HAP5_SCHPO
ID HAP5_SCHPO Reviewed; 415 AA.
AC P79007;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 161.
DE RecName: Full=Transcriptional activator hap5;
GN Name=hap5; Synonyms=php5; ORFNames=SPBC3B8.02;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Component of the CCAAT-bound heteromer, php5 is essential for
CC DNA-binding activity. It is essential for transcription activation of
CC cyc1. It is the linchpin that binds to the subunit association domains
CC (SAD) of php2 and php3 to bring these proteins together.
CC {ECO:0000269|PubMed:9372932}.
CC -!- SUBUNIT: Two complexes bind CCAAT; complex I, that consists of php2/3/5
CC and complex II, that consists of php2/3/5/4. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the NFYC/HAP5 subunit family. {ECO:0000305}.
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DR EMBL; U88525; AAB88012.1; -; mRNA.
DR EMBL; CU329671; CAA18291.1; -; Genomic_DNA.
DR PIR; T40338; T40338.
DR RefSeq; NP_596412.1; NM_001022331.2.
DR AlphaFoldDB; P79007; -.
DR SMR; P79007; -.
DR BioGRID; 276670; 259.
DR STRING; 4896.SPBC3B8.02.1; -.
DR iPTMnet; P79007; -.
DR MaxQB; P79007; -.
DR PaxDb; P79007; -.
DR EnsemblFungi; SPBC3B8.02.1; SPBC3B8.02.1:pep; SPBC3B8.02.
DR GeneID; 2540133; -.
DR KEGG; spo:SPBC3B8.02; -.
DR PomBase; SPBC3B8.02; -.
DR VEuPathDB; FungiDB:SPBC3B8.02; -.
DR eggNOG; KOG1657; Eukaryota.
DR HOGENOM; CLU_662506_0_0_1; -.
DR InParanoid; P79007; -.
DR OMA; YMAEHLY; -.
DR PRO; PR:P79007; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0016602; C:CCAAT-binding factor complex; IMP:PomBase.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0010723; P:positive regulation of transcription from RNA polymerase II promoter in response to iron; IMP:PomBase.
DR GO; GO:1903715; P:regulation of aerobic respiration; IMP:PomBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR003958; CBFA_NFYB_domain.
DR InterPro; IPR027170; HAP5_su.
DR InterPro; IPR009072; Histone-fold.
DR PANTHER; PTHR10252:SF8; PTHR10252:SF8; 1.
DR Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 2: Evidence at transcript level;
KW Activator; DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..415
FT /note="Transcriptional activator hap5"
FT /id="PRO_0000218261"
FT REGION 354..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 415 AA; 46674 MW; D98E8CBE384D8C67 CRC64;
MNSIPDSYSL KQGFPEGLGE YVDPSGNPNS QVRIGYGQDS VSRFQQPVPD VDPTAVNHYN
ASAPIEVASP FDNVTQGLVG SDAQALAEYW QKTIDTLEHD DQAVKTLHLP LARIKKVMKT
DDDVKNKMIS AEAPFLFAKG SEIFIAELTM RAWLHAKKNQ RRTLQRSDIA NAVSKSEMYD
FLIDIISKDN NNSRASSSQA HMSATQVAAM GGMNGLQPFP TQAGLPNQGF PMPTGSQLPF
SNQQSSQPSM QYSSHPSRMQ QMQDIDQSMY KQQRLGSEYP QLQMSDNSGN VNQMNMQRPV
MVAPYMAEHL YRYPPTHLES GSSAFRLQSS PMGYQMPQFQ GNMRPNMQQS QMFDPSAYGM
SRRPGSPRQF DQQQRLYSQP NAMMYQTQQG RQGNPMHQQF SQQQNPLSRY SQQPQ
