ID   2AD2_SCHPO              Reviewed;         627 AA.
AC   P78759;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1999, sequence version 2.
DT   25-MAY-2022, entry version 138.
DE   RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta 2 isoform;
DE   AltName: Full=PP2A, B subunit, B' delta 2 isoform;
GN   Name=par2; Synonyms=pbp2; ORFNames=SPAC6F12.12;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=11380623; DOI=10.1046/j.1365-2443.2001.00429.x;
RA   Tanabe O., Hirata D., Usui H., Nishito Y., Miyakawa T., Igarashi K.,
RA   Takeda M.;
RT   "Fission yeast homologues of the B' subunit of protein phosphatase 2A:
RT   multiple roles in mitotic cell division and functional interaction with
RT   calcineurin.";
RL   Genes Cells 6:455-473(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=10757751; DOI=10.1093/genetics/154.3.1025;
RA   Jiang W., Hallberg R.L.;
RT   "Isolation and characterization of par1(+) and par2(+): two
RT   Schizosaccharomyces pombe genes encoding B' subunits of protein phosphatase
RT   2A.";
RL   Genetics 154:1025-1038(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 215-627.
RC   STRAIN=PR745;
RX   PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA   Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT   "Identification of open reading frames in Schizosaccharomyces pombe
RT   cDNAs.";
RL   DNA Res. 4:363-369(1997).
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. Has a role in
CC       cell shape control and septum formation. {ECO:0000269|PubMed:10757751,
CC       ECO:0000269|PubMed:11380623}.
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       {ECO:0000269|PubMed:11380623}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B family.
CC       {ECO:0000305}.
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DR   EMBL; AB041232; BAB40598.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB11096.1; -; Genomic_DNA.
DR   EMBL; D89107; BAA13770.1; -; mRNA.
DR   PIR; T11663; T11663.
DR   RefSeq; NP_593298.1; NM_001018728.2.
DR   AlphaFoldDB; P78759; -.
DR   SMR; P78759; -.
DR   BioGRID; 279335; 61.
DR   STRING; 4896.SPAC6F12.12.1; -.
DR   iPTMnet; P78759; -.
DR   MaxQB; P78759; -.
DR   PaxDb; P78759; -.
DR   EnsemblFungi; SPAC6F12.12.1; SPAC6F12.12.1:pep; SPAC6F12.12.
DR   GeneID; 2542891; -.
DR   KEGG; spo:SPAC6F12.12; -.
DR   PomBase; SPAC6F12.12; par2.
DR   VEuPathDB; FungiDB:SPAC6F12.12; -.
DR   eggNOG; KOG2085; Eukaryota.
DR   HOGENOM; CLU_012437_1_2_1; -.
DR   InParanoid; P78759; -.
DR   OMA; QDRRMQM; -.
DR   PhylomeDB; P78759; -.
DR   Reactome; R-SPO-389513; CTLA4 inhibitory signaling.
DR   Reactome; R-SPO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   PRO; PR:P78759; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0032153; C:cell division site; IDA:PomBase.
DR   GO; GO:0051286; C:cell tip; IDA:PomBase.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000159; C:protein phosphatase type 2A complex; TAS:PomBase.
DR   GO; GO:0019888; F:protein phosphatase regulator activity; TAS:PomBase.
DR   GO; GO:0031030; P:negative regulation of septation initiation signaling; IMP:PomBase.
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   1: Evidence at protein level;
KW   Cytoplasm; Nucleus; Reference proteome.
FT   CHAIN           1..627
FT                   /note="Serine/threonine-protein phosphatase 2A 56 kDa
FT                   regulatory subunit delta 2 isoform"
FT                   /id="PRO_0000071470"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   627 AA;  72465 MW;  82AD6FD5EA5097C3 CRC64;
     MKGLRSKFVK ALSLKDEQGS HKNGHSKSHY ISKNGSYVET DDVKHTDTHH SSKHELKKLK
     SHFLKDTLKH KRNHHANSNN EKHENSDKKI HTTVLASGHE DSDYSTFLPV IETSKVKDAN
     HFPPNYPEPK NDSVSSNIDE FPNDSISSAS FLSVPQSTPP YLVSQPTPLN KFLAGAENVD
     IPHSLRPVPR REHSSQFQVS EKRTLVRLPS FDDVHTSERE ELFIKKLEQC NIIFDFNDPS
     SDLASKEIKR EALLQMIDYV SENRGISSAS LFPYVVNTFS LNVFRPISPA LNDYSSDMFA
     LDDEPFLEPA WPHLEEVYLL FIKFLESPDF RASKAKSLVD RRFFNRLLAL FDTEDPRERE
     LLKTTLHRIY GKFLNLRSYI RKSMNNVFLQ FIYEREKFHG IAELLEILGS IINGFAVPLK
     EEHKIFLSKV LIPLHQTKSV FLYHPQLTYC IVQFIDKDPS LTKAVLTGIL KYWPRINSFK
     ELLFLNEIED IFEVLEPSEF VNIMSPLFQQ LARSISSMHF QVAERALCLW SNEYFTSLVS
     QNVVTLLPII YPSLYKTANE HWNSTIQAIA CNVLQIFVDM DADFFNGLVE DYKQAIIKQE
     EVMIIRKQQW CQIEALAAEN KPTDYLR