CAB3_YEAST
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 03-AUG-2022, entry version 162.
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; P26570: PPZ1; NbExp=6; IntAct=EBI-26778, EBI-13807;
CC P36076; P33329: PPZ2; NbExp=4; IntAct=EBI-26778, EBI-13815;
CC P36076; P36024: SIS2; NbExp=8; 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; 42.
DR ComplexPortal; CPX-393; Phosphopantothenoylcysteine decarboxylase complex.
DR ComplexPortal; CPX-396; Coenzyme A-synthesizing protein complex.
DR DIP; DIP-4475N; -.
DR IntAct; P36076; 74.
DR MINT; P36076; -.
DR STRING; 4932.YKL088W; -.
DR iPTMnet; P36076; -.
DR MaxQB; P36076; -.
DR PaxDb; P36076; -.
DR PRIDE; P36076; -.
DR EnsemblFungi; YKL088W_mRNA; YKL088W; YKL088W.
DR GeneID; 853774; -.
DR KEGG; sce:YKL088W; -.
DR SGD; S000001571; CAB3.
DR VEuPathDB; FungiDB:YKL088W; -.
DR eggNOG; KOG0672; Eukaryota.
DR GeneTree; ENSGT00440000038107; -.
DR HOGENOM; CLU_014402_2_1_1; -.
DR InParanoid; P36076; -.
DR OMA; NMNGKQG; -.
DR BioCyc; MetaCyc:MON3O-299; -.
DR BioCyc; YEAST:MON3O-299; -.
DR Reactome; R-SCE-196783; Coenzyme A biosynthesis.
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 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; 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 1..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..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
