ID   P4R2B_XENLA             Reviewed;         398 AA.
AC   Q6DCQ0;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Serine/threonine-protein phosphatase 4 regulatory subunit 2-B;
GN   Name=ppp4r2-b;
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=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-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; BC077952; AAH77952.1; -; mRNA.
DR   RefSeq; NP_001087055.1; NM_001093586.1.
DR   AlphaFoldDB; Q6DCQ0; -.
DR   PRIDE; Q6DCQ0; -.
DR   DNASU; 446890; -.
DR   GeneID; 446890; -.
DR   KEGG; xla:446890; -.
DR   CTD; 446890; -.
DR   Xenbase; XB-GENE-6255088; ppp4r2.S.
DR   OMA; PMEDTPV; -.
DR   OrthoDB; 774806at2759; -.
DR   Proteomes; UP000186698; Chromosome 4S.
DR   Bgee; 446890; Expressed in blastula 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..398
FT                   /note="Serine/threonine-protein phosphatase 4 regulatory
FT                   subunit 2-B"
FT                   /id="PRO_0000299373"
FT   REGION          138..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..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        283..307
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..335
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..386
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   398 AA;  43957 MW;  CEA36FCD2B00CD53 CRC64;
     MDVDRLQEAL KDFEKRGKKD VSPELDQFLC HVAKTGETVV QWPQFKEYFL FKLEKVMDDF
     RTSAPEQRGP PNPNVEYIPF DEMKQRILKI VASFNGTPFT IQRLCELLTD PRRNYTGTDK
     FLRGVEKNIM VVSCVYPSSE KNTSPSLNRM NGVMFPSNSQ SYTDRSNVNG PGTPRPTNRP
     KFTLSSPMNT NGLPDSMENK ESDLQQKEKS LSDSAVFDDG SQATTPKNKH SAEDSVEAEE
     HEVKRLKFDT EEDEEAACAN PDASSEVSTE MAEEAECAST SADKGKESCQ TAQTADEESL
     MTASESTEVE CNERDSETVS VSEESSEESH QMEESEQSES ACSLNSEEPN SAAAAASTAG
     TDSSEGNIGI KSTEILSLSP MENSEEATNA PEEPMEQD