ID   PP4R3_KLULA             Reviewed;         749 AA.
AC   Q6CQ91;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Serine/threonine-protein phosphatase 4 regulatory subunit 3;
DE            Short=PP4R3;
GN   Name=PSY2; OrderedLocusNames=KLLA0D18887g;
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: Core regulatory subunit of the histone H2A phosphatase
CC       complex, which dephosphorylates H2AS128ph (gamma-H2A) that has been
CC       displaced from sites of DNA lesions in the double-stranded DNA break
CC       repair process. Dephosphorylation is necessary for efficient recovery
CC       from the DNA damage checkpoint (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Regulatory subunit 3 (R3) of the histone H2A phosphatase
CC       complex (HTP-C) consisting of PPH3, PSY2 and PSY4. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR382124; CAH00994.1; -; Genomic_DNA.
DR   RefSeq; XP_453898.1; XM_453898.1.
DR   AlphaFoldDB; Q6CQ91; -.
DR   STRING; 28985.XP_453898.1; -.
DR   EnsemblFungi; CAH00994; CAH00994; KLLA0_D18887g.
DR   GeneID; 2893105; -.
DR   KEGG; kla:KLLA0_D18887g; -.
DR   eggNOG; KOG2175; Eukaryota.
DR   HOGENOM; CLU_004909_4_0_1; -.
DR   InParanoid; Q6CQ91; -.
DR   OMA; YHRYMIS; -.
DR   Proteomes; UP000000598; Chromosome D.
DR   GO; GO:0000794; C:condensed nuclear chromosome; IEA:EnsemblFungi.
DR   GO; GO:0030289; C:protein phosphatase 4 complex; IEA:EnsemblFungi.
DR   GO; GO:0019888; F:protein phosphatase regulator activity; IEA:EnsemblFungi.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:EnsemblFungi.
DR   GO; GO:0051598; P:meiotic recombination checkpoint signaling; IEA:EnsemblFungi.
DR   GO; GO:2000002; P:negative regulation of DNA damage checkpoint; IEA:EnsemblFungi.
DR   GO; GO:1902660; P:negative regulation of glucose mediated signaling pathway; IEA:EnsemblFungi.
DR   GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; IEA:EnsemblFungi.
DR   Gene3D; 1.25.10.10; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR006887; DUF625.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   Pfam; PF04802; SMK-1; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   3: Inferred from homology;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..749
FT                   /note="Serine/threonine-protein phosphatase 4 regulatory
FT                   subunit 3"
FT                   /id="PRO_0000223657"
SQ   SEQUENCE   749 AA;  86516 MW;  5C68CE51D1D49581 CRC64;
     MSESNNMHVS GDGAKQSVYT EKKRVKVYVL ENNEWKDTGT GFCQGTVEER TIDDTQTAEK
     MAYLLVVDED SDDQVLLKSR LEQNIEYQRQ EETLIVWKDL NGQDIALSFE ESIGCDSLCE
     YICFVQKNIE SRISLVAVRS TDDGIGSVHE IITGPVNLPS NVPNQTEESL LEALKILNEN
     TSFDYLRNET IQFVINDHYL ATLIRSFYQS EESKLYRNLL LLSNIVKTLI LFNSKEILEE
     MINDENFLCV CGILEYDTEF PNSKLNHRQY LKDKEPNFKE MIPISDPTIK LMITQNFRLQ
     FLKDVVLVRF LDDQSFTFIS DLMLSYQNSI IDFLQEDSNN FINQVISMYK VEEDSTVTPD
     KRRDGIKLLH ECIQLSQNLN SIEKTLFYKF LIKKGLFQVI QFAFNMETNN DIRILATDIV
     VGLIEHDIQL IQSVQSDEVT LLNDENSDID STDMSLLLIL TKILLTDKSP GLKEQSFQAL
     VSLLDPEDYI VDDYQNHDDN IDTRIDNMLQ IQNGKNHDGL DGERNHEKFQ LAEYLQCFYR
     QVAPSLFHCF IDGSVNLYEC DQQLLIKLVK LLNLMIQGHE ASISRRFILE NGILIRLISL
     ASSDYILQLR LAAVRCFKNI VFLNDDFYLR YLIGKNLFDP IFEVFKENLN EDNMANSTIL
     DFLKSLNTQL KVVEQEDIPL SGSKSSRNFM LLNKYICGRY GDILLKADYV SFTREMMAIY
     HEETQKLASL STTETSFDEN DNTTLEVEV