ID A0A087G4K0_ARAAL Unreviewed; 444 AA.
AC A0A087G4K0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Serine/threonine protein phosphatase 2A regulatory subunit {ECO:0000256|PIRNR:PIRNR028043};
GN OrderedLocusNames=AALP_Aa8g026900 {ECO:0000313|EMBL:KFK24802.1};
OS Arabis alpina (Alpine rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Arabideae; Arabis.
OX NCBI_TaxID=50452 {ECO:0000313|EMBL:KFK24802.1, ECO:0000313|Proteomes:UP000029120};
RN [1] {ECO:0000313|Proteomes:UP000029120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pajares {ECO:0000313|Proteomes:UP000029120};
RX PubMed=27246759; DOI=10.1038/nplants.2014.23;
RA Willing E.M., Rawat V., Mandakova T., Maumus F., James G.V.,
RA Nordstroem K.J., Becker C., Warthmann N., Chica C., Szarzynska B.,
RA Zytnicki M., Albani M.C., Kiefer C., Bergonzi S., Castaings L.,
RA Mateos J.L., Berns M.C., Bujdoso N., Piofczyk T., de Lorenzo L.,
RA Barrero-Sicilia C., Mateos I., Piednoel M., Hagmann J., Chen-Min-Tao R.,
RA Iglesias-Fernandez R., Schuster S.C., Alonso-Blanco C., Roudier F.,
RA Carbonero P., Paz-Ares J., Davis S.J., Pecinka A., Quesneville H.,
RA Colot V., Lysak M.A., Weigel D., Coupland G., Schneeberger K.;
RT "Genome expansion of Arabis alpina linked with retrotransposition and
RT reduced symmetric DNA methylation.";
RL Nat. Plants 1:14023-14023(2015).
CC -!- FUNCTION: The B regulatory subunit might modulate substrate selectivity
CC and catalytic activity, and also might direct the localization of the
CC catalytic enzyme to a particular subcellular compartment.
CC {ECO:0000256|PIRNR:PIRNR028043}.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit.
CC {ECO:0000256|PIRNR:PIRNR028043}.
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DR EMBL; CM002876; KFK24802.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087G4K0; -.
DR EnsemblPlants; KFK24802; KFK24802; AALP_AA8G026900.
DR Gramene; KFK24802; KFK24802; AALP_AA8G026900.
DR Proteomes; UP000029120; Chromosome 8.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IEA:UniProtKB-UniRule.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002554; PP2A_B56.
DR PANTHER; PTHR10257; SERINE/THREONINE PROTEIN PHOSPHATASE 2A PP2A REGULATORY SUBUNIT B; 1.
DR PANTHER; PTHR10257:SF71; SERINE_THREONINE PROTEIN PHOSPHATASE 2A 57 KDA REGULATORY SUBUNIT B' ALPHA ISOFORM; 1.
DR Pfam; PF01603; B56; 1.
DR PIRSF; PIRSF028043; PP2A_B56; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000029120}.
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 444 AA; 51777 MW; 88BF1C193EF43A80 CRC64;
MKGGSRKLSR NESNDPSMFG FDPPNRSSLG GSNMVVNHAS RGSTVPLSPD TLKNAREKEI
KRQTLLELVD FIQSGPGKIN ETCQGEMVKM IGVNIFRCLP PASHENTGQE PADPEEEEPY
LEPSWPHLQL VYELLLRYIV PSDTDTKIAK RYIDHSFVLR LLELFETEDP REREYLKTIL
HRIYGKFMVH RPFIRKGINH IFYRFIYETE RHSGIGELLE ILGSIINGFA LPMKEEHKLF
LIRALIPLHK PKPIAMYHQQ LSYCIVQFVE KDYKLADTVI RGLLKFWPLT NCTKEVLFLN
ELEEVLEATQ PVEFQRCMVS LFQQIARCLN SSHFQVAERS LFLWNNEHVV GLIAQNRGVI
LPIIYSSLEK NIESHWNQAV HGLSSNIQRM FMEMDPELFE ECQLQYEEKL AKSKEVEEQR
QIRWKRLHEA VEERERIEDP MITS
//
