SIS2_YEAST
ID SIS2_YEAST Reviewed; 562 AA.
AC P36024; D6VXD3;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Phosphopantothenoylcysteine decarboxylase subunit SIS2;
DE AltName: Full=Halotolerance protein HAL3;
DE AltName: Full=Sit4 suppressor 2;
GN Name=SIS2; Synonyms=HAL3; OrderedLocusNames=YKR072C;
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].
RX PubMed=7705654; DOI=10.1093/genetics/139.1.95;
RA di Como C.J., Bose R., Arndt K.T.;
RT "Overexpression of SIS2, which contains an extremely acidic region,
RT increases the expression of SWI4, CLN1 and CLN2 in sit4 mutants.";
RL Genetics 139:95-107(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
RP GENOME REANNOTATION.
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 [4]
RP CHARACTERIZATION.
RX PubMed=7565698; DOI=10.1128/mcb.15.10.5470;
RA Ferrando A., Kron S.J., Rios G., Fink G.R., Serrano R.;
RT "Regulation of cation transport in Saccharomyces cerevisiae by the salt
RT tolerance gene HAL3.";
RL Mol. Cell. Biol. 15:5470-5481(1995).
RN [5]
RP IDENTIFICATION AS AN INHIBITORY SUBUNIT OF PPZ1.
RX PubMed=9636153; DOI=10.1073/pnas.95.13.7357;
RA de Nadal E., Clotet J., Posas F., Serrano R., Gomez N., Arino J.;
RT "The yeast halotolerance determinant Hal3p is an inhibitory subunit of the
RT Ppz1p Ser/Thr protein phosphatase.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:7357-7362(1998).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-50 AND SER-54, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-155, AND
RP IDENTIFICATION BY 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 [11]
RP FUNCTION, MUTAGENESIS OF HIS-378, AND INTERACTION WITH CAB3 AND VHS3.
RX PubMed=19915539; DOI=10.1038/nchembio.243;
RA Ruiz A., Gonzalez A., Munoz I., Serrano R., Abrie J.A., Strauss E.,
RA Arino J.;
RT "Moonlighting proteins Hal3 and Vhs3 form a heteromeric PPCDC with Ykl088w
RT in yeast CoA biosynthesis.";
RL Nat. Chem. Biol. 5:920-928(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-50; SER-54 AND
RP SER-56, AND IDENTIFICATION BY 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).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Component of the phosphopantothenoylcysteine decarboxylase
CC (PPCDC) involved in the coenzyme A synthesis. Acts as an inhibitory
CC subunit of protein phosphatase PPZ1, which is involved in many cellular
CC processes such as G1-S transition or salt tolerance. Also modulates the
CC expression of the ENA1 ATPase. {ECO:0000269|PubMed:19915539}.
CC -!- SUBUNIT: Interacts with the C-terminal domain of PPZ1. Component of the
CC phosphopantothenoylcysteine decarboxylase (PPCDC) complex, a
CC heterotrimer composed of CAB3, SIS2 and VHS3.
CC {ECO:0000269|PubMed:19915539}.
CC -!- INTERACTION:
CC P36024; P36076: CAB3; NbExp=8; IntAct=EBI-17250, EBI-26778;
CC P36024; P26570: PPZ1; NbExp=7; IntAct=EBI-17250, EBI-13807;
CC P36024; P36024: SIS2; NbExp=5; IntAct=EBI-17250, EBI-17250;
CC P36024; Q08438: VHS3; NbExp=3; IntAct=EBI-17250, EBI-30482;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 3750 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the HFCD (homooligomeric flavin containing Cys
CC decarboxylase) superfamily. {ECO:0000305}.
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DR EMBL; U01878; AAA80000.1; -; Genomic_DNA.
DR EMBL; Z28297; CAA82151.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09223.1; -; Genomic_DNA.
DR PIR; S38149; S38149.
DR RefSeq; NP_012998.1; NM_001179862.1.
DR AlphaFoldDB; P36024; -.
