ID   SA190_YEAS8             Reviewed;        1033 AA.
AC   C8ZCJ2;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=SIT4-associating protein SAP190;
GN   Name=SAP190; ORFNames=EC1118_1K5_2872g;
OS   Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's
OS   yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=643680;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lalvin EC1118 / Prise de mousse;
RX   PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA   Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambon B.,
RA   Legras J.-L., Wincker P., Casaregola S., Dequin S.;
RT   "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT   sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009).
CC   -!- FUNCTION: Positive regulator of protein phosphatase SIT4. Involved in
CC       the general amino acid control (GAAC) response regulated by TOR.
CC       Involved in the dephosphorylation of the elongator complex subunit IKI3
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Associates with the SIT4 protein phosphatase catalytic subunit
CC       in a cell-cycle-dependent manner. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- PTM: Hyperphosphorylated in the absence of SIT4. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SAPS family. {ECO:0000305}.
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DR   EMBL; FN393077; CAY81108.1; -; Genomic_DNA.
DR   AlphaFoldDB; C8ZCJ2; -.
DR   EnsemblFungi; CAY81108; CAY81108; EC1118_1K5_2872g.
DR   HOGENOM; CLU_003676_2_0_1; -.
DR   Proteomes; UP000000286; Chromosome XI, Scaffold EC1118_1K5.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019903; F:protein phosphatase binding; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IEA:InterPro.
DR   InterPro; IPR007587; SAPS.
DR   PANTHER; PTHR12634; PTHR12634; 1.
DR   Pfam; PF04499; SAPS; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cytoplasm; Phosphoprotein.
FT   CHAIN           1..1033
FT                   /note="SIT4-associating protein SAP190"
FT                   /id="PRO_0000393320"
FT   REGION          32..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          147..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          768..813
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          828..1033
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..78
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..174
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..197
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        773..787
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        795..813
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        856..892
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        893..921
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        965..979
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        998..1018
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         774
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P36123"
FT   MOD_RES         857
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P36123"
FT   MOD_RES         862
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P36123"
FT   MOD_RES         892
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P36123"
FT   MOD_RES         990
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P36123"
FT   MOD_RES         991
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P36123"
SQ   SEQUENCE   1033 AA;  117120 MW;  99E5F17DC46654C7 CRC64;
     MSGSFWKFGQ DYSIESPVSK ILNSAFIKIN KDQDDDVPTG TCEENIADDE DNSSHDYAAS
     EDNVVNENEE KEEENTLPTT ESEYENYRPN LDVLDDLLDD DELYTELMCS NFKLLIFLKY
     PEVLSKLIEY VTNEKILDEE TDSAKKPEII EGVNDHPILI ERDRKDKKED AEEGGDSEET
     TNDSDHDSGD ERSVDSEETS ITLPPESEEQ VETRRARIAA EILSADVWPI SAAIMQNKDL
     LGRLWSILDH PAPLPIPAST YFMKINERLL DMDITGMLEF ILSRDSLVAR FLTHVDNPSL
     MDFLLKVIST DKPDSPTGVI KILKSQELIP KLLDHLNPEY GISTQSAAGD FIKAFVTLST
     NSSNELASGI GPNELTRQLV SEEMIEKLIK IMLKGGTSLS NGVGIIIELI RKNNSDYDFI
     QLVYTTLESH PPTDRDPIHL IHLVKLFAKH MPDFADMLDK TKLPLMEMPF GNIEPLGFER
     FKICELIAEL LHCSNMTLLN EPNGEMIAQE RDIERAKELE TSTEKENITA IVDNKSSYYD
     KDCVEKDITE NLGALQINNQ GSEEDELNDT GVSSVKLDVK SDAKVVEGLE NDASGVELYD
     ETLSDTESVR ECLREKPLVG DRLKIALEDT KILISILDMF TEFPWNNFLH NVIFDIAQQI
     FNGPLKTGYN RFLLKDYLVD AYLTKKIVDA DKACQDYEKK TGLRHGYMGH LTLVAEEISK
     FKEYIDEMKL TFCNTAVSDR FEEPFWKEYS ETILADTREK YNTVLGDFGN DQESDDDVIR
     NSDSEDIIGD TEGNENYGNG ENDELLSNGH DSGNMDLYYN FNNNENEENE EDYAEYSDVD
     NKNYYNNVET NDDDYDSDDG KSKSAESEFT DKISEHRDGN SLYNEDNDEN GSDKWTSGTS
     LFPPDHFPSR SQPSDPKLQD QNIFHHQFDF EGVGDDDDYM DPNDDGQSYA RPGNPLYTTP
     KTPPRPKTIL FNSLSALDNN GEDEEVALGT SVDDRMDNEI SSDEEDSEDE DEENDMGNEE
     GYSLYRSRSK EAF