2A5G_RABIT
ID 2A5G_RABIT Reviewed; 524 AA.
AC Q28651; Q28648; Q28650; Q28652;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform;
DE AltName: Full=PP2A B subunit isoform B'-beta;
DE AltName: Full=PP2A B subunit isoform B'-gamma;
DE AltName: Full=PP2A B subunit isoform B56-gamma;
DE AltName: Full=PP2A B subunit isoform PR61-gamma;
DE AltName: Full=PP2A B subunit isoform R5-gamma;
GN Name=PPP2R5C;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS GAMMA-1; GAMMA-3; GAMMA-4 AND
RP GAMMA-5).
RC STRAIN=New Zealand; TISSUE=Skeletal muscle;
RX PubMed=8576224; DOI=10.1074/jbc.271.5.2578;
RA Csortos C., Zolnierowicz S., Bako E., Durbin S.D., Depaoli-Roach A.A.;
RT "High complexity in the expression of the B' subunit of protein phosphatase
RT 2A0. Evidence for the existence of at least seven novel isoforms.";
RL J. Biol. Chem. 271:2578-2588(1996).
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. The PP2A-
CC PPP2R5C holoenzyme may activate TP53 and play a role in DNA damage-
CC induced inhibition of cell proliferation. PP2A-PPP2R5C may also
CC regulate the ERK signaling pathway through ERK dephosphorylation (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, composed
CC of PPP2CA a 36 kDa catalytic subunit (subunit C) and PPP2R1A a 65 kDa
CC constant regulatory subunit (PR65 or subunit A), that associates with a
CC variety of regulatory subunits. Proteins that associate with the core
CC dimer include three families of regulatory subunits B (the
CC R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48
CC kDa variable regulatory subunit, viral proteins, and cell signaling
CC molecules. Interacts with SGO1 (By similarity). Interacts with SGO1;
CC the interaction is direct. May interact with TP53 (By similarity).
CC Interacts with IER3 and/or ERK kinases; regulates ERK dephosphorylation
CC (By similarity) Interacts with CIP2A; this interaction stabilizes CIP2A
CC (By similarity). {ECO:0000250|UniProtKB:Q13362}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=Gamma-3; Synonyms=Beta-3;
CC IsoId=Q28651-1; Sequence=Displayed;
CC Name=Gamma-1; Synonyms=Beta-4;
CC IsoId=Q28651-2; Sequence=VSP_005116;
CC Name=Gamma-4; Synonyms=Beta-1;
CC IsoId=Q28651-3; Sequence=VSP_005114;
CC Name=Gamma-5; Synonyms=Beta-2;
CC IsoId=Q28651-4; Sequence=VSP_005115;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, heart and spleen. Also
CC found in brain and skeletal muscle.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56
CC family. {ECO:0000305}.
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DR EMBL; U38191; AAC48530.1; -; mRNA.
DR EMBL; U37770; AAC48528.1; -; mRNA.
DR EMBL; U38190; AAC48529.1; -; mRNA.
DR EMBL; U38192; AAC48531.1; -; mRNA.
DR RefSeq; NP_001075833.1; NM_001082364.1. [Q28651-1]
DR AlphaFoldDB; Q28651; -.
DR SMR; Q28651; -.
DR STRING; 9986.ENSOCUP00000023817; -.
DR Ensembl; ENSOCUT00000053898; ENSOCUP00000036260; ENSOCUG00000011221. [Q28651-3]
DR GeneID; 100009216; -.
DR KEGG; ocu:100009216; -.
DR CTD; 5527; -.
DR eggNOG; KOG2085; Eukaryota.
DR GeneTree; ENSGT01030000234620; -.
DR InParanoid; Q28651; -.
DR OrthoDB; 890437at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000011221; Expressed in autopod skin and 17 other tissues.
DR GO; GO:0000775; C:chromosome, centromeric region; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; ISS:UniProtKB.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IEA:InterPro.
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 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; Centromere; Chromosome; Nucleus;
KW Reference proteome.
FT CHAIN 1..524
FT /note="Serine/threonine-protein phosphatase 2A 56 kDa
FT regulatory subunit gamma isoform"
FT /id="PRO_0000071459"
FT REGION 476..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 472..489
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q13362"
FT VAR_SEQ 443..524
FT /note="YSLCSHASTVSMPLAMETDGPLFEDVQMLRKTVSDEARQAQKDPKKERPLAR
FT RKSELPQDPHTKKALEAHCRADELVPQDGR -> VLKKRAI (in isoform
FT Gamma-1)"
FT /evidence="ECO:0000303|PubMed:8576224"
FT /id="VSP_005116"
FT VAR_SEQ 482..524
FT /note="AQKDPKKERPLARRKSELPQDPHTKKALEAHCRADELVPQDGR -> QLVGR
FT KAVSSTQVRKV (in isoform Gamma-4)"
FT /evidence="ECO:0000303|PubMed:8576224"
FT /id="VSP_005114"
FT VAR_SEQ 482..524
FT /note="AQKDPKKERPLARRKSELPQDPHTKKALEAHCRADELVPQDGR -> VKVPG
FT (in isoform Gamma-5)"
FT /evidence="ECO:0000303|PubMed:8576224"
FT /id="VSP_005115"
SQ SEQUENCE 524 AA; 60985 MW; DC4520D122DAF386 CRC64;
MLTCNKAGSR MVVDAASSNG PFQPVALLHI RDVPPADQEK LFIQKLRQCC VLFDFVSDPL
SDLKWKEVKR AALSEMVEYI THNRNVITEP IYPEVVHMFA VNMFRTLPPS SNPTGAEFDP
EEDEPTLEAA WPHLQLVYEF FLRFLESPDF QPNIAKKYID QKFVLQLLEL FDSEDPRERD
FLKTTLHRIY GKFLGLRAYI RKQINNIFYR FIYETEHHNG IAELLEILGS IINGFALPLK
EEHKIFLLKV LLPLHKVKSL SVYHPQLAYC VVQFLEKDST LTEPVVMALL KYWPKTHSPK
EVMFLNELEE ILDVIEPSEF VKIMEPLFRQ LAKCVSSPHF QVAERALYYW NNEYIMSLIS
DNAAKILPIM FPSLYRNSKT HWNKTIHGLI YNALKLFMEM NQKLFDDCTQ QFKAEKLKEK
LKMKEREEAW VKIENLAKAN PQYSLCSHAS TVSMPLAMET DGPLFEDVQM LRKTVSDEAR
QAQKDPKKER PLARRKSELP QDPHTKKALE AHCRADELVP QDGR
