HAP4_YEAST
ID HAP4_YEAST Reviewed; 554 AA.
AC P14064; D6VXH8;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Transcriptional activator HAP4;
GN Name=HAP4; OrderedLocusNames=YKL109W; ORFNames=YKL465;
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], AND FUNCTION.
RC STRAIN=ATCC MYA-3516 / BWG1-7A;
RX PubMed=2676721; DOI=10.1101/gad.3.8.1166;
RA Forsburg S.L., Guarente L.;
RT "Identification and characterization of HAP4: a third component of the
RT CCAAT-bound HAP2/HAP3 heteromer.";
RL Genes Dev. 3:1166-1178(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8109175; DOI=10.1002/yea.320091113;
RA Cheret G., Pallier C., Valens M., Daignan-Fornier B., Fukuhara H.,
RA Bolotin-Fukuhara M., Sor F.;
RT "The DNA sequence analysis of the HAP4-LAP4 region on chromosome XI of
RT Saccharomyces cerevisiae suggests the presence of a second aspartate
RT aminotransferase gene in yeast.";
RL Yeast 9:1259-1265(1993).
RN [3]
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 [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 IDENTIFICATION IN THE CCAT-BINDING FACTOR.
RX PubMed=9372932; DOI=10.1128/mcb.17.12.7008;
RA McNabb D.S., Tseng K.A.-S., Guarente L.;
RT "The Saccharomyces cerevisiae Hap5p homolog from fission yeast reveals two
RT conserved domains that are essential for assembly of heterotetrameric
RT CCAAT-binding factor.";
RL Mol. Cell. Biol. 17:7008-7018(1997).
RN [6]
RP FUNCTION, DOMAIN, AND MUTAGENESIS OF 148-PHE--PHE-151; 390-ILE--LEU-394;
RP 427-TYR--LEU-430; 456-PHE--LEU-459; LEU-466 AND MET-467.
RX PubMed=15075264; DOI=10.1128/ec.3.2.339-347.2004;
RA Stebbins J.L., Triezenberg S.J.;
RT "Identification, mutational analysis, and coactivator requirements of two
RT distinct transcriptional activation domains of the Saccharomyces cerevisiae
RT Hap4 protein.";
RL Eukaryot. Cell 3:339-347(2004).
RN [7]
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).
RN [8]
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: 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'. HAP4 encodes a regulatory subunit of the DNA-
CC bound complex and seems to provide the principal transcriptional
CC activation domains. Does not bind DNA directly, but augments the
CC binding of HAP2 and HAP3. {ECO:0000269|PubMed:15075264,
CC ECO:0000269|PubMed:2676721}.
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:9372932}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- INDUCTION: Its expression is glucose-repressible.
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DR EMBL; X16727; CAA34707.1; -; Genomic_DNA.
DR EMBL; X71133; CAA50448.1; -; Genomic_DNA.
DR EMBL; Z28109; CAA81949.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09048.1; -; Genomic_DNA.
DR PIR; S37936; S37936.
DR RefSeq; NP_012813.1; NM_001179675.1.
DR AlphaFoldDB; P14064; -.
DR BioGRID; 34024; 290.
DR ComplexPortal; CPX-1830; CCAAT-binding factor complex.
DR DIP; DIP-2360N; -.
DR IntAct; P14064; 3.
DR MINT; P14064; -.
DR STRING; 4932.YKL109W; -.
DR iPTMnet; P14064; -.
DR PaxDb; P14064; -.
DR PRIDE; P14064; -.
DR EnsemblFungi; YKL109W_mRNA; YKL109W; YKL109W.
DR GeneID; 853751; -.
DR KEGG; sce:YKL109W; -.
DR SGD; S000001592; HAP4.
DR VEuPathDB; FungiDB:YKL109W; -.
DR eggNOG; ENOG502SGDX; Eukaryota.
DR HOGENOM; CLU_036426_0_0_1; -.
