2A5K_ORYSJ
ID 2A5K_ORYSJ Reviewed; 510 AA.
AC Q6I621; Q0DG37; Q8L6I7;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Serine/threonine protein phosphatase 2A 57 kDa regulatory subunit B' kappa isoform {ECO:0000305};
DE Short=OsB'kappa {ECO:0000303|PubMed:31221736};
DE Short=PP2A, B' subunit, kappa isoform {ECO:0000305};
GN Name=B'KAPPA {ECO:0000303|PubMed:12068121};
GN OrderedLocusNames=Os05g0555100 {ECO:0000312|EMBL:BAF18186.1},
GN LOC_Os05g48150 {ECO:0000305};
GN ORFNames=OJ1263_E10.15 {ECO:0000312|EMBL:AAT58738.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12068121; DOI=10.1104/pp.020004;
RA Terol J., Bargues M., Carrasco P., Perez-Alonso M., Paricio N.;
RT "Molecular characterization and evolution of the protein phosphatase 2A B'
RT regulatory subunit family in plants.";
RL Plant Physiol. 129:808-822(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH SIT1,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY SALT STRESS,
RP PHOSPHORYLATION AT THR-476; THR-493; SER-502 AND THR-508, MUTAGENESIS OF
RP 330-SER-SER-331; THR-476; THR-493; SER-502 AND THR-508, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=31221736; DOI=10.1105/tpc.18.00706;
RA Zhao J.L., Zhang L.Q., Liu N., Xu S.L., Yue Z.L., Zhang L.L., Deng Z.P.,
RA Burlingame A.L., Sun D.Y., Wang Z.Y., Sun Y., Zhang S.W.;
RT "Mutual regulation of receptor-like kinase SIT1 and B'kappa-PP2A shapes the
RT early response of rice to salt stress.";
RL Plant Cell 31:2131-2151(2019).
CC -!- FUNCTION: B regulatory subunit of phosphatase 2A (PP2A) involved in
CC salt stress response (PubMed:31221736). Under salt stress conditions,
CC required for the catalytic activity of PP2A and the dephosphorylation
CC of SIT1, a negative regulator of salt tolerance (PubMed:31221736).
CC Dephosphorylation of SIT1 turns off salt-induced SIT1 activity
CC directly, which has a positive effect on salt tolerance
CC (PubMed:31221736). {ECO:0000269|PubMed:31221736}.
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 SIT1 (PubMed:31221736).
CC {ECO:0000250|UniProtKB:Q13362, ECO:0000269|PubMed:31221736}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:31221736}.
CC Cell membrane {ECO:0000269|PubMed:31221736}; Peripheral membrane
CC protein {ECO:0000305|PubMed:31221736}. Note=The partial localization to
CC the plasma membrane may be due to its association with SIT1.
CC {ECO:0000269|PubMed:31221736}.
CC -!- TISSUE SPECIFICITY: Expressed in root stele and epidermal cells.
CC {ECO:0000269|PubMed:31221736}.
CC -!- INDUCTION: Induced by salt stress (at protein level).
CC {ECO:0000269|PubMed:31221736}.
CC -!- PTM: Phosphorylated at THR-476, THR-493, SER-502 and THR-508 by SIT1.
CC {ECO:0000269|PubMed:31221736}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants exhibit increased sensitivity to salt
CC stress. {ECO:0000269|PubMed:31221736}.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF18186.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAS95256.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ312313; CAC85920.1; -; Genomic_DNA.
DR EMBL; AC093956; AAT58738.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF18186.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014961; BAS95256.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_015637801.1; XM_015782315.1.
DR AlphaFoldDB; Q6I621; -.
DR SMR; Q6I621; -.
DR STRING; 4530.OS05T0555100-01; -.
DR EnsemblPlants; Os05t0555100-01; Os05t0555100-01; Os05g0555100.
DR GeneID; 4339558; -.
DR Gramene; Os05t0555100-01; Os05t0555100-01; Os05g0555100.
DR KEGG; osa:4339558; -.
DR eggNOG; KOG2085; Eukaryota.
DR HOGENOM; CLU_012437_4_1_1; -.
DR InParanoid; Q6I621; -.
DR OrthoDB; 890437at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IEA:InterPro.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IDA:UniProtKB.
DR GO; GO:1901002; P:positive regulation of response to salt stress; IMP:UniProtKB.
DR GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002554; PP2A_B56.
DR PANTHER; PTHR10257; PTHR10257; 1.
DR Pfam; PF01603; B56; 1.
DR PIRSF; PIRSF028043; PP2A_B56; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Membrane; Phosphoprotein; Reference proteome;
KW Stress response.
FT CHAIN 1..510
FT /note="Serine/threonine protein phosphatase 2A 57 kDa
FT regulatory subunit B' kappa isoform"
FT /id="PRO_0000448552"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 476
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:31221736"
FT MOD_RES 493
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:31221736"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:31221736"
FT MOD_RES 508
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:31221736"
FT MUTAGEN 330..331
FT /note="SS->AA: No effect on salt-induced B'KAPPA protein
FT accumulation."
FT /evidence="ECO:0000269|PubMed:31221736"
FT MUTAGEN 476
FT /note="T->A: No effect on salt-induced B'KAPPA protein
FT accumulation."
FT /evidence="ECO:0000269|PubMed:31221736"
FT MUTAGEN 493
FT /note="T->A: No effect on salt-induced B'KAPPA protein
FT accumulation."
FT /evidence="ECO:0000269|PubMed:31221736"
FT MUTAGEN 502
FT /note="S->A: Abolishes salt-induced B'KAPPA protein
FT accumulation."
FT /evidence="ECO:0000269|PubMed:31221736"
FT MUTAGEN 508
FT /note="T->A: Reduces salt-induced B'KAPPA protein
FT accumulation."
FT /evidence="ECO:0000269|PubMed:31221736"
SQ SEQUENCE 510 AA; 57468 MW; 7BEE942851DAC2B4 CRC64;
MWKGFLSKLP RKTSASGRGA DLDSGQCSNG AGNGNPIQRT SSCGSIPSGR STSTIKRMSS
AIFPSSVVAG IEPLVSFKDV PNSEKQNLFV SKLNLCCAVF DFSDPNKSSA EKDIKRQTLL
DLIDYVDSSS SRFSEAVIAA SSRMFAVNLF RVFPPNYRSS SSGGGEGEEE EPMFEPAWCH
LQLVYELLLK FIGSSSLDAK VGKKYFDHSF IVKLLNLLDS EDPRERDCLK TILHRIYGKF
MVHRPFIRKA VSNIFYHFVF ETDRHNGIAE LLEVFGSVIS GFALPLKEEH KIFLWRVLVP
LHKPKSVGVY LQQLTYCVTQ FIEKDPKLAS SVIIGLLRYW PITNSQKEVM FLSEIEEILE
TISTAEFQKC MVPLFRRIAQ CIKSSHFQVA ERALFIWNND NVISLIAQNR QMIMPIIVPA
LEHNSQNHWN QAVLNLTDNV KKMFSEMDDV LFSACLVKYK EDEERQASLE SKRRLTWEKL
ESAASFQPVT GHTAVLVGRQ PSANLIATLI
