SA155_YEAST
ID SA155_YEAST Reviewed; 1002 AA.
AC P43612; D6VTS3; Q96VG4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 4.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=SIT4-associating protein SAP155;
GN Name=SAP155; OrderedLocusNames=YFR040W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, INTERACTION
RP WITH SIT4, AND PHOSPHORYLATION.
RX PubMed=8649382; DOI=10.1128/mcb.16.6.2744;
RA Luke M.M., della Seta F., di Como C.J., Sugimoto H., Kobayashi R.,
RA Arndt K.T.;
RT "The SAPs, a new family of proteins, associate and function positively with
RT the SIT4 phosphatase.";
RL Mol. Cell. Biol. 16:2744-2755(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND IDENTIFICATION OF FRAMESHIFT.
RX PubMed=11779790; DOI=10.1093/genetics/159.4.1479;
RA Jablonowski D., Butler A.R., Fichtner L., Gardiner D., Schaffrath R.,
RA Stark M.J.R.;
RT "Sit4p protein phosphatase is required for sensitivity of Saccharomyces
RT cerevisiae to Kluyveromyces lactis zymocin.";
RL Genetics 159:1479-1489(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8686379;
RX DOI=10.1002/(sici)1097-0061(199602)12:2<149::aid-yea893>3.0.co;2-g;
RA Eki T., Naitou M., Hagiwara H., Ozawa M., Sasanuma S., Sasanuma M.,
RA Tsuchiya Y., Shibata T., Hanaoka F., Murakami Y.;
RT "Analysis of a 36.2 kb DNA sequence including the right telomere of
RT chromosome VI from Saccharomyces cerevisiae.";
RL Yeast 12:149-167(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
RN [5]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 663.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP FUNCTION.
RX PubMed=15367655; DOI=10.1128/mcb.24.19.8332-8341.2004;
RA Rohde J.R., Campbell S., Zurita-Martinez S.A., Cutler N.S., Ashe M.,
RA Cardenas M.E.;
RT "TOR controls transcriptional and translational programs via Sap-Sit4
RT protein phosphatase signaling effectors.";
RL Mol. Cell. Biol. 24:8332-8341(2004).
RN [9]
RP FUNCTION.
RX PubMed=15947196; DOI=10.1128/ec.4.6.1041-1049.2005;
RA Manlandro C.M.A., Haydon D.H., Rosenwald A.G.;
RT "Ability of Sit4p to promote K+ efflux via Nha1p is modulated by Sap155p
RT and Sap185p.";
RL Eukaryot. Cell 4:1041-1049(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-613 AND THR-618, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Positive regulator of protein phosphatase SIT4. Involved in
CC directing expression of TOR-repressed genes and in dephosphorylation of
CC NPR1 in response to nutrient starvation. Negatively modulates K(+)
CC efflux of the cell by the Na(+)-K(+)/H(+) antiporter NHA1.
CC {ECO:0000269|PubMed:15367655, ECO:0000269|PubMed:15947196}.
CC -!- SUBUNIT: Associates with the SIT4 protein phosphatase catalytic subunit
CC in a cell-cycle-dependent manner.
CC -!- INTERACTION:
CC P43612; P20604: SIT4; NbExp=9; IntAct=EBI-16370, EBI-13707;
CC P43612; Q12199: TIP41; NbExp=3; IntAct=EBI-16370, EBI-38123;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- PTM: Hyperphosphorylated in the absence of SIT4.
CC -!- MISCELLANEOUS: Present with 5960 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SAPS family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA09279.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U50560; AAC49303.1; -; Genomic_DNA.
DR EMBL; AJ318331; CAC42243.1; -; Genomic_DNA.
DR EMBL; D50617; BAA09279.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006940; DAA12483.2; -; Genomic_DNA.
DR RefSeq; NP_116698.3; NM_001180005.2.
DR AlphaFoldDB; P43612; -.
DR BioGRID; 31198; 347.
DR ComplexPortal; CPX-1864; SIT4-SAP155 phosphatase complex.
DR DIP; DIP-5852N; -.
DR IntAct; P43612; 45.
DR MINT; P43612; -.
DR STRING; 4932.YFR040W; -.
DR iPTMnet; P43612; -.
DR MaxQB; P43612; -.
DR PaxDb; P43612; -.