DR SMR; P36024; -.
DR BioGRID; 34203; 248.
DR ComplexPortal; CPX-393; Phosphopantothenoylcysteine decarboxylase complex.
DR DIP; DIP-2521N; -.
DR IntAct; P36024; 14.
DR MINT; P36024; -.
DR STRING; 4932.YKR072C; -.
DR MoonProt; P36024; -.
DR iPTMnet; P36024; -.
DR MaxQB; P36024; -.
DR PaxDb; P36024; -.
DR PRIDE; P36024; -.
DR EnsemblFungi; YKR072C_mRNA; YKR072C; YKR072C.
DR GeneID; 853946; -.
DR KEGG; sce:YKR072C; -.
DR SGD; S000001780; SIS2.
DR VEuPathDB; FungiDB:YKR072C; -.
DR eggNOG; KOG0672; Eukaryota.
DR GeneTree; ENSGT00940000176509; -.
DR HOGENOM; CLU_014402_1_0_1; -.
DR InParanoid; P36024; -.
DR OMA; KRHLKMI; -.
DR BioCyc; MetaCyc:MON3O-474; -.
DR BioCyc; YEAST:MON3O-474; -.
DR PRO; PR:P36024; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36024; protein.
DR GO; GO:0000785; C:chromatin; IDA:SGD.
DR GO; GO:1990143; C:CoA-synthesizing protein complex; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IC:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0071513; C:phosphopantothenoylcysteine decarboxylase complex; IDA:SGD.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; IDA:SGD.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IGI:SGD.
DR GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IDA:SGD.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IGI:SGD.
DR GO; GO:0009651; P:response to salt stress; IMP:SGD.
DR Gene3D; 3.40.50.1950; -; 1.
DR InterPro; IPR036551; Flavin_trans-like.
DR InterPro; IPR003382; Flavoprotein.
DR Pfam; PF02441; Flavoprotein; 1.
DR SUPFAM; SSF52507; SSF52507; 1.
PE 1: Evidence at protein level;
KW Coenzyme A biosynthesis; Cytoplasm; Nucleus; Phosphoprotein;
KW Protein phosphatase inhibitor; Reference proteome.
FT CHAIN 1..562
FT /note="Phosphopantothenoylcysteine decarboxylase subunit
FT SIS2"
FT /id="PRO_0000182037"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..553
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 378
FT /note="H->A: Abolishes PPCDC activity."
FT /evidence="ECO:0000269|PubMed:19915539"
SQ SEQUENCE 562 AA; 62478 MW; 19A9A475145DA7AB CRC64;
MTAVASTSGK QDADHNQSIE CPRFSRGQKE ILLDHEDAKG KDSIINSPVS GRQSISPTLS
NATTTTTKSI MNATGTSGAV VSNTPEPGLK RVPAVTFSDL KQQQKQDSLT QLKNDSERTK
SPNSNPAPVS NSIPGNHAVI PNHTNTSRTT QLSGSPLVNE MKDYDPKKKD SALKIVDTMK
PDKIMATSTP ISRENNKVTA KAPTSITLRK EDAQDQANNV SGQINVRSTP EETPVKQSVI
PSIIPKRENS KNLDPRLPQD DGKLHVLFGA TGSLSVFKIK PMIKKLEEIY GRDRISIQVI
LTQSATQFFE QRYTKKIIKS SEKLNKMSQY ESTPATPVTP TPGQCNMAQV VELPPHIQLW
TDQDEWDAWK QRTDPVLHIE LRRWADILVV APLTANTLSK IALGLCDNLL TSVIRAWNPS
YPILLAPSMV SSTFNSMMTK KQLQTIKEEM SWVTVFKPSE KVMDINGDIG LGGMMDWNEI
VNKIVMKLGG YPKNNEEEDD DEDEEEDDDE EEDTEDKNEN NNDDDDDDDD DDDDDDDDDD
DDDDDDEDED EAETPGIIDK HQ
