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NFYA_RAT
ID   NFYA_RAT                Reviewed;         341 AA.
AC   P18576;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=Nuclear transcription factor Y subunit alpha;
DE   AltName: Full=CAAT box DNA-binding protein subunit A;
DE   AltName: Full=CCAAT-binding transcription factor subunit A;
DE            Short=CBF-A;
DE   AltName: Full=Nuclear transcription factor Y subunit A;
DE            Short=NF-YA;
GN   Name=Nfya;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=Sprague-Dawley;
RX   PubMed=2196566; DOI=10.1073/pnas.87.14.5378;
RA   Maity S.N., Vuorio T., de Crombrugghe B.;
RT   "The B subunit of a rat heteromeric CCAAT-binding transcription factor
RT   shows a striking sequence identity with the yeast Hap2 transcription
RT   factor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:5378-5382(1990).
RN   [2]
RP   DOMAINS.
RX   PubMed=1569083; DOI=10.1016/s0021-9258(18)42440-4;
RA   Maity S.N., de Crombrugghe B.;
RT   "Biochemical analysis of the B subunit of the heteromeric CCAAT-binding
RT   factor. A DNA-binding domain and a subunit interaction domain are specified
RT   by two separate segments.";
RL   J. Biol. Chem. 267:8286-8292(1992).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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.
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   -!- INTERACTION:
CC       P18576; Q01714: Sp1; NbExp=2; IntAct=EBI-862695, EBI-862787;
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; M34238; AAA40889.1; -; mRNA.
DR   PIR; A35777; A35777.
DR   RefSeq; NP_036997.1; NM_012865.1.
DR   AlphaFoldDB; P18576; -.
DR   SMR; P18576; -.
DR   BioGRID; 248146; 1.
DR   IntAct; P18576; 2.
DR   MINT; P18576; -.
DR   STRING; 10116.ENSRNOP00000017157; -.
DR   iPTMnet; P18576; -.
DR   PhosphoSitePlus; P18576; -.
DR   PaxDb; P18576; -.
DR   PRIDE; P18576; -.
DR   GeneID; 29508; -.
DR   KEGG; rno:29508; -.
DR   UCSC; RGD:70976; rat.
DR   CTD; 4800; -.
DR   RGD; 70976; Nfya.
DR   VEuPathDB; HostDB:ENSRNOG00000012702; -.
DR   eggNOG; KOG1561; Eukaryota.
DR   HOGENOM; CLU_071609_1_0_1; -.
DR   InParanoid; P18576; -.
DR   PhylomeDB; P18576; -.
DR   PRO; PR:P18576; -.
DR   Proteomes; UP000002494; Chromosome 9.
DR   Bgee; ENSRNOG00000012702; Expressed in thymus and 20 other tissues.
DR   ExpressionAtlas; P18576; baseline and differential.
DR   Genevisible; P18576; RN.
DR   GO; GO:0016602; C:CCAAT-binding factor complex; IDA:RGD.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0032993; C:protein-DNA complex; ISO:RGD.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR   GO; GO:0003677; F:DNA binding; ISO:RGD.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
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:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:0001221; F:transcription coregulator binding; IPI:RGD.
DR   GO; GO:0080182; P:histone H3-K4 trimethylation; ISO:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0035065; P:regulation of histone acetylation; ISO:RGD.
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; ISO:RGD.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IC:RGD.
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   1: Evidence at protein level;
KW   Activator; Biological rhythms; Direct protein sequencing; DNA-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..341
FT                   /note="Nuclear transcription factor Y subunit alpha"
FT                   /id="PRO_0000198770"
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:0007744|PubMed:22673903"
SQ   SEQUENCE   341 AA;  36294 MW;  3332DB595D67B3A8 CRC64;
     MEQYTANSNS STEQIVVQAG 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
 
 
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