ID   NFYA_BOVIN              Reviewed;         341 AA.
AC   Q5E9S2;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Nuclear transcription factor Y subunit alpha;
DE   AltName: Full=CAAT box DNA-binding protein subunit A;
DE   AltName: Full=Nuclear transcription factor Y subunit A;
DE            Short=NF-YA;
GN   Name=NFYA;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
CC   -!- FUNCTION: Component of the sequence-specific heterotrimeric
CC       transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3'
CC       box motif found in the promoters of its target genes. NF-Y can function
CC       as both an activator and a repressor, depending on its interacting
CC       cofactors. NF-YA positively regulates the transcription of the core
CC       clock component ARNTL/BMAL1 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterotrimeric transcription factor composed of three
CC       components, NF-YA, NF-YB and NF-YC. NF-YB and NF-YC must interact and
CC       dimerize for NF-YA association and DNA binding (By similarity).
CC       Interacts with SP1; the interaction is inhibited by glycosylation of
CC       SP1. Interacts (via N-terminus) with ZHX2 (via homeobox domain).
CC       Interacts with ZFX3. Interacts with ZHX1 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00966}.
CC   -!- SIMILARITY: Belongs to the NFYA/HAP2 subunit family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00966}.
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DR   EMBL; BT020848; AAX08865.1; -; mRNA.
DR   RefSeq; NP_001014956.1; NM_001014956.1.
DR   AlphaFoldDB; Q5E9S2; -.
DR   SMR; Q5E9S2; -.
DR   STRING; 9913.ENSBTAP00000013080; -.
DR   PaxDb; Q5E9S2; -.
DR   PRIDE; Q5E9S2; -.
DR   Ensembl; ENSBTAT00000013080; ENSBTAP00000013080; ENSBTAG00000009905.
DR   GeneID; 539584; -.
DR   KEGG; bta:539584; -.
DR   CTD; 4800; -.
DR   VEuPathDB; HostDB:ENSBTAG00000009905; -.
DR   VGNC; VGNC:32055; NFYA.
DR   eggNOG; KOG1561; Eukaryota.
DR   GeneTree; ENSGT00390000015714; -.
DR   HOGENOM; CLU_071609_1_0_1; -.
DR   InParanoid; Q5E9S2; -.
DR   OMA; GNMMNSG; -.
DR   OrthoDB; 1269806at2759; -.
DR   TreeFam; TF323257; -.
DR   Proteomes; UP000009136; Chromosome 23.
DR   Bgee; ENSBTAG00000009905; Expressed in thymus and 111 other tissues.
DR   ExpressionAtlas; Q5E9S2; baseline.
DR   GO; GO:0016602; C:CCAAT-binding factor complex; ISS:AgBase.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISS:AgBase.
DR   GO; GO:0032993; C:protein-DNA complex; IEA:Ensembl.
DR   GO; GO:0003677; F:DNA binding; ISS:AgBase.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0080182; P:histone H3-K4 trimethylation; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0035065; P:regulation of histone acetylation; IEA:Ensembl.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:AgBase.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Activator; Biological rhythms; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..341
FT                   /note="Nuclear transcription factor Y subunit alpha"
FT                   /id="PRO_0000198767"
FT   DNA_BIND        290..315
FT                   /note="NFYA/HAP2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00966"
FT   REGION          294..341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           260..283
FT                   /note="Subunit association domain (SAD)"
FT   COMPBIAS        306..326
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         320
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P23511"
SQ   SEQUENCE   341 AA;  36234 MW;  B1A118D4D2BB13D7 CRC64;
     MEQYAANSNS SAEQIVVQAG QIQQQQQGGV TAVQLQTEAQ VASASGQQVQ TLQVVQGQPL
     MVQVSGGQLI TSTGQPIMVQ AVPGGQGQTI MQVPVSGTQG LQQIQLVPPG QIQIQGGQAV
     QVQGQQGQTQ QIIIQQPQTA VTAGQTQTQQ QIAVQGQQVA QTAEGQTIVY QPVNADGTIL
     QQGMITIPAA SLAGAQIVQT GANTNTTSSG QGTVTVTLPV AGNVVNSGGM VMMVPGAGSV
     PAIQRIPLPG AEMLEEEPLY VNAKQYHRIL KRRQARAKLE AEGKIPKERR KYLHESRHRH
     AMARKRGEGG RFFSPKEKDS PHMQDPNQAD EEAMTQIIRV S