ID   P4R2A_XENLA             Reviewed;         403 AA.
AC   Q5M7D6;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Serine/threonine-protein phosphatase 4 regulatory subunit 2-A;
GN   Name=ppp4r2-a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulatory subunit of serine/threonine-protein phosphatase 4
CC       (PP4). {ECO:0000250}.
CC   -!- SUBUNIT: Serine/threonine-protein phosphatase 4 (PP4) occurs in
CC       different assemblies of the catalytic and one or more regulatory
CC       subunits. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PPP4R2 family. {ECO:0000305}.
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DR   EMBL; BC088694; AAH88694.1; -; mRNA.
DR   RefSeq; NP_001088887.1; NM_001095418.1.
DR   AlphaFoldDB; Q5M7D6; -.
DR   MaxQB; Q5M7D6; -.
DR   DNASU; 496232; -.
DR   GeneID; 496232; -.
DR   KEGG; xla:496232; -.
DR   CTD; 496232; -.
DR   Xenbase; XB-GENE-6252224; ppp4r2.L.
DR   OrthoDB; 774806at2759; -.
DR   Proteomes; UP000186698; Chromosome 4L.
DR   Bgee; 496232; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0030289; C:protein phosphatase 4 complex; IEA:InterPro.
DR   GO; GO:0019888; F:protein phosphatase regulator activity; IEA:InterPro.
DR   InterPro; IPR015267; PPP4R2.
DR   PANTHER; PTHR16487; PTHR16487; 1.
DR   Pfam; PF09184; PPP4R2; 1.
PE   2: Evidence at transcript level;
KW   Reference proteome.
FT   CHAIN           1..403
FT                   /note="Serine/threonine-protein phosphatase 4 regulatory
FT                   subunit 2-A"
FT                   /id="PRO_0000299372"
FT   REGION          140..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..170
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..214
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..229
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..254
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..307
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..337
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..360
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..389
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   403 AA;  44554 MW;  FE8A51BDF31808E1 CRC64;
     MDVDRLQEAL KDFEKRGKKE VSPELDQFLC HVAKTGETVV QWPQFKEYFV FKLEMVMDDF
     RTSAPEQRGS PNPNVEYIPF DEMKQRILKI VTGFNGTPFT IQRLCELLTD PRKNYNGTDK
     FLRGVEKNIM VVSCVYPSSE KNNSTSLNRM NGVMFPSNSQ SYTDRSNVNG PGTPRPMIRP
     KFSLSSPMNT NGLPDSTENK ESDLQQKEKS QSDSAVSDDG SQATTSRNKH SAEDSAEVEE
     HEVKRLKFDP DEEEEAACAN PDASSEVSAE MAEEAESAST SADKGKESCQ TAQASDEESL
     MTASESTEAE SNERDSENVS VTEESSEESH HMDQSEESES ACSLTSDEHN STAAATTSTE
     DADPSEEEHL ATSSGKSTET LTLSPMENSE EATDAPEEPM EQD