase.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IMP:FlyBase.
DR GO; GO:0006470; P:protein dephosphorylation; IMP:FlyBase.
DR GO; GO:0050821; P:protein stabilization; IDA:FlyBase.
DR GO; GO:0046599; P:regulation of centriole replication; IMP:FlyBase.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IMP:UniProtKB.
DR GO; GO:0007423; P:sensory organ development; IMP:FlyBase.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR000009; PP2A_PR55.
DR InterPro; IPR018067; PP2A_PR55_CS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR11871; PTHR11871; 1.
DR PIRSF; PIRSF037309; PP2A_PR55; 1.
DR PRINTS; PR00600; PP2APR55.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS01024; PR55_1; 1.
DR PROSITE; PS01025; PR55_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..499
FT /note="Protein phosphatase PP2A 55 kDa regulatory subunit"
FT /id="PRO_0000071437"
FT REPEAT 79..118
FT /note="WD 1"
FT REPEAT 144..185
FT /note="WD 2"
FT REPEAT 228..266
FT /note="WD 3"
FT REPEAT 277..317
FT /note="WD 4"
FT REPEAT 336..374
FT /note="WD 5"
FT REPEAT 391..432
FT /note="WD 6"
FT REPEAT 467..498
FT /note="WD 7"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..30
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..56
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:8382567,
FT ECO:0000303|PubMed:8383623"
FT /id="VSP_005105"
FT VAR_SEQ 57..59
FT /note="PAS -> MAG (in isoform B)"
FT /evidence="ECO:0000303|PubMed:8382567,
FT ECO:0000303|PubMed:8383623"
FT /id="VSP_005106"
FT CONFLICT 211
FT /note="K -> M (in Ref. 1; AAA99871)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 499 AA; 56967 MW; D871A7E3058B7286 CRC64;
MGRWGRQSPV LEPPDPQMQT TPPPPTLPPR TFMRQSSITK IGNMLNTAIN INGAKKPASN
GEASWCFSQI KGALDDDVTD ADIISCVEFN HDGELLATGD KGGRVVIFQR DPASKAANPR
RGEYNVYSTF QSHEPEFDYL KSLEIEEKIN KIRWLQQKNP VHFLLSTNDK TVKLWKVSER
DKSFGGYNTK EENGLIRDPQ NVTALRVPSV KQIPLLVEAS PRRTFANAHT YHINSISVNS
DQETFLSADD LRINLWHLEV VNQSYNIVDI KPTNMEELTE VITAAEFHPT ECNVFVYSSS
KGTIRLCDMR SAALCDRHSK QFEEPENPTN RSFFSEIISS ISDVKLSNSG RYMISRDYLS
IKVWDLHMET KPIETYPVHE YLRAKLCSLY ENDCIFDKFE CCWNGKDSSI MTGSYNNFFR
VFDRNSKKDV TLEASRDIIK PKTVLKPRKV CTGGKRKKDE ISVDCLDFNK KILHTAWHPE
ENIIAVAATN NLFIFQDKF
