2ABA_ARATH
ID 2ABA_ARATH Reviewed; 513 AA.
AC Q38821; Q0WL96; Q27GN0; Q8L842; Q9C8H8;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Serine/threonine protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform;
DE Short=AtB alpha;
DE Short=PP2A, subunit B, alpha isoform;
GN Name=PP2AB1; OrderedLocusNames=At1g51690; ORFNames=F19C24.10;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=7599311; DOI=10.1007/bf00020245;
RA Rundle S.J., Hartung A.J., Corum J.W. III, O'Neill M.;
RT "Characterization of a cDNA encoding the 55 kDa B regulatory subunit of
RT Arabidopsis protein phosphatase 2A.";
RL Plant Mol. Biol. 28:257-266(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [7]
RP INTERACTION WITH SIC/RON3.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=26888284; DOI=10.1073/pnas.1501343112;
RA Karampelias M., Neyt P., De Groeve S., Aesaert S., Coussens G., Rolcik J.,
RA Bruno L., De Winne N., Van Minnebruggen A., Van Montagu M., Ponce M.R.,
RA Micol J.L., Friml J., De Jaeger G., Van Lijsebettens M.;
RT "ROTUNDA3 function in plant development by phosphatase 2A-mediated
RT regulation of auxin transporter recycling.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:2768-2773(2016).
CC -!- FUNCTION: The B regulatory subunit may modulate substrate selectivity
CC and catalytic activity, and also may direct the localization of the
CC catalytic enzyme to a particular subcellular compartment.
CC {ECO:0000250}.
CC -!- SUBUNIT: PP2A consists of a common heteromeric enzyme, composed of a
CC catalytic subunit (subunits C), a constant regulatory subunit (subunit
CC A), and a variety of regulatory subunits such as subunits B (the
CC R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families) (By
CC similarity). Interacts with SIC/RON3 (PubMed:26888284). {ECO:0000250,
CC ECO:0000269|PubMed:26888284}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q38821-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q38821-2; Sequence=VSP_025610;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC {ECO:0000269|PubMed:7599311}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B family.
CC {ECO:0000305}.
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DR EMBL; U18129; AAA86695.1; -; mRNA.
DR EMBL; AC025294; AAG50878.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32701.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32702.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60211.1; -; Genomic_DNA.
DR EMBL; AY120756; AAM53314.1; -; mRNA.
DR EMBL; BT000109; AAN15428.1; -; mRNA.
DR EMBL; AK230310; BAF02111.1; -; mRNA.
DR PIR; G96555; G96555.
DR PIR; S55889; S55889.
DR RefSeq; NP_001322512.1; NM_001333494.1. [Q38821-1]
DR RefSeq; NP_564595.1; NM_104047.4. [Q38821-1]
DR RefSeq; NP_974003.1; NM_202274.2. [Q38821-2]
DR AlphaFoldDB; Q38821; -.
DR SMR; Q38821; -.
DR BioGRID; 26819; 4.
DR IntAct; Q38821; 1.
DR STRING; 3702.AT1G51690.3; -.
DR iPTMnet; Q38821; -.
DR PaxDb; Q38821; -.
DR PRIDE; Q38821; -.
DR ProteomicsDB; 244588; -. [Q38821-1]
DR EnsemblPlants; AT1G51690.1; AT1G51690.1; AT1G51690. [Q38821-1]
DR EnsemblPlants; AT1G51690.2; AT1G51690.2; AT1G51690. [Q38821-2]
DR EnsemblPlants; AT1G51690.4; AT1G51690.4; AT1G51690. [Q38821-1]
DR GeneID; 841594; -.
DR Gramene; AT1G51690.1; AT1G51690.1; AT1G51690. [Q38821-1]
DR Gramene; AT1G51690.2; AT1G51690.2; AT1G51690. [Q38821-2]
DR Gramene; AT1G51690.4; AT1G51690.4; AT1G51690. [Q38821-1]
DR KEGG; ath:AT1G51690; -.
DR Araport; AT1G51690; -.
DR eggNOG; KOG1354; Eukaryota.
DR InParanoid; Q38821; -.
DR PhylomeDB; Q38821; -.
DR PRO; PR:Q38821; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q38821; baseline and differential.
DR Genevisible; Q38821; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IBA:GO_Central.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 3.
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 Pfam; PF00400; WD40; 1.
DR PIRSF; PIRSF037309; PP2A_PR55; 1.
DR PRINTS; PR00600; PP2APR55.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS01024; PR55_1; 1.
DR PROSITE; PS01025; PR55_2; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..513
FT /note="Serine/threonine protein phosphatase 2A 55 kDa
FT regulatory subunit B alpha isoform"
FT /id="PRO_0000071438"
FT REPEAT 36..75
FT /note="WD 1"
FT REPEAT 112..153
FT /note="WD 2"
FT REPEAT 232..270
FT /note="WD 3"
FT REPEAT 281..321
FT /note="WD 4"
FT REPEAT 340..378
FT /note="WD 5"
FT REPEAT 483..513
FT /note="WD 6"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q39247"
FT VAR_SEQ 214
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_025610"
FT CONFLICT 165
FT /note="G -> R (in Ref. 1; AAA86695)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 513 AA; 56935 MW; 2AF84BE214172D19 CRC64;
MNGGDEVVAA SADPSLPLEW RFSQVFGERS AGEEVQEVDI ISAIEFDNSG NHLATGDRGG
RVVLFERTDT NNSSGTRREL EEADYPLRHP EFRYKTEFQS HDPEFDYLKS LEIEEKINKI
RWCQTANGAL FLLSTNDKTI KFWKVQDKKI KKICDMNSDP SRTVGNGTVA SSSNSNITNS
CLVNGGVSEV NNSLCNDFSL PAGGISSLRL PVVVTSHESS PVARCRRVYA HAHDYHINSI
SNNSDGETFI SADDLRINLW NLEISNQSFN IVDVKPAKME DLSEVITSAE FHPTHCNMLA
YSSSKGSIRL IDLRQSALCD SHSKLFEEPE QAGPKSFFTE IIASVSDIKF AKEGRYLLSR
DYMTLKLWDI NMDAGPVATF QVHEYLKPKL CDLYENDSIF DKFECCISGN GLRAATGSYS
NLFRVFGVAP GSTETATLEA SRNPMRRHVP IPSRPSRALS SITRVVSRGS ESPGVDGNTN
ALDYTTKLLH LAWHPNENSI ACAAANSLYM YYA
