ID 2AAA_SCHPO Reviewed; 590 AA.
AC Q9UT08; Q10293;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 24-JAN-2024, entry version 138.
DE RecName: Full=Protein phosphatase PP2A regulatory subunit A;
DE AltName: Full=Protein phosphatase 2A 65 kDa regulatory subunit;
DE Short=PR65;
GN Name=paa1; ORFNames=SPAP8A3.09c;
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].
RX PubMed=9078365; DOI=10.1046/j.1365-2443.1996.02002.x;
RA Kinoshita K., Nemoto T., Nabeshima K., Kondoh H., Niwa H., Yanagida M.;
RT "The regulatory subunits of fission yeast protein phosphatase 2A (PP2A)
RT affect cell morphogenesis, cell wall synthesis and cytokinesis.";
RL Genes Cells 1:29-45(1996).
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).
CC -!- FUNCTION: Phosphatase 2A affects a variety of biological processes in
CC the cell such as transcription, cell cycle progression and cellular
CC morphogenesis, and provides an initial identification of critical
CC substrates for this phosphatase. The regulatory subunit may direct the
CC catalytic subunit to distinct, albeit overlapping, subsets of
CC substrates (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: PP2A exists in several trimeric forms, all of which consist of
CC a core composed of a catalytic subunit associated with a 65 kDa (PR65)
CC (Subunit A) and a 55 kDa (PR55) (Subunit B) regulatory subunit.
CC -!- INTERACTION:
CC Q9UT08; P13681: dis2; NbExp=10; IntAct=EBI-16132377, EBI-4320127;
CC Q9UT08; Q12702: pab1; NbExp=6; IntAct=EBI-16132377, EBI-16132256;
CC Q9UT08; Q10428: par1; NbExp=6; IntAct=EBI-16132377, EBI-989357;
CC -!- DOMAIN: Each HEAT repeat appears to consist of two alpha helices joined
CC by a hydrophilic region, the intrarepeat loop. The repeat units may be
CC arranged laterally to form a rod-like structure.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A family.
CC {ECO:0000305}.
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DR EMBL; D63916; BAA09946.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB55176.1; -; Genomic_DNA.
DR PIR; T39246; T39246.
DR PIR; T44416; T44416.
DR RefSeq; NP_594948.1; NM_001020379.2.
DR AlphaFoldDB; Q9UT08; -.
DR SMR; Q9UT08; -.
DR BioGRID; 279477; 152.
DR DIP; DIP-61474N; -.
DR IntAct; Q9UT08; 3.
DR STRING; 284812.Q9UT08; -.
DR MaxQB; Q9UT08; -.
DR PaxDb; 4896-SPAP8A3-09c-1; -.
DR EnsemblFungi; SPAP8A3.09c.1; SPAP8A3.09c.1:pep; SPAP8A3.09c.
DR GeneID; 2543042; -.
DR KEGG; spo:SPAP8A3.09c; -.
DR PomBase; SPAP8A3.09c; paa1.
DR VEuPathDB; FungiDB:SPAP8A3.09c; -.
DR eggNOG; KOG0211; Eukaryota.
DR HOGENOM; CLU_015533_2_1_1; -.
DR InParanoid; Q9UT08; -.
DR OMA; NRVEAMQ; -.
DR PhylomeDB; Q9UT08; -.
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 Reactome; R-SPO-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-SPO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:Q9UT08; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0090443; C:FAR/SIN/STRIPAK complex; IDA:PomBase.
DR GO; GO:0110085; C:mitotic actomyosin contractile ring; IDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; EXP:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:PomBase.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0061509; P:asymmetric protein localization to old mitotic spindle pole body; IMP:PomBase.
DR GO; GO:0030952; P:establishment or maintenance of cytoskeleton polarity; IMP:PomBase.
DR GO; GO:1990813; P:meiotic centromeric cohesion protection in anaphase I; IMP:PomBase.
DR GO; GO:0031030; P:negative regulation of septation initiation signaling; IMP:PomBase.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000357; HEAT.
DR InterPro; IPR021133; HEAT_type_2.
DR PANTHER; PTHR10648:SF4; PROTEIN PHOSPHATASE 2 (FORMERLY 2A), REGULATORY SUBUNIT A, BETA ISOFORM-RELATED; 1.
DR PANTHER; PTHR10648; SERINE/THREONINE-PROTEIN PHOSPHATASE PP2A 65 KDA REGULATORY SUBUNIT; 1.
DR Pfam; PF02985; HEAT; 1.
DR Pfam; PF13646; HEAT_2; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 11.
PE 1: Evidence at protein level;
KW Reference proteome; Repeat.
FT CHAIN 1..590
FT /note="Protein phosphatase PP2A regulatory subunit A"
FT /id="PRO_0000071413"
FT REPEAT 12..50
FT /note="HEAT 1"
FT /evidence="ECO:0000305"
FT REPEAT 89..127
FT /note="HEAT 2"
FT /evidence="ECO:0000305"
FT REPEAT 206..244
FT /note="HEAT 3"
FT /evidence="ECO:0000305"
FT REPEAT 246..284
FT /note="HEAT 4"
FT /evidence="ECO:0000305"
FT REPEAT 285..323
FT /note="HEAT 5"
FT /evidence="ECO:0000305"
FT REPEAT 324..362
FT /note="HEAT 6"
FT /evidence="ECO:0000305"
FT REPEAT 363..401
FT /note="HEAT 7"
FT /evidence="ECO:0000305"
FT REPEAT 402..440
FT /note="HEAT 8"
FT /evidence="ECO:0000305"
FT REPEAT 480..518
FT /note="HEAT 9"
FT /evidence="ECO:0000305"
FT REPEAT 519..551
FT /note="HEAT 10"
FT /evidence="ECO:0000305"
FT REPEAT 562..590
FT /note="HEAT 11"
FT /evidence="ECO:0000305"
FT CONFLICT 2..5
FT /note="QTEN -> LDNS (in Ref. 1; BAA09946)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="L -> R (in Ref. 1; BAA09946)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 590 AA; 66617 MW; 7F6337739B98CDC3 CRC64;
MQTENQVNDL YPIAVLIDEL KHDEITYRLN ALERLSTIAL ALGPERTRDE LIPFLDESID
DEDEVLSALA DQLGNFVDYV GGPEYAHVLL SPLENLAATE ETVVRDKAVD SLNKVCICLS
QEQLEQYFVP LVQRLSTAEW FTSRASSAGL YCAAYSQSEN PAVKVSLRQS FSHLCHDEAP
MVRRPAATNC AKFVFLVTKQ EAIDEFIPLF NSLSNDDQDS VRLLSFDIMV SLAEVLKSDS
EIRHYLLQPL RSFVSDSSWR TRYMVAANFV KLAKVVGPSL IKDELIKPFV LLMKDTEQEV
RRAIATQIPG FCELLDKRIV LEEIIPVIQE LINDPAQHVR AALGMNIGAL APQLGKEKTT
EYLLPMFLEL LKDENPEVRL NIISKLEVVN KVVGIELLSQ SLLPAIVTLA EDKQWRVRLA
IIDYIPLLAQ QLGVEFFNEK MGNLCMSWLE DHVYSIREAA IKNLRKLTEI FGLEWATETI
IPKFLAMRSH PNYLYRMTTI FAISEIAPAL NAEVIEKQIL PTLEQLVNDP IPNIRFNVAK
AFEVLKPVLA AGGDSTVYEQ QIIPLLEQLT KDNDPDVQYF ATQALEQTND
//
