PP4R2_KLULA
ID PP4R2_KLULA Reviewed; 402 AA.
AC Q6CPD5;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Serine/threonine-protein phosphatase 4 regulatory subunit 2;
DE Short=PP4R2;
GN Name=PSY4; OrderedLocusNames=KLLA0E05676g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Regulatory subunit of the histone H2A phosphatase complex,
CC which dephosphorylates H2AS128ph (gamma-H2A) that has been displaced
CC from sites of DNA lesions in the double-stranded DNA break repair
CC process. Dephosphorylation is necessary for efficient recovery from the
CC DNA damage checkpoint (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Regulatory subunit (R2) of the histone H2A phosphatase complex
CC (HTP-C) consisting of PPH3, PSY2 and PSY4. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PPP4R2 family. {ECO:0000305}.
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DR EMBL; CR382125; CAG99291.1; -; Genomic_DNA.
DR RefSeq; XP_454204.1; XM_454204.1.
DR AlphaFoldDB; Q6CPD5; -.
DR STRING; 28985.XP_454204.1; -.
DR EnsemblFungi; CAG99291; CAG99291; KLLA0_E05721g.
DR GeneID; 2893683; -.
DR KEGG; kla:KLLA0_E05721g; -.
DR eggNOG; ENOG502S2WZ; Eukaryota.
DR HOGENOM; CLU_036743_1_0_1; -.
DR InParanoid; Q6CPD5; -.
DR OMA; NMMGIKS; -.
DR Proteomes; UP000000598; Chromosome E.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 Pfam; PF09184; PPP4R2; 1.
PE 3: Inferred from homology;
KW Nucleus; Reference proteome.
FT CHAIN 1..402
FT /note="Serine/threonine-protein phosphatase 4 regulatory
FT subunit 2"
FT /id="PRO_0000223654"
FT REGION 206..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..256
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 402 AA; 46356 MW; 1E37324E923DA4B5 CRC64;
MMGIKSRHLY DRLTKIVIDK DLSAFNEISP SQLIPQLSEH FSITIPKEIF NYNEDQEEDL
LHRLKELSRY LVVKFAKRDK YPFTIQRICE LSYHPLQYFP VHSLQKFVSA MEKCCLVNTD
WTPRLGKECP NTNPMEDVSL IPIEWIRTNK EDEKSLQAFI SKIETIVAVN FGYDDFDDDN
EDGTDHDIGR GYDNHGDVLI EEYEEMDEEF EDEDYEDHED EEEDEEDEDN DSDVDEMEAE
EVEEDASDDI SIGEIAENDD QDNAHTDVTD TQLKYNGVPI EEELRLSSTS SVLSVSSHAA
NEDENESILS RKRNVTELDD YQYKETKEND GFITTPKKSK MPLNEFGSSS SMVSPVVSNQ
EDPSRNDDSR INTFISPDTT NSVTQAEKNE LSTSPLQDKK RM