ID   HAP3_YEAST              Reviewed;         144 AA.
AC   P13434; D6VPX9;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   24-JAN-2024, entry version 197.
DE   RecName: Full=Transcriptional activator HAP3;
DE   AltName: Full=UAS2 regulatory protein A;
GN   Name=HAP3; OrderedLocusNames=YBL021C; ORFNames=YBL0441;
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].
RC   STRAIN=ATCC MYA-3516 / BWG1-7A;
RX   PubMed=2832732; DOI=10.1128/mcb.8.2.655-663.1988;
RA   Hahn S., Pinkham J., Wei R., Miller R., Guarente L.;
RT   "The HAP3 regulatory locus of Saccharomyces cerevisiae encodes divergent
RT   overlapping transcripts.";
RL   Mol. Cell. Biol. 8:655-663(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8276800; DOI=10.1016/s0021-9258(17)42340-4;
RA   van Dyck L., Pearce D.A., Sherman F.;
RT   "PIM1 encodes a mitochondrial ATP-dependent protease that is required for
RT   mitochondrial function in the yeast Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 269:238-242(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [6]
RP   MUTAGENESIS.
RX   PubMed=8223474; DOI=10.1002/j.1460-2075.1993.tb06153.x;
RA   Xing Y., Fikes J.D., Guarente L.;
RT   "Mutations in yeast HAP2/HAP3 define a hybrid CCAAT box binding domain.";
RL   EMBO J. 12:4647-4655(1993).
RN   [7]
RP   IDENTIFICATION IN THE CCAT-BINDING FACTOR.
RX   PubMed=11390369; DOI=10.1074/jbc.c100274200;
RA   Li Y., Takagi Y., Jiang Y., Tokunaga M., Erdjument-Bromage H., Tempst P.,
RA   Kornberg R.D.;
RT   "A multiprotein complex that interacts with RNA polymerase II elongator.";
RL   J. Biol. Chem. 276:29628-29631(2001).
RN   [8]
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   [9]
RP   ASSEMBLY OF THE CCAT-BINDING FACTOR.
RX   PubMed=16278450; DOI=10.1128/ec.4.11.1829-1839.2005;
RA   McNabb D.S., Pinto I.;
RT   "Assembly of the Hap2p/Hap3p/Hap4p/Hap5p-DNA complex in Saccharomyces
RT   cerevisiae.";
RL   Eukaryot. Cell 4:1829-1839(2005).
CC   -!- FUNCTION: Acts a component of the CCAT-binding factor, which is a
CC       transcriptional activator and binds to the upstream activation site
CC       (UAS2) of the CYC1 gene and other genes involved in mitochondrial
CC       electron transport and activates their expression. Recognizes the
CC       sequence 5'-CCAAT-3'.
CC   -!- SUBUNIT: Component of the CCAT-binding factor (CBF or HAP complex II),
CC       which consists of one copy each of HAP2, HAP3, HAP4 and HAP5. The
CC       assembly of the HAP2-HAP3-HAP5 heteromer (HAP complex I) occurs in a
CC       one-step pathway and its binding to DNA is a prerequisite for the
CC       association of HAP4. {ECO:0000269|PubMed:11390369}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- MISCELLANEOUS: Present with 2510 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the NFYB/HAP3 subunit family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M20318; AAA53538.1; -; Genomic_DNA.
DR   EMBL; X74544; CAA52633.1; -; Genomic_DNA.
DR   EMBL; Z35782; CAA84840.1; -; Genomic_DNA.
DR   EMBL; AY558459; AAS56785.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07099.1; -; Genomic_DNA.
DR   PIR; A28123; A28123.
DR   RefSeq; NP_009532.1; NM_001178261.1.
DR   AlphaFoldDB; P13434; -.
DR   SMR; P13434; -.
DR   BioGRID; 32677; 385.
DR   ComplexPortal; CPX-1830; CCAAT-binding factor complex.
DR   DIP; DIP-1362N; -.
DR   IntAct; P13434; 11.
DR   MINT; P13434; -.
DR   STRING; 4932.YBL021C; -.
DR   MaxQB; P13434; -.
DR   PaxDb; 4932-YBL021C; -.
DR   PeptideAtlas; P13434; -.
DR   EnsemblFungi; YBL021C_mRNA; YBL021C; YBL021C.
DR   GeneID; 852260; -.
DR   KEGG; sce:YBL021C; -.
DR   AGR; SGD:S000000117; -.
DR   SGD; S000000117; HAP3.
DR   VEuPathDB; FungiDB:YBL021C; -.
DR   eggNOG; KOG0869; Eukaryota.
DR   GeneTree; ENSGT00940000174727; -.
DR   HOGENOM; CLU_066247_12_1_1; -.
DR   InParanoid; P13434; -.
DR   OMA; KQNHRTI; -.
DR   OrthoDB; 24067at2759; -.
DR   BioCyc; YEAST:G3O-28924-MONOMER; -.
DR   BioGRID-ORCS; 852260; 10 hits in 10 CRISPR screens.
DR   PRO; PR:P13434; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P13434; Protein.
DR   GO; GO:0016602; C:CCAAT-binding factor complex; IDA:SGD.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0000436; P:carbon catabolite activation of transcription from RNA polymerase II promoter; IDA:SGD.
DR   GO; GO:0006109; P:regulation of carbohydrate metabolic process; NAS:ComplexPortal.
DR   GO; GO:0043457; P:regulation of cellular respiration; IMP:SGD.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; NAS:ComplexPortal.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR   InterPro; IPR003958; CBFA_NFYB_domain.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR027113; Transc_fact_NFYB/HAP3.
DR   InterPro; IPR003956; Transcrpt_fac_NFYB/HAP3_CS.
DR   PANTHER; PTHR11064; CCAAT-BINDING TRANSCRIPTION FACTOR-RELATED; 1.
DR   PANTHER; PTHR11064:SF9; NUCLEAR TRANSCRIPTION FACTOR Y SUBUNIT BETA; 1.
DR   Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR   PRINTS; PR00615; CCAATSUBUNTA.
DR   SUPFAM; SSF47113; Histone-fold; 1.
DR   PROSITE; PS00685; NFYB_HAP3; 1.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..144
FT                   /note="Transcriptional activator HAP3"
FT                   /id="PRO_0000204630"
FT   DNA_BIND        42..48
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          69..80
FT                   /note="Subunit association domain (SAD)"
SQ   SEQUENCE   144 AA;  16154 MW;  7AB5027BAE420337 CRC64;
     MNTNESEHVS TSPEDTQENG GNASSSGSLQ QISTLREQDR WLPINNVARL MKNTLPPSAK
     VSKDAKECMQ ECVSELISFV TSEASDRCAA DKRKTINGED ILISLHALGF ENYAEVLKIY
     LAKYRQQQAL KNQLMYEQDD EEVP
//