ID   2AB2D_ARATH             Reviewed;         535 AA.
AC   Q9SLI8;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Probable serine/threonine protein phosphatase 2A regulatory subunit B''delta;
DE            Short=AtB''delta;
GN   Name=B''DELTA; OrderedLocusNames=At1g54450; ORFNames=F20D21.27;
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 [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   [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   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: Probable regulatory subunit of type 2A protein phosphatase.
CC       {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
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DR   EMBL; AC005287; AAD25624.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE33105.1; -; Genomic_DNA.
DR   PIR; D96586; D96586.
DR   RefSeq; NP_175847.1; NM_104323.4.
DR   AlphaFoldDB; Q9SLI8; -.
DR   SMR; Q9SLI8; -.
DR   BioGRID; 27112; 5.
DR   STRING; 3702.AT1G54450.1; -.
DR   iPTMnet; Q9SLI8; -.
DR   PaxDb; Q9SLI8; -.
DR   PRIDE; Q9SLI8; -.
DR   ProteomicsDB; 244503; -.
DR   DNASU; 841887; -.
DR   EnsemblPlants; AT1G54450.1; AT1G54450.1; AT1G54450.
DR   GeneID; 841887; -.
DR   Gramene; AT1G54450.1; AT1G54450.1; AT1G54450.
DR   KEGG; ath:AT1G54450; -.
DR   Araport; AT1G54450; -.
DR   TAIR; locus:2020043; AT1G54450.
DR   eggNOG; KOG2562; Eukaryota.
DR   HOGENOM; CLU_019589_3_0_1; -.
DR   InParanoid; Q9SLI8; -.
DR   OMA; YGHEDGL; -.
DR   OrthoDB; 255081at2759; -.
DR   PhylomeDB; Q9SLI8; -.
DR   PRO; PR:Q9SLI8; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SLI8; baseline and differential.
DR   Genevisible; Q9SLI8; 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   Pfam; PF13833; EF-hand_8; 1.
DR   SUPFAM; SSF47473; SSF47473; 2.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
PE   3: Inferred from homology;
KW   Calcium; Metal-binding; Reference proteome; Repeat.
FT   CHAIN           1..535
FT                   /note="Probable serine/threonine protein phosphatase 2A
FT                   regulatory subunit B''delta"
FT                   /id="PRO_0000422790"
FT   DOMAIN          174..209
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          387..422
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   REGION          67..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..104
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"
SQ   SEQUENCE   535 AA;  61939 MW;  01AEFA0A20B510F3 CRC64;
     MESITLDIEL LQLPETSPMS MKSNQDFVKK LFDQWLALPE TNRLVTSLVN DAKAGVALNV
     MCGGGSSGTN SGSNSPLASM FPARNGPPLS PRNSTGSPRI ARQRTGLSNL SSPLKVVSDH
     VKELIPQFYF EDGRPPPNDL KEQCIAKINS LFYGHEDGLQ LQEFKLVTTE ICKVPSFFST
     SIFKKVDTNN TGFVKREDFI DYWVKGNMLT KEITSQVFTI LKQPDHNYLV QDDFKPVLQE
     LLATHPGLEF LQGTPEFQDR YAETVIYRIY YYINRSGNGH LTLRELKRGN LVDAMQHADE
     EEDINKVLRY FSYEHFYVIY CKFWELDTDH DFLIDKENLI RYSNHALTYR IVDRIFSQVP
     RKFTSKTEGK MGYEDFVYFI LAEEDKSSEP SLEYWFKCID LDANGVLTRN ELQFFYEEQL
     HRMECMAQEA VLFEDILCQL FDMVKPEDEG FICLNDLKGS KLSGNVFNIL FNLNKFMAFE
     TRDPFLIRQE RANPTWTEWD RFAHREYIRL SMEEDVEDAS NGSAEAWDDS LEVPF