HAP2_SCHPO
ID HAP2_SCHPO Reviewed; 334 AA.
AC P24488;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=Transcriptional activator hap2;
GN Name=hap2; Synonyms=php2; ORFNames=SPBC725.11c;
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 [GENOMIC DNA].
RC STRAIN=401;
RX PubMed=1899284; DOI=10.1128/mcb.11.2.611-619.1991;
RA Olesen J.T., Fikes J.D., Guarente L.;
RT "The Schizosaccharomyces pombe homolog of Saccharomyces cerevisiae HAP2
RT reveals selective and stringent conservation of the small essential core
RT protein domain.";
RL Mol. Cell. Biol. 11:611-619(1991).
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: Global regulator of respiratory functions in yeast cells. It
CC belongs to a complex that binds to the sequence CCAAT located upstream
CC of genes involved in mitochondrial electron transport.
CC -!- SUBUNIT: Belongs to a heterotrimeric CCAAT-binding complex.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the NFYA/HAP2 subunit family.
CC {ECO:0000255|PROSITE-ProRule:PRU00966}.
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DR EMBL; M63639; AAA35322.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA22183.1; -; Genomic_DNA.
DR PIR; A39605; A39605.
DR RefSeq; NP_595491.1; NM_001021402.2.
DR AlphaFoldDB; P24488; -.
DR SMR; P24488; -.
DR BioGRID; 277676; 5.
DR STRING; 4896.SPBC725.11c.1; -.
DR MaxQB; P24488; -.
DR PaxDb; P24488; -.
DR EnsemblFungi; SPBC725.11c.1; SPBC725.11c.1:pep; SPBC725.11c.
DR GeneID; 2541161; -.
DR KEGG; spo:SPBC725.11c; -.
DR PomBase; SPBC725.11c; -.
DR VEuPathDB; FungiDB:SPBC725.11c; -.
DR eggNOG; KOG1561; Eukaryota.
DR HOGENOM; CLU_831980_0_0_1; -.
DR InParanoid; P24488; -.
DR PRO; PR:P24488; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0016602; C:CCAAT-binding factor complex; IMP:PomBase.
DR GO; GO:0000792; C:heterochromatin; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:PomBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0140585; F:promoter-enhancer loop anchoring activity; EXP:PomBase.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:PomBase.
DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:PomBase.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:PomBase.
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:0006109; P:regulation of carbohydrate metabolic process; ISO:PomBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0033217; P:regulation of transcription from RNA polymerase II promoter in response to iron ion starvation; IMP:PomBase.
DR InterPro; IPR018362; CCAAT-binding_factor_CS.
DR InterPro; IPR001289; NFYA.
DR PANTHER; PTHR12632; PTHR12632; 1.
DR Pfam; PF02045; CBFB_NFYA; 1.
DR PRINTS; PR00616; CCAATSUBUNTB.
DR SMART; SM00521; CBF; 1.
DR PROSITE; PS00686; NFYA_HAP2_1; 1.
DR PROSITE; PS51152; NFYA_HAP2_2; 1.
PE 3: Inferred from homology;
KW Activator; DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..334
FT /note="Transcriptional activator hap2"
FT /id="PRO_0000198783"
FT DNA_BIND 42..67
FT /note="NFYA/HAP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00966"
FT REGION 46..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 11..35
FT /note="Subunit association domain (SAD)"
FT COMPBIAS 88..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 334 AA; 34893 MW; 7B582C9BC2CA27B6 CRC64;
MNPYEPVEGL YVNAKQYHRI LKRREARAKL EERLRGVQTT KKPYLHESRH KHAMRRPRGP
GGRFLTADKV SKLRAQEAAE AAANGGSTGD DVNATNANDA TVPATVSSEV THTSEGYADS
NDSRPSSISN SSESPAPINS ATASMSPANN TSGNNITSPN VRGELDMSGN IAMSGGPTNT
ASTSGPVPHD MTVLPQTDSN TSNLMSSGSQ LGSFATASTN GNNSTTTTTS SAAHPGSFHK
GTNDYSSTLA GNEHSAFPGL DVYHDDSVSA GAAFIPHNPM DSIDHLDVND PTATGLPVLP
ASDIDPLNLT GNTQDSMIIG QQTYPSHGSS GTMK
