2A5E_BOVIN
ID 2A5E_BOVIN Reviewed; 467 AA.
AC A4FV68;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform;
DE AltName: Full=PP2A B subunit isoform B'-epsilon;
DE AltName: Full=PP2A B subunit isoform B56-epsilon;
DE AltName: Full=PP2A B subunit isoform PR61-epsilon;
DE AltName: Full=PP2A B subunit isoform R5-epsilon;
GN Name=PPP2R5E;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RA Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., Siddiqui A.,
RA Holt R., Jones S.J., Marra M.A.;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION IN A COMPLEX WITH ARL2; PPP2CB; PPP2R1A; PPP2R2A AND TBCD,
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12912990; DOI=10.1074/jbc.m308678200;
RA Shern J.F., Sharer J.D., Pallas D.C., Bartolini F., Cowan N.J., Reed M.S.,
RA Pohl J., Kahn R.A.;
RT "Cytosolic Arl2 is complexed with cofactor D and protein phosphatase 2A.";
RL J. Biol. Chem. 278:40829-40836(2003).
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: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), the 48 kDa variable
CC regulatory subunit, viral proteins, and cell signaling molecules.
CC Interacts with SGO1 (By similarity). Found in a complex with at least
CC ARL2, PPP2CB; PPP2R1A, PPP2R2A, PPP2R5E and TBCD. {ECO:0000250,
CC ECO:0000269|PubMed:12912990}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12912990}.
CC -!- PTM: Phosphorylated on serine residues. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC123807; AAI23808.1; -; mRNA.
DR RefSeq; NP_001076937.1; NM_001083468.1.
DR RefSeq; XP_005212050.1; XM_005211993.3.
DR AlphaFoldDB; A4FV68; -.
DR SMR; A4FV68; -.
DR STRING; 9913.ENSBTAP00000026361; -.
DR PaxDb; A4FV68; -.
DR PRIDE; A4FV68; -.
DR Ensembl; ENSBTAT00000026361; ENSBTAP00000026361; ENSBTAG00000019784.
DR GeneID; 533617; -.
DR KEGG; bta:533617; -.
DR CTD; 5529; -.
DR VEuPathDB; HostDB:ENSBTAG00000019784; -.
DR VGNC; VGNC:33264; PPP2R5E.
DR eggNOG; KOG2085; Eukaryota.
DR GeneTree; ENSGT01030000234620; -.
DR HOGENOM; CLU_012437_4_0_1; -.
DR InParanoid; A4FV68; -.
DR OMA; GADNNCK; -.
DR OrthoDB; 890437at2759; -.
DR TreeFam; TF105556; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000019784; Expressed in spermatid and 106 other tissues.
DR ExpressionAtlas; A4FV68; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IBA:GO_Central.
DR GO; GO:0072542; F:protein phosphatase activator activity; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
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 Acetylation; Cytoplasm; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q16537"
FT CHAIN 2..467
FT /note="Serine/threonine-protein phosphatase 2A 56 kDa
FT regulatory subunit epsilon isoform"
FT /id="PRO_0000405259"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q16537"
FT MOD_RES 7
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16537"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16537"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16537"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16537"
SQ SEQUENCE 467 AA; 54699 MW; DD9CE11433F499CF CRC64;
MSSAPTTPPS VDKVDGFSRK SVRKARQKRS QSSSQFRSQG KPIELTPLPL LKDVPSSEQP
ELFLKKLQQC CVIFDFMDTL SDLKMKEYKR STLNELVDYI TISRGCLTEQ TYPEVVRMVS
CNIFRTLPPS DSNEFDPEED EPTLEASWPH LQLVYEFFIR FLESQEFQPS IAKKYIDQKF
VLQLLELFDS EDPRERDYLK TVLHRIYGKF LGLRAFIRKQ INNIFLRFVY ETEHFNGVAE
LLEILGSIIN GFALPLKAEH KQFLVKVLIP LHTVRSLSLF HAQLAYCIVQ FLEKDPSLTE
PVIRGLMKFW PKTCSQKEVM FLGELEEILD VIEPSQFVKI QEPLFKQIAK CVSSPHFQVA
ERALYYWNNE YIMSLIEENS NVILPIMFSS LYRISKEHWN PAIVALVYNV LKAFMEMNST
MFDELTATYK SDRQREKKKE KEREELWKKL EDLELKRGLR RDGIIPT