DR PRIDE; P43612; -.
DR EnsemblFungi; YFR040W_mRNA; YFR040W; YFR040W.
DR GeneID; 850601; -.
DR KEGG; sce:YFR040W; -.
DR SGD; S000001936; SAP155.
DR VEuPathDB; FungiDB:YFR040W; -.
DR eggNOG; KOG2073; Eukaryota.
DR GeneTree; ENSGT00390000009899; -.
DR HOGENOM; CLU_003676_2_1_1; -.
DR InParanoid; P43612; -.
DR OMA; DYDLNCG; -.
DR BioCyc; YEAST:G3O-30487-MON; -.
DR PRO; PR:P43612; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P43612; protein.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008287; C:protein serine/threonine phosphatase complex; IPI:ComplexPortal.
DR GO; GO:0019903; F:protein phosphatase binding; IEA:InterPro.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:SGD.
DR GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IBA:GO_Central.
DR InterPro; IPR007587; SAPS.
DR PANTHER; PTHR12634; PTHR12634; 1.
DR Pfam; PF04499; SAPS; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cytoplasm; Direct protein sequencing; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1002
FT /note="SIT4-associating protein SAP155"
FT /id="PRO_0000097561"
FT REGION 51..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..238
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..979
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..1002
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 613
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 618
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT CONFLICT 663
FT /note="N -> T (in Ref. 3 and 4; BAA09279)"
FT /evidence="ECO:0000305"
FT CONFLICT 668
FT /note="T -> G (in Ref. 2; CAC42243)"
FT /evidence="ECO:0000305"
FT CONFLICT 674..690
FT /note="DLFKIKLYDTRIVSKIM -> TYSKSNYMIRDCFQNN (in Ref. 1; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 815..824
FT /note="ELISPDIQVI -> DYISRYSSN (in Ref. 1; AAC49303)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1002 AA; 115002 MW; 50CDC17130333022 CRC64;
MSFWPFGQNL NHSNINKILD EYFHVLHELE RINPSVGKAI PAIFNNVQER GTSDSLDSIP
EEYSHGDEVK TARGDQKSRF EKDDQQERYE KEEEERSMNS SESSTTSFSS GSTSKTDLDE
EDISNATAPM MVTTKNLDNS FIERMLVETE LLNELSRQNK TLLDFICFGF FFDKKTNKKV
NNMEYLVDQL MECISKIKTA TTVDLNNLID YQEQQQLDDS SQEDVYVESD TEQEEEKEDD
NNSNNKKRRK RGSSSFGNDD INNNDDDDDA NEDDESAYLT KATIISEIFS LDIWLISESL
VKNQSYLNKI WSIINQPNFN SENSPLVPIF LKINQNLLLT RQDQYLNFIR TERSFVDDML
KHVDISLLMD FFLKIISTDK IESPTGIIEL VYDQNLISKC LSFLNNKESP ADIQACVGDF
LKALIAISAN APLDDISIGP NSLTRQLASP ESIAKLVDIM INQRGAALNT TVSIVIELIR
KNNSDYDQVN LLTTTIKTHP PSNRDPIYLG YLLRKFSNHL SDFFQIILDI ENDANIPLHE
NQLHEKFKPL GFERFKVVEL IAELLHCSNM GLMNSKRAER IARRRDKVRS QLSHHLQDAL
NDLSIEEKEQ LKTKHSPTRD TDHDLKNNNG KIDNDNNDND DESDYGDEID ESFEIPYINM
KQNIKLRTDP TVGDLFKIKL YDTRIVSKIM ELFLTHPWNN FWHNVIFDII QQIFNGRMDF
SYNSFLVLSL FNLKSSYQFM TDIVISDEKG TDVSRFSPVI RDPNFDFKIT TDFILRGYQD
SYKFYELRKM NLGYMGHIVL IAEEVVKFSK LYKVELISPD IQVILQTEEW QYYSEEVLNE
TRMMYSKILG GGSYIDDGNG NIIPQLPDNT TVLTPNGDAS NNNEILDSDT GSSNGTSGGG
QLINVESLEE QLSLSTESDL HNKLREMLIN RAQEDVDNKN TENGVFILGP PEDKNSNSNI
NNTNHNSNNS NNNDNNDNND NDNDNTRNYN EDADNDNDYD HE
