2A5D_RABIT
ID 2A5D_RABIT Reviewed; 586 AA.
AC Q28653; Q28655;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform;
DE AltName: Full=PP2A B subunit isoform B'-delta;
DE AltName: Full=PP2A B subunit isoform B'-gamma;
DE AltName: Full=PP2A B subunit isoform B56-delta;
DE AltName: Full=PP2A B subunit isoform PR61-delta;
DE AltName: Full=PP2A B subunit isoform R5-delta;
GN Name=PPP2R5D;
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].
RC STRAIN=New Zealand; TISSUE=Brain, and 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.
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). Interacts with ADCY8 (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q14738}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56
CC family. {ECO:0000305}.
CC -!- CAUTION: Nomenclature used in PubMed:8576224 refers to PP2A B subunit
CC B' gamma isoform, which is cited as PP2A B subunit delta-PR61 isoform
CC in later publications. {ECO:0000305}.
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DR EMBL; U38193; AAC48532.1; -; mRNA.
DR EMBL; U38195; AAC48534.1; -; mRNA.
DR RefSeq; NP_001076223.1; NM_001082754.1.
DR AlphaFoldDB; Q28653; -.
DR SMR; Q28653; -.
DR STRING; 9986.ENSOCUP00000001342; -.
DR GeneID; 100009533; -.
DR KEGG; ocu:100009533; -.
DR CTD; 5528; -.
DR eggNOG; KOG2085; Eukaryota.
DR InParanoid; Q28653; -.
DR OrthoDB; 890437at2759; -.
DR BRENDA; 3.1.3.16; 1749.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IEA:InterPro.
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 Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..586
FT /note="Serine/threonine-protein phosphatase 2A 56 kDa
FT regulatory subunit delta isoform"
FT /id="PRO_0000071453"
FT REPEAT 21..22
FT /note="1"
FT REPEAT 23..24
FT /note="2"
FT REPEAT 25..26
FT /note="3"
FT REPEAT 27..28
FT /note="4"
FT REPEAT 29..30
FT /note="5"
FT REPEAT 31..32
FT /note="6"
FT REPEAT 33..34
FT /note="7; approximate"
FT REPEAT 35..36
FT /note="8"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 21..36
FT /note="8 X 2 AA approximate tandem repeats of Q-P"
FT MOTIF 507..514
FT /note="SH3-binding; class I"
FT /evidence="ECO:0000255"
FT MOTIF 532..549
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 23..37
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14738"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14738"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14738"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14738"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14738"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14738"
SQ SEQUENCE 586 AA; 68090 MW; E149A309CDDA7495 CRC64;
MSPSPSSSGK DGGGENAEEA QPQPQPQPQP QPQSQPPSSN KRPSNSTPPP TQLSKIKYSG
GPQIVKKERR QSSSRFNLSK NRELQKLPAL KDSPTQEREE LFIQKLRQCC VLFDFVSDPL
SDLKFKEVKR AGLNEMVEYI THSRDVVTEA IYPEAVTMFS VNLFRTLPPS SNPTGAEFDP
EEDEPTLEAA WPHLQLVYEF FLRFLESPDF QPNIAKKYID QKFVLALLDL FDSEDPRERD
FLKTILHRIY GKFLGLRAYI RRQINHIFYR FIYETEHHNG IAELLEILGS IINGFALPLK
EEHKMFLIRV LLPLHKVKSL SVYHPQLAYC VVQFLEKESS LTEPVIVGLL KFWPKTHSPK
EVMFLNELEE ILDVIEPSEF SKVMEPLFRQ LAKCVSSPHF QVAERALYYW NNEYIMSLIS
DNAARVLPIM FPALYRNSKS HWNKTIHGLI YNALKLFMEM NQKLFDDCTQ QYKAEKQKGR
FRMKEREEMW QKIEELARLN PQYPMFRAPP PLPPVYSMET ETPTAEDIQL LKRTVETEAV
QMLKDIKKEK VLLRRKSELP QDVYTIKALE AHKRAEEFLT ASQEAL
