ID   CAB3_YEAST              Reviewed;         571 AA.
AC   P36076; D6VXK0;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   10-JUN-2026, entry version 177.
DE   RecName: Full=Coenzyme A biosynthesis protein 3;
GN   Name=CAB3; OrderedLocusNames=YKL088W;
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 [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   [2]
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   [3]
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   [4]
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   [5]
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-116; SER-121 AND
RP   SER-124, AND 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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND IDENTIFICATION BY
RP   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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND SER-264, 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   [9]
RP   FUNCTION.
RX   PubMed=19266201; DOI=10.1007/s00294-009-0234-1;
RA   Olzhausen J., Schuebbe S., Schueller H.-J.;
RT   "Genetic analysis of coenzyme A biosynthesis in the yeast Saccharomyces
RT   cerevisiae: identification of a conditional mutation in the pantothenate
RT   kinase gene CAB1.";
RL   Curr. Genet. 55:163-173(2009).
RN   [10]
RP   FUNCTION, MUTAGENESIS OF CYS-478, AND INTERACTION WITH HAL3 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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116 AND SER-121, AND
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).
CC   -!- FUNCTION: Component of the phosphopantothenoylcysteine decarboxylase
CC       (PPCDC) involved in the coenzyme A synthesis.
CC       {ECO:0000269|PubMed:19266201, ECO:0000269|PubMed:19915539}.
CC   -!- SUBUNIT: Component of the phosphopantothenoylcysteine decarboxylase
CC       (PPCDC) complex, a heterotrimer composed of CAB3, HAL3 and VHS3.
CC   -!- INTERACTION:
CC       P36076; P40506: CAB2; NbExp=6; IntAct=EBI-26778, EBI-25089;
CC       P36076; P36076: CAB3; NbExp=3; IntAct=EBI-26778, EBI-26778;
CC       P36076; P53332: CAB4; NbExp=5; IntAct=EBI-26778, EBI-23648;
CC       P36076; Q03941: CAB5; NbExp=7; IntAct=EBI-26778, EBI-22174;
CC       P36076; P19454: CKA2; NbExp=3; IntAct=EBI-26778, EBI-9548;
CC       P36076; P26570: PPZ1; NbExp=7; IntAct=EBI-26778, EBI-13807;
CC       P36076; P33329: PPZ2; NbExp=5; IntAct=EBI-26778, EBI-13815;
CC       P36076; P36024: SIS2; NbExp=10; IntAct=EBI-26778, EBI-17250;
CC       P36076; Q08438: VHS3; NbExp=9; IntAct=EBI-26778, EBI-30482;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 2940 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; Z28088; CAA81926.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA09070.1; -; Genomic_DNA.
DR   PIR; S37913; S37913.
DR   RefSeq; NP_012835.1; NM_001179654.1.
DR   AlphaFoldDB; P36076; -.
DR   SMR; P36076; -.
DR   BioGRID; 34045; 48.
DR   ComplexPortal; CPX-393; Phosphopantothenoylcysteine decarboxylase complex.
DR   ComplexPortal; CPX-396; Coenzyme A-synthesizing protein complex.
DR   DIP; DIP-4475N; -.
DR   FunCoup; P36076; 245.
DR   IntAct; P36076; 76.
DR   MINT; P36076; -.
DR   STRING; 4932.YKL088W; -.
DR   iPTMnet; P36076; -.
DR   PaxDb; 4932-YKL088W; -.
DR   PeptideAtlas; P36076; -.
DR   EnsemblFungi; YKL088W_mRNA; YKL088W; YKL088W.
DR   GeneID; 853774; -.
DR   KEGG; sce:YKL088W; -.
DR   AGR; SGD:S000001571; -.
DR   SGD; S000001571; CAB3.
DR   VEuPathDB; FungiDB:YKL088W; -.
DR   eggNOG; KOG0672; Eukaryota.
DR   HOGENOM; CLU_014402_2_1_1; -.
DR   InParanoid; P36076; -.
DR   OMA; HEIQINT; -.
DR   OrthoDB; 1532798at2759; -.
DR   BioCyc; MetaCyc:MONOMER3O-299; -.
DR   BioCyc; YEAST:MONOMER3O-299; -.
DR   Reactome; R-SCE-196783; Coenzyme A biosynthesis.
DR   BioGRID-ORCS; 853774; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P36076; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P36076; protein.
DR   GO; GO:1990143; C:CoA-synthesizing protein complex; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; HDA: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:0015937; P:coenzyme A biosynthetic process; IGI:SGD.
DR   FunFam; 3.40.50.1950:FF:000010; Coenzyme A biosynthesis protein 3; 1.
DR   Gene3D; 3.40.50.1950; Flavin prenyltransferase-like; 1.
DR   InterPro; IPR036551; Flavin_trans-like.
DR   InterPro; IPR003382; Flavoprotein.
DR   PANTHER; PTHR14359; HOMO-OLIGOMERIC FLAVIN CONTAINING CYS DECARBOXYLASE FAMILY; 1.
DR   PANTHER; PTHR14359:SF6; PHOSPHOPANTOTHENOYLCYSTEINE DECARBOXYLASE; 1.
DR   Pfam; PF02441; Flavoprotein; 1.
DR   SUPFAM; SSF52507; Homo-oligomeric flavin-containing Cys decarboxylases, HFCD; 1.
PE   1: Evidence at protein level;
KW   Coenzyme A biosynthesis; Cytoplasm; Phosphoprotein; Reference proteome.
FT   CHAIN           1..571
FT                   /note="Coenzyme A biosynthesis protein 3"
FT                   /id="PRO_0000182039"
FT   REGION          1..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          100..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          140..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          209..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          507..571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..72
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..171
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        516..571
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         42
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358,
FT                   ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956"
FT   MOD_RES         116
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         121
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         124
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         264
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MUTAGEN         478
FT                   /note="C->S: Abolishes PPCDC activity."
FT                   /evidence="ECO:0000269|PubMed:19915539"
SQ   SEQUENCE   571 AA;  65238 MW;  9C674C2394EFCEAB CRC64;
     MTDEKVNSDQ NMNGKQGVNL ISSLPTTQVP VSILTNKERR KSIHDESNFE RSDSHEDQSK
     SNSNRRNIYK NDYSTNLRDF SFANLKQNSE RNKDGHEIQI NTSMPANTNG QQKRFSPSLP
     SAVSFTVPEV ERLPYHRYSI SNKPGKQQQQ QEQLQQNQQQ EEQQKAQLQE QNQRAKQQEE
     VKQIQEQVQK KQTERQQLID EKERIANAIF KENTTNDGTD IRKHSVSSGT SNSEDEVDSP
     SMEKNSIVHM PGDFIYFNPK SNASKPITAK AAPLSANNST HKNKEVITAP TGPRVPFTEF
     FQKEDDKKFH ILIGATGSVA TIKVPLIIDK LFKIYGPEKI SIQLIVTKPA EHFLKGLKMS
     THVKIWREED AWVFDAVNKN DTSLSLNLIL HHELRKWADI FLIAPLSANT LAKLANGICN
     NLLTSVMRDW SPLTPVLIAP AMNTFMYINP MTKKHLTSLV QDYPFIQVLK PVEKVLICGD
     IGMGGMREWT DIVEIVRRRI NEIRKARDEE TGDKEQEQEE QEGADNEDDD DEDDEEDEED
     EEEEEALNET ASDESNDEED EEDEEDVKTE V
//