ID B6K406_SCHJY Unreviewed; 625 AA.
AC B6K406;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 2.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit {ECO:0000256|PIRNR:PIRNR028043};
GN Name=par2 {ECO:0000313|JaponicusDB:SJAG_03353};
GN ORFNames=SJAG_03353 {ECO:0000313|EMBL:EEB08213.2};
OS Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=402676 {ECO:0000313|EMBL:EEB08213.2, ECO:0000313|Proteomes:UP000001744};
RN [1] {ECO:0000313|EMBL:EEB08213.2, ECO:0000313|Proteomes:UP000001744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=yFS275 / FY16936 {ECO:0000313|Proteomes:UP000001744};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
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:0000256|PIRNR:PIRNR028043}.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit.
CC {ECO:0000256|PIRNR:PIRNR028043}.
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DR EMBL; KE651167; EEB08213.2; -; Genomic_DNA.
DR RefSeq; XP_002174506.2; XM_002174470.2.
DR AlphaFoldDB; B6K406; -.
DR STRING; 402676.B6K406; -.
DR EnsemblFungi; EEB08213; EEB08213; SJAG_03353.
DR GeneID; 7050075; -.
DR JaponicusDB; SJAG_03353; par2.
DR VEuPathDB; FungiDB:SJAG_03353; -.
DR eggNOG; KOG2085; Eukaryota.
DR HOGENOM; CLU_012437_1_2_1; -.
DR OMA; MRKHINN; -.
DR OrthoDB; 5473951at2759; -.
DR Proteomes; UP000001744; Unassembled WGS sequence.
DR GO; GO:0032153; C:cell division site; IEA:EnsemblFungi.
DR GO; GO:0051286; C:cell tip; IEA:EnsemblFungi.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IEA:UniProtKB-UniRule.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IEA:UniProtKB-UniRule.
DR GO; GO:1902426; P:deactivation of mitotic spindle assembly checkpoint; IEA:EnsemblFungi.
DR GO; GO:0031030; P:negative regulation of septation initiation signaling; IEA:EnsemblFungi.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002554; PP2A_B56.
DR PANTHER; PTHR10257; SERINE/THREONINE PROTEIN PHOSPHATASE 2A PP2A REGULATORY SUBUNIT B; 1.
DR PANTHER; PTHR10257:SF3; WELL-ROUNDED, ISOFORM B; 1.
DR Pfam; PF01603; B56; 1.
DR PIRSF; PIRSF028043; PP2A_B56; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001744}.
FT REGION 1..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 625 AA; 71667 MW; C888B80FD44FF773 CRC64;
MKGFKNKVVR ALSFKDDSSS ENKSGNSSRK MKGHDGSSKS KKEKDSSSSK SEKAEKSSRK
HKFSSSDKSS SSKDIRKQNS YDKIGIERSD SPSSSTNAAS KKSGTSTPTQ TTTNVPSRAP
TPIQKEPDLL KLPIATPIAS APSSPIDKLL TSGADVDLPE SLPTGPRRQP SSQFQVSEQR
VLQRLPAFHE VSSSRRQELF IKKLEQCNVI FDFTDPSSDL ASKEIKREAL QQLLEYITNN
RNVLTPALYP HIVHTFAVNL FRTIPPPVNE DIESFDPEED DYYLEPAWPH LQGVYLLFIK
FLESPDFSTS KAKPYIDHKF FTRLLSLFDT EDPRERDLLK TTLHRIYGKF LNLRCYIRKS
MNFVFFQYIY EQERFNGIAE LLEILGSIVN GFAIPLKEEH KTFLTRVLIP LHKAKTLYLY
HPQLAYCIVQ FLDKDSTLTK DVVLGLLKYW PRVNSAKEIM FLNEIEDIFE VLEPSEFPNI
QVPLFQQLSK SIASSHFQVA ERALCLWNNE YFTSLVSDNL PTILPIIYPT LYENSKNHWN
RTIQSMTYGV LRMFIDLNPA LFDKVVTEHQ RKLNEQKRMQ SERTKAWENI EDAAEKNLDK
LKSRDDVEYL DVSSDLEMGN LSLNE
//