DR InParanoid; P14064; -.
DR OMA; HIQTIDE; -.
DR BioCyc; YEAST:G3O-31895-MON; -.
DR PRO; PR:P14064; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P14064; protein.
DR GO; GO:0016602; C:CCAAT-binding factor complex; IDA:SGD.
DR GO; GO:0005746; C:mitochondrial respirasome; IMP:CACAO.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:SGD.
DR GO; GO:0003713; F:transcription coactivator activity; IMP:SGD.
DR GO; GO:0000436; P:carbon catabolite activation of transcription from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:0006109; P:regulation of carbohydrate metabolic process; IC:ComplexPortal.
DR GO; GO:0043457; P:regulation of cellular respiration; IMP:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR InterPro; IPR018287; Hap4_TF_heteromerisation.
DR Pfam; PF10297; Hap4_Hap_bind; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..554
FT /note="Transcriptional activator HAP4"
FT /id="PRO_0000083900"
FT REGION 1..327
FT /note="Probably encodes all the information necessary to
FT anchor HAP4 to HAP2/3"
FT REGION 1..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..300
FT /note="Activation domain 1"
FT REGION 359..476
FT /note="Activation domain 2"
FT REGION 393..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 148..151
FT /note="FLKF->SSKS: Greatly diminishes transcriptional
FT activation."
FT /evidence="ECO:0000269|PubMed:15075264"
FT MUTAGEN 390..394
FT /note="IWNYL->SSNSS: Greatly diminishes transcriptional
FT activation."
FT /evidence="ECO:0000269|PubMed:15075264"
FT MUTAGEN 427..430
FT /note="YLFL->SSSS: Greatly diminishes transcriptional
FT activation."
FT /evidence="ECO:0000269|PubMed:15075264"
FT MUTAGEN 456..459
FT /note="FSYL->SSSS: Greatly diminishes transcriptional
FT activation."
FT /evidence="ECO:0000269|PubMed:15075264"
FT MUTAGEN 466..467
FT /note="LM->SS: Abolishes transcriptional activation."
FT MUTAGEN 466
FT /note="L->A: Greatly diminishes transcriptional
FT activation."
FT /evidence="ECO:0000269|PubMed:15075264"
FT MUTAGEN 467
FT /note="M->A: Abolishes transcriptional activation."
FT /evidence="ECO:0000269|PubMed:15075264"
FT CONFLICT 160
FT /note="H -> R (in Ref. 1; CAA34707)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 554 AA; 62412 MW; CF8A46219F8CA431 CRC64;
MTAKTFLLQA SASRPRSNHF KNEHNNIPLA PVPIAPNTNH HNNSSLEFEN DGSKKKKKSS
LVVRTSKHWV LPPRPRPGRR SSSHNTLPAN NTNNILNVGP NSRNSSNNNN NNNIISNRKQ
ASKEKRKIPR HIQTIDEKLI NDSNYLAFLK FDDLENEKFH SSASSISSPS YSSPSFSSYR
NRKKSEFMDD ESCTDVETIA AHNSLLTKNH HIDSSSNVHA PPTKKSKLND FDLLSLSSTS
SSATPVPQLT KDLNMNLNFH KIPHKASFPD SPADFSPADS VSLIRNHSLP TNLQVKDKIE
DLNEIKFFND FEKLEFFNKY AKVNTNNDVN ENNDLWNSYL QSMDDTTGKN SGNYQQVDND
DNMSLLNLPI LEETVSSGQD DKVEPDEEDI WNYLPSSSSQ QEDSSRALKK NTNSEKANIQ
AKNDETYLFL QDQDESADSH HHDELGSEIT LADNKFSYLP PTLEELMEEQ DCNNGRSFKN
FMFSNDTGID GSAGTDDDYT KVLKSKKIST SKSNANLYDL NDNNNDATAT NELDQSSFID
DLDEDVDFLK VQVF
