VHS3_YEAST
ID VHS3_YEAST Reviewed; 674 AA.
AC Q08438; D6W2B8; O00019;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Phosphopantothenoylcysteine decarboxylase subunit VHS3;
DE AltName: Full=Viable in a HAL3 SIT4 background protein 3;
GN Name=VHS3; OrderedLocusNames=YOR054C; ORFNames=YOR29-05;
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=9133743;
RX DOI=10.1002/(sici)1097-0061(19970330)13:4<379::aid-yea85>3.0.co;2-g;
RA Valens M., Bohn C., Daignan-Fornier B., Dang V.-D., Bolotin-Fukuhara M.;
RT "The sequence of a 54.7 kb fragment of yeast chromosome XV reveals the
RT presence of two tRNAs and 24 new open reading frames.";
RL Yeast 13:379-390(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
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 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 [5]
RP FUNCTION.
RX PubMed=12518319; DOI=10.1002/yea.938;
RA Munoz I., Simon E., Casals N., Clotet J., Arino J.;
RT "Identification of multicopy suppressors of cell cycle arrest at the G1-S
RT transition in Saccharomyces cerevisiae.";
RL Yeast 20:157-169(2003).
RN [6]
RP FUNCTION, INTERACTION WITH PPZ1, AND MUTAGENESIS OF HIS-459.
RX PubMed=15192104; DOI=10.1074/jbc.m400572200;
RA Ruiz A., Munoz I., Serrano R., Gonzalez A., Simon E., Arino J.;
RT "Functional characterization of the Saccharomyces cerevisiae VHS3 gene. A
RT regulatory subunit of the Ppz1 protein phosphatase with novel, phosphatase-
RT unrelated functions.";
RL J. Biol. Chem. 279:34421-34430(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-90, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-90, 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 [9]
RP FUNCTION, MUTAGENESIS OF HIS-459, AND INTERACTION WITH CAB3 AND SIS2.
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 [10]
RP 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 [11]
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.
CC {ECO:0000269|PubMed:12518319, ECO:0000269|PubMed:15192104,
CC 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:15192104, ECO:0000269|PubMed:19915539}.
CC -!- INTERACTION:
CC Q08438; P36076: CAB3; NbExp=9; IntAct=EBI-30482, EBI-26778;
CC Q08438; P26570: PPZ1; NbExp=4; IntAct=EBI-30482, EBI-13807;
CC Q08438; P36024: SIS2; NbExp=3; IntAct=EBI-30482, EBI-17250;
CC Q08438; Q08438: VHS3; NbExp=4; IntAct=EBI-30482, EBI-30482;
CC -!- SIMILARITY: Belongs to the HFCD (homooligomeric flavin containing Cys
CC decarboxylase) superfamily. {ECO:0000305}.
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DR EMBL; Z70678; CAA94539.1; -; Genomic_DNA.
DR EMBL; Z74961; CAA99246.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10834.1; -; Genomic_DNA.
DR PIR; S66937; S66937.
DR RefSeq; NP_014697.1; NM_001183473.1.
DR AlphaFoldDB; Q08438; -.
DR SMR; Q08438; -.
DR BioGRID; 34453; 194.
DR ComplexPortal; CPX-393; Phosphopantothenoylcysteine decarboxylase complex.
DR DIP; DIP-4172N; -.
DR IntAct; Q08438; 15.
DR MINT; Q08438; -.
DR STRING; 4932.YOR054C; -.
DR MoonProt; Q08438; -.
DR iPTMnet; Q08438; -.
DR MaxQB; Q08438; -.
DR PaxDb; Q08438; -.
DR PRIDE; Q08438; -.
DR EnsemblFungi; YOR054C_mRNA; YOR054C; YOR054C.
DR GeneID; 854220; -.
DR KEGG; sce:YOR054C; -.
DR SGD; S000005580; VHS3.
DR VEuPathDB; FungiDB:YOR054C; -.
DR eggNOG; KOG0672; Eukaryota.
DR GeneTree; ENSGT00940000176509; -.
DR HOGENOM; CLU_014402_1_0_1; -.
DR InParanoid; Q08438; -.
DR OMA; ICIQVIL; -.
DR BioCyc; MetaCyc:MON3O-317; -.
DR BioCyc; YEAST:MON3O-317; -.
DR PRO; PR:Q08438; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08438; protein.
DR GO; GO:1990143; C:CoA-synthesizing protein complex; 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:0004864; F:protein phosphatase inhibitor activity; IDA:SGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030004; P:cellular monovalent inorganic cation homeostasis; IGI:SGD.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IGI: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; 2.
PE 1: Evidence at protein level;
KW Cell cycle; Coenzyme A biosynthesis; Phosphoprotein;
KW Protein phosphatase inhibitor; Reference proteome.
FT CHAIN 1..674
FT /note="Phosphopantothenoylcysteine decarboxylase subunit
FT VHS3"
FT /id="PRO_0000182038"
FT REGION 1..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..592
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..661
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 90
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT MUTAGEN 459
FT /note="H->A: Does not strongly affect the phosphatase
FT inhibitor function but abolishes PPCDC activity."
FT /evidence="ECO:0000269|PubMed:15192104,
FT ECO:0000269|PubMed:19915539"
SQ SEQUENCE 674 AA; 73649 MW; A97623473CB6F605 CRC64;
MTNKSSLKNN RKGVASNTLS GAEQANIGSS AMPDTNSTGP FSSVSSLDTP VVRKSTSPTG
SQTKSIMNAS GTSGAVVSNT PEPGLKRIPT VTFSDPKLGS LRSDVEQTPP NQVARQSSEK
KATSVHIAAE GANQGRNLKD INTKVPKDGE ASASSFSTPT SILSNADMGN NISSLLAKKL
SFTGGTDSIL NSDNSSDSPR KEHPHFYVED PLHTPSVRSR SNSTSPRPSV VVNTFNPINI
EREGSISKTG EPTLLESVLE EAMSPNAVSN PLKRENIMTN MDPRLPQDDG KLHVLFGATG
SLSVFKLKHM IRKLEEIYGR DKICIQVILT NSATKFFAMK YMRKNKKQHN SIDTSFNSTN
SNAGNITGNK KKVASLEKFS IQKTSSNSAA SQTNNKQEEE KQMASTTGFP STLGGSRTYS
NSSNVVSQHP QIELPAHIQF WTDQDEWDVW RQRTDPVLHI ELRRWADILV VAPLTANTLA
KIALGLCDNL LTSVIRAWNP TFPIFLAPSM GSGTFNSIMT KKHFRIIQEE MPWVTVFKPS
EKVMGINGDI GLSGMMDANE IVGKIVVKLG GYPDVSAGKE EEEDEDNDEE DDNKKNDTGG
KDEDNDDDDD DDDDDDDDDD DDDDDDDDDD DDDDDDDDDD DDDDDDDDDD EDDEDEDEDD
EGKKKEDKGG LQRS
