2AB2A_ARATH
ID 2AB2A_ARATH Reviewed; 538 AA.
AC Q9XGR4;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Serine/threonine protein phosphatase 2A regulatory subunit B''alpha;
DE Short=AtB''alpha;
DE Short=PP2A, B'' subunit, alpha isoform;
GN Name=B''ALPHA; OrderedLocusNames=At5g44090; ORFNames=MLN1.1;
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].
RA Hendershot J.D III, Esmon C.A., Lumb J.E., Rundle S.J.;
RT "Identification and Characterization of Sequences Encoding a 62 kDa B'
RT Regulatory Subunit of Arabidopsis thaliana Protein Phosphatase 2A
RT (Accession No. AF165429).";
RL (er) Plant Gene Register PGR99-125(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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].
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 [MRNA], INTERACTION WITH HMG1 AND PP2AA1, FUNCTION,
RP 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).
CC -!- FUNCTION: Regulatory subunit of type 2A protein phosphatase. Not
CC involved in HMGR regulation in seedlings grown in standard medium, but
CC negatively regulates root growth in response to salt.
CC {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 -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:21478440}.
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DR EMBL; AF165429; AAD45158.1; -; mRNA.
DR EMBL; AB005239; BAB10976.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95057.1; -; Genomic_DNA.
DR EMBL; AY099553; AAM20405.1; -; mRNA.
DR EMBL; BT002124; AAN72135.1; -; mRNA.
DR EMBL; AY462121; AAS44556.1; -; mRNA.
DR RefSeq; NP_199222.1; NM_123776.4.
DR AlphaFoldDB; Q9XGR4; -.
DR SMR; Q9XGR4; -.
DR BioGRID; 19682; 11.
DR IntAct; Q9XGR4; 7.
DR STRING; 3702.AT5G44090.1; -.
DR iPTMnet; Q9XGR4; -.
DR PaxDb; Q9XGR4; -.
DR PRIDE; Q9XGR4; -.
DR ProteomicsDB; 245168; -.
DR EnsemblPlants; AT5G44090.1; AT5G44090.1; AT5G44090.
DR GeneID; 834432; -.
DR Gramene; AT5G44090.1; AT5G44090.1; AT5G44090.
DR KEGG; ath:AT5G44090; -.
DR Araport; AT5G44090; -.
DR TAIR; locus:2167623; AT5G44090.
DR eggNOG; KOG2562; Eukaryota.
DR HOGENOM; CLU_019589_3_0_1; -.
DR InParanoid; Q9XGR4; -.
DR OMA; NLNIACG; -.
DR PhylomeDB; Q9XGR4; -.
DR PRO; PR:Q9XGR4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9XGR4; baseline and differential.
DR Genevisible; Q9XGR4; AT.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
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 Pfam; PF13833; EF-hand_8; 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 Calcium; Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..538
FT /note="Serine/threonine protein phosphatase 2A regulatory
FT subunit B''alpha"
FT /id="PRO_0000422787"
FT DOMAIN 177..212
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 264..299
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 390..425
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 88..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 403
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 405
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 407
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 414
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 538 AA; 62325 MW; EAFEAE38F8C8D40A CRC64;
MEIDGGNDVQ ILDPELLQLP GLSPVSLKEN PHIAEELFSQ WLSLPETGRL VKSLIDDTKS
STPVSVSKNC TSLNVACGSA LPSVFLNSGT PPLSPRGSPG SPRFSRQKTS PSLQSPLKSV
REPKRQLIPQ FYFQHGRPPA KELREQCISM VDQFFSNYID GLHMDEFKSI TKEVCKLPSF
LSSVLFRKID TSGTGIVTRD AFIKYWVDGH MLAMDVASQI YNILRQPGCK YLRQADFKPV
LDELLTTHPG LEFLRNTPEF QERYAETVIY RIFYYINRSG TGCITLRELK RGNLITAMQQ
VDEEDDINKV IRYFSYEHFY VIYCRFWELD GDHDFLIDKE NLIKYGNHAL TYRIVDRIFS
QVPRKFTSKV EGKMSYEDFA YFILAEEDKS SEPSLEYWFK CIDLDGDGVI TPNEMQFFYE
EQLHRMECIT QEPVLFEDIL CQIFDMIKPE KENCITLQDL KASKLSGNIF NILFNLNKFM
AFETRDPFLI RQERENPTLT EWDRFAQREY VRLSMEEDVE EVSNGSADVW DEPLESPF
