ID   2AD1_SCHPO              Reviewed;         548 AA.
AC   Q10428;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta 1 isoform;
DE   AltName: Full=PP2A, B subunit, B' delta 1 isoform;
GN   Name=par1; Synonyms=pbp1; ORFNames=SPCC188.02;
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, 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   [2]
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   [3]
RP   IDENTIFICATION, FUNCTION, SUBUNIT, AND SUBCELLULAR 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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-96; SER-99; SER-109 AND
RP   SER-542, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
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   -!- INTERACTION:
CC       Q10428; P13681: dis2; NbExp=12; IntAct=EBI-989357, EBI-4320127;
CC       Q10428; Q9UT08: paa1; NbExp=6; IntAct=EBI-989357, EBI-16132377;
CC       Q10428; Q9P7A0: sgo1; NbExp=4; IntAct=EBI-989357, EBI-989427;
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; CU329672; CAB41222.1; -; Genomic_DNA.
DR   PIR; T41182; T41182.
DR   RefSeq; NP_588206.1; NM_001023196.2.
DR   AlphaFoldDB; Q10428; -.
DR   SMR; Q10428; -.
DR   BioGRID; 275945; 304.
DR   DIP; DIP-36612N; -.
DR   IntAct; Q10428; 3.
DR   STRING; 4896.SPCC188.02.1; -.
DR   iPTMnet; Q10428; -.
DR   MaxQB; Q10428; -.
DR   PaxDb; Q10428; -.
DR   PRIDE; Q10428; -.
DR   EnsemblFungi; SPCC188.02.1; SPCC188.02.1:pep; SPCC188.02.
DR   GeneID; 2539379; -.
DR   KEGG; spo:SPCC188.02; -.
DR   PomBase; SPCC188.02; par1.
DR   VEuPathDB; FungiDB:SPCC188.02; -.
DR   eggNOG; KOG2085; Eukaryota.
DR   HOGENOM; CLU_012437_1_2_1; -.
DR   InParanoid; Q10428; -.
DR   OMA; CSHEYNE; -.
DR   PhylomeDB; Q10428; -.
DR   Reactome; R-SPO-198753; ERK/MAPK targets.
DR   Reactome; R-SPO-202670; ERKs are inactivated.
DR   Reactome; R-SPO-389513; CTLA4 inhibitory signaling.
DR   Reactome; R-SPO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   PRO; PR:Q10428; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0032153; C:cell division site; IDA:PomBase.
DR   GO; GO:0000775; C:chromosome, centromeric region; IDA:PomBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0000939; C:inner kinetochore; IDA:PomBase.
DR   GO; GO:0072687; C:meiotic spindle; IDA:PomBase.
DR   GO; GO:0110085; C:mitotic actomyosin contractile ring; IDA:PomBase.
DR   GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:PomBase.
DR   GO; GO:0072542; F:protein phosphatase activator activity; EXP:PomBase.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; EXP:PomBase.
DR   GO; GO:1990813; P:meiotic centromeric cohesion protection; IMP:PomBase.
DR   GO; GO:0031568; P:mitotic G1 cell size control checkpoint signaling; IMP:PomBase.
DR   GO; GO:0031030; P:negative regulation of septation initiation signaling; IMP:PomBase.
DR   GO; GO:0007089; P:traversing start control point of mitotic cell cycle; IMP:PomBase.
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; Phosphoprotein; Reference proteome.
FT   CHAIN           1..548
FT                   /note="Serine/threonine-protein phosphatase 2A 56 kDa
FT                   regulatory subunit delta 1 isoform"
FT                   /id="PRO_0000071469"
FT   REGION          1..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..39
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         96
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         99
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         109
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         542
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   548 AA;  63346 MW;  A15FD882D516F88A CRC64;
     MKGIKSKMLS RGKSQDTQKS SKKKESKKSN SHDSSKAPKE SPSTDPNGSV IGAQNDFLTV
     PKHSGKKVPI DTTPTPRDEI LLENVRTVRK QRSSLYHISE NRNLVRLPSF TDVPVNKWHS
     LALEKLEQCC VVFDFNDPST DLYGKEVKRE ALQDLIDLIS VRKEAIDESL YPSIVHMFAV
     NVFRPLPPPS NPPGEIMDLE EDEPALEVAW PHLHLVYDFF LRFFESPSLN TSVAKVYINQ
     KFIRKLLVLF DSEDPRERDF LKTTLHRIYG KFLSLRAFIR RSINNLFLQF VYENEQFNGI
     AELLEILGSI INGFALPLKE EHKIFLSRVL IPLHKAKSLP LYYPQIAYGI VQFVEKDSSV
     TEEVVLGLLR YWPKVNSSKE VLFLNEIEDI IEVMEPSEFL KIQVPLFHKL ATSISSQNFQ
     VAERALYFFN NDYFVHLVEE NVDIILPIIY PALFEISKSH WNRVIHSMVC NVLKLFMDIN
     PSLFDEVDAE YSESRRKKED EEIIREERWT ILENIAKENA MKLKSQNPTT VHSTTERLKK
     LSLDYTNG