2ABB_ARATH
ID 2ABB_ARATH Reviewed; 501 AA.
AC Q39247; Q9FZ61;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Serine/threonine protein phosphatase 2A 55 kDa regulatory subunit B beta isoform;
DE Short=AtB beta;
DE Short=PP2A, subunit B, beta isoform;
GN Name=PP2AB2; OrderedLocusNames=At1g17720; ORFNames=F11A6.6;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=8756607; DOI=10.1007/bf00021804;
RA Corum J.W. III, Hartung A.J., Stamey R.T., Rundle S.J.;
RT "Characterization of DNA sequences encoding a novel isoform of the 55 kDa B
RT regulatory subunit of the type 2A protein serine/threonine phosphatase of
RT Arabidopsis thaliana.";
RL Plant Mol. Biol. 31:419-427(1996).
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] (ISOFORMS 1 AND 2).
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 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [6]
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=Q39247-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q39247-2; Sequence=VSP_017095;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC {ECO:0000269|PubMed:8756607}.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B family.
CC {ECO:0000305}.
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DR EMBL; U40161; AAB60777.1; -; mRNA.
DR EMBL; AC034257; AAF99812.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29626.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29627.1; -; Genomic_DNA.
DR EMBL; AF370519; AAK43896.1; -; mRNA.
DR EMBL; AY045665; AAK74023.1; -; mRNA.
DR EMBL; BT000645; AAN18211.1; -; mRNA.
DR EMBL; BT002183; AAN72194.1; -; mRNA.
DR PIR; B86312; B86312.
DR RefSeq; NP_564033.1; NM_101634.4. [Q39247-1]
DR RefSeq; NP_849681.1; NM_179350.4. [Q39247-2]
DR AlphaFoldDB; Q39247; -.
DR SMR; Q39247; -.
DR BioGRID; 23588; 24.
DR IntAct; Q39247; 3.
DR STRING; 3702.AT1G17720.1; -.
DR iPTMnet; Q39247; -.
DR PaxDb; Q39247; -.
DR PRIDE; Q39247; -.
DR ProteomicsDB; 244591; -. [Q39247-1]
DR EnsemblPlants; AT1G17720.1; AT1G17720.1; AT1G17720. [Q39247-1]
DR EnsemblPlants; AT1G17720.2; AT1G17720.2; AT1G17720. [Q39247-2]
DR GeneID; 838348; -.
DR Gramene; AT1G17720.1; AT1G17720.1; AT1G17720. [Q39247-1]
DR Gramene; AT1G17720.2; AT1G17720.2; AT1G17720. [Q39247-2]
DR KEGG; ath:AT1G17720; -.
DR Araport; AT1G17720; -.
DR TAIR; locus:2007963; AT1G17720.
DR eggNOG; KOG1354; Eukaryota.
DR HOGENOM; CLU_021713_3_3_1; -.
DR InParanoid; Q39247; -.
DR OMA; HPISCNW; -.
DR PhylomeDB; Q39247; -.
DR PRO; PR:Q39247; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q39247; baseline and differential.
DR Genevisible; Q39247; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; ISS:TAIR.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:TAIR.
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; 2.
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..501
FT /note="Serine/threonine protein phosphatase 2A 55 kDa
FT regulatory subunit B beta isoform"
FT /id="PRO_0000071439"
FT REPEAT 34..73
FT /note="WD 1"
FT REPEAT 110..151
FT /note="WD 2"
FT REPEAT 220..258
FT /note="WD 3"
FT REPEAT 269..309
FT /note="WD 4"
FT REPEAT 328..366
FT /note="WD 5"
FT REPEAT 471..501
FT /note="WD 6"
FT REGION 439..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VAR_SEQ 200
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_017095"
SQ SEQUENCE 501 AA; 56275 MW; 030B7997B730F581 CRC64;
MNGGDDAATS GPPPSLEWRF SQVFGERTAG EEVQEVDIIS AIEFDKSGDH LATGDRGGRV
VLFERTDTKD HGGSRKDLEQ TDYPVRHPEF RYKTEFQSHE PEFDYLKSLE IEEKINKIRW
CQPANGALFL LSTNDKTIKY WKVQEKKIKK ISEMNIDPSE SSNIPPQLVT NGLPADKGHD
YLSKDFSFPP GGIPSLRLPV VVTSQETNLV ARCRRVYAHA HDYHINSISN SSDGETFISA
DDLRVNLWNL EISNQSFNIV DVKPTNMEDL TEVITSAEFH PIHCNMLAYS SSKGSIRLID
MRQSALCDSH TKLFEEPEAP GSRSFFTEII ASISDIKFSK DGRYILSRDY MTLKLWDINM
DSGPVASYQV HEHLRPRLCD LYENDSIFDK FECCLSGDGL RVATGSYSNL FRVFGASQGS
TEAATLEASK NPMRRQIQTP ARPSRSIGSM TRVVRRGSES PGTEANGNAY DFTTKLLHMA
WHPTENSIAC AAANSLYMYY A
