2AB2B_ARATH
ID 2AB2B_ARATH Reviewed; 536 AA.
AC Q5QIT3; Q56WJ0; Q940C6;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Serine/threonine protein phosphatase 2A regulatory subunit B''beta;
DE Short=AtB''beta;
DE AltName: Full=Serine/threonine protein phosphatase 2A regulatory subunit B'' beta 1 isoform;
DE Short=PP2A, B'' subunit, beta 1 isoform;
GN Name=B''BETA; OrderedLocusNames=At5g28850; ORFNames=F7P1.30;
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), INTERACTION WITH HMG1 AND PP2AA1,
RP FUNCTION, DISRUPTION PHENOTYPE, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=21478440; DOI=10.1105/tpc.110.074278;
RA Leivar P., Antolin-Llovera M., Ferrero S., Closa M., Arro M., Ferrer A.,
RA Boronat A., Campos N.;
RT "Multilevel control of Arabidopsis 3-hydroxy-3-methylglutaryl coenzyme A
RT reductase by protein phosphatase 2A.";
RL Plant Cell 23:1494-1511(2011).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 191-536 (ISOFORM 1).
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulatory subunit of type 2A protein phosphatase. Involved
CC in post-transcriptional regulation of HMGR but not in root growth
CC regulation in response to salt. {ECO:0000269|PubMed:21478440}.
CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, composed
CC of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant
CC regulatory subunit (PR65 or subunit A), that associates with a variety
CC of regulatory subunits. Proteins that associate with the core dimer
CC include three families of regulatory subunits B (the R2/B/PR55/B55,
CC R3/B''/PR72/PR130/PR59 and R5/B'/B56 families) and cell signaling
CC molecules. Interacts with HMGR1L and HMGR1S (via N-terminus), but not
CC with HMG2. Interacts with PP2AA1. {ECO:0000269|PubMed:21478440}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5QIT3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5QIT3-2; Sequence=VSP_046803;
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:21478440}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD94815.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY462122; AAS44557.1; -; mRNA.
DR EMBL; CP002688; AED93845.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93846.1; -; Genomic_DNA.
DR EMBL; AY056110; AAL06997.1; -; mRNA.
DR EMBL; BT003095; AAO23892.1; -; mRNA.
DR EMBL; AK222050; BAD94815.1; ALT_INIT; mRNA.
DR RefSeq; NP_568509.1; NM_122768.2. [Q5QIT3-1]
DR RefSeq; NP_851089.1; NM_180758.1. [Q5QIT3-2]
DR AlphaFoldDB; Q5QIT3; -.
DR SMR; Q5QIT3; -.
DR BioGRID; 18276; 5.
DR STRING; 3702.AT5G28850.2; -.
DR iPTMnet; Q5QIT3; -.
DR PaxDb; Q5QIT3; -.
DR PRIDE; Q5QIT3; -.
DR ProMEX; Q5QIT3; -.
DR ProteomicsDB; 243263; -. [Q5QIT3-1]
DR EnsemblPlants; AT5G28850.1; AT5G28850.1; AT5G28850. [Q5QIT3-2]
DR EnsemblPlants; AT5G28850.2; AT5G28850.2; AT5G28850. [Q5QIT3-1]
DR GeneID; 833004; -.
DR Gramene; AT5G28850.1; AT5G28850.1; AT5G28850. [Q5QIT3-2]
DR Gramene; AT5G28850.2; AT5G28850.2; AT5G28850. [Q5QIT3-1]
DR KEGG; ath:AT5G28850; -.
DR Araport; AT5G28850; -.
DR TAIR; locus:2150446; AT5G28850.
DR eggNOG; KOG2562; Eukaryota.
DR HOGENOM; CLU_019589_3_0_1; -.
DR InParanoid; Q5QIT3; -.
DR OMA; DYWINDN; -.
DR OrthoDB; 255081at2759; -.
DR PhylomeDB; Q5QIT3; -.
DR PRO; PR:Q5QIT3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q5QIT3; baseline and differential.
DR Genevisible; Q5QIT3; AT.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR041534; EF-hand_13.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF17958; EF-hand_13; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..536
FT /note="Serine/threonine protein phosphatase 2A regulatory
FT subunit B''beta"
FT /id="PRO_0000422788"
FT DOMAIN 174..209
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 261..296
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 387..422
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 69..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 400
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 402
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 404
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 411
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT VAR_SEQ 1..231
FT /note="MVDTVIPGDMACLDADLLQLQEMSSFVLNSKPGFTQKLFDQWLSLPEAQRQV
FT GSLLKDAVAGAPINVTGSASGSNSATIPSMFPAGSAPPLSPRSCGSPRTTKQRAPSNLG
FT STLKVVNEPVKEPIPQFYFQNGRPPPSEIKEQCMFRINHFFYGHMDGLQIQEFKLVTRE
FT ICKLPSFFSTSLFRKIDLNNTGFVTRDAFIDFWVNGNMLIMDTTTQIFKILKQKDQSFI
FT VK -> MKASLYSRFYSFLFFFSWQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_046803"
SQ SEQUENCE 536 AA; 61977 MW; 4F55BBEBA77DC52B CRC64;
MVDTVIPGDM ACLDADLLQL QEMSSFVLNS KPGFTQKLFD QWLSLPEAQR QVGSLLKDAV
AGAPINVTGS ASGSNSATIP SMFPAGSAPP LSPRSCGSPR TTKQRAPSNL GSTLKVVNEP
VKEPIPQFYF QNGRPPPSEI KEQCMFRINH FFYGHMDGLQ IQEFKLVTRE ICKLPSFFST
SLFRKIDLNN TGFVTRDAFI DFWVNGNMLI MDTTTQIFKI LKQKDQSFIV KDDFKPLLKE
LLATHPGLEF LQSTPEFQER YAETVTYRIF YYINRSGNGR ITFRELKRGN LIDAMLHADE
EEDINKVLRY FSYEHFYVIY CKFWELDTDH DFLIDKENLM RYGNHALTYR IVDRIFSQVA
RKFTSKVEGK MGYEDFVYFI LAEEDKSSVP SLEYWFKCID LDANGIITRN EMQFFYEEQL
HRMECMAQEA VLFEDILCQM IDMIGPENES HITLHDLKGS KLSGNVFNIL FNLNKFMAFE
TRDPFLIRQE RENPTLTDWD RFAHREYIRL SMEEDVEDAS NGSAEVWDDS SLEAPF
