ID   SA190_YEAS6             Reviewed;        1033 AA.
AC   B5VMH6;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=SIT4-associating protein SAP190;
GN   Name=SAP190; ORFNames=AWRI1631_112520;
OS   Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=545124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AWRI1631;
RX   PubMed=18778279; DOI=10.1111/j.1567-1364.2008.00434.x;
RA   Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.;
RT   "Comparative genome analysis of a Saccharomyces cerevisiae wine strain.";
RL   FEMS Yeast Res. 8:1185-1195(2008).
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; ABSV01001499; EDZ70867.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5VMH6; -.
DR   Proteomes; UP000008988; Unassembled WGS sequence.
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_0000393319"
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;  117188 MW;  525C4A40AFA6D1E4 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 TSTEKENITF IVDNKSSYYD
     KDCVEKDITE NLGALQINNQ GSEEDELNDT GVSSVKLDVK SDAKVVEGLE NDASGVELYD
     ETLSDTESVR ECLREKPLVG DRLKIALEDT KILISILDMF TEFPWNNFLH NVIFDIAQQI
     FNGPLKTGYN RFLLKDYLVD AYLTKKIVDA DKACQDYEKK TGLRYGYMGH LTLVAEEISK
     FKEYIDEMKL TFCNTAVSDR LEEPFWKEYS 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