NFYA1_ARATH
ID NFYA1_ARATH Reviewed; 272 AA.
AC Q9LXV5; O23630;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Nuclear transcription factor Y subunit A-1;
DE Short=AtNF-YA-1;
DE AltName: Full=Protein EMBRYO DEFECTIVE 2220;
DE AltName: Full=Transcriptional activator HAP2A;
GN Name=NFYA1; Synonyms=EMB2220, HAP2A; OrderedLocusNames=At5g12840;
GN ORFNames=T24H18_10;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX PubMed=9662544; DOI=10.1104/pp.117.3.1015;
RA Edwards D., Murray J.A.H., Smith A.G.;
RT "Multiple genes encoding the conserved CCAAT-box transcription factor
RT complex are expressed in Arabidopsis.";
RL Plant Physiol. 117:1015-1022(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=11250072; DOI=10.1016/s0378-1119(01)00323-7;
RA Gusmaroli G., Tonelli C., Mantovani R.;
RT "Regulation of the CCAAT-binding NF-Y subunits in Arabidopsis thaliana.";
RL Gene 264:173-185(2001).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11867211; DOI=10.1016/s0378-1119(01)00833-2;
RA Gusmaroli G., Tonelli C., Mantovani R.;
RT "Regulation of novel members of the Arabidopsis thaliana CCAAT-binding
RT nuclear factor Y subunits.";
RL Gene 283:41-48(2002).
CC -!- FUNCTION: Stimulates the transcription of various genes by recognizing
CC and binding to a CCAAT motif in promoters. {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 {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LXV5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LXV5-2; Sequence=VSP_016046;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11250072,
CC ECO:0000269|PubMed:9662544}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NFYA/HAP2 subunit family.
CC {ECO:0000255|PROSITE-ProRule:PRU00966}.
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DR EMBL; Y13720; CAA74048.1; -; mRNA.
DR EMBL; AL353013; CAB88248.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91817.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91818.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91819.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91820.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM71110.1; -; Genomic_DNA.
DR PIR; T49898; T49898.
DR RefSeq; NP_001318552.1; NM_001343248.1. [Q9LXV5-1]
DR RefSeq; NP_568282.1; NM_121287.4. [Q9LXV5-1]
DR RefSeq; NP_850811.1; NM_180480.3. [Q9LXV5-2]
DR RefSeq; NP_974773.1; NM_203044.4. [Q9LXV5-1]
DR RefSeq; NP_974774.1; NM_203045.2. [Q9LXV5-2]
DR AlphaFoldDB; Q9LXV5; -.
DR SMR; Q9LXV5; -.
DR BioGRID; 16402; 9.
DR STRING; 3702.AT5G12840.3; -.
DR iPTMnet; Q9LXV5; -.
DR PaxDb; Q9LXV5; -.
DR PRIDE; Q9LXV5; -.
DR ProteomicsDB; 250590; -. [Q9LXV5-1]
DR EnsemblPlants; AT5G12840.1; AT5G12840.1; AT5G12840. [Q9LXV5-1]
DR EnsemblPlants; AT5G12840.2; AT5G12840.2; AT5G12840. [Q9LXV5-2]
DR EnsemblPlants; AT5G12840.3; AT5G12840.3; AT5G12840. [Q9LXV5-1]
DR EnsemblPlants; AT5G12840.4; AT5G12840.4; AT5G12840. [Q9LXV5-2]
DR EnsemblPlants; AT5G12840.5; AT5G12840.5; AT5G12840. [Q9LXV5-1]
DR GeneID; 831124; -.
DR Gramene; AT5G12840.1; AT5G12840.1; AT5G12840. [Q9LXV5-1]
DR Gramene; AT5G12840.2; AT5G12840.2; AT5G12840. [Q9LXV5-2]
DR Gramene; AT5G12840.3; AT5G12840.3; AT5G12840. [Q9LXV5-1]
DR Gramene; AT5G12840.4; AT5G12840.4; AT5G12840. [Q9LXV5-2]
DR Gramene; AT5G12840.5; AT5G12840.5; AT5G12840. [Q9LXV5-1]
DR KEGG; ath:AT5G12840; -.
DR Araport; AT5G12840; -.
DR TAIR; locus:2182245; AT5G12840.
DR eggNOG; KOG1561; Eukaryota.
DR InParanoid; Q9LXV5; -.
DR OMA; SSMECPN; -.
DR PhylomeDB; Q9LXV5; -.
DR PRO; PR:Q9LXV5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LXV5; baseline and differential.
DR Genevisible; Q9LXV5; AT.
DR GO; GO:0016602; C:CCAAT-binding factor complex; ISS:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
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; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0055046; P:microgametogenesis; IMP:TAIR.
DR GO; GO:0048510; P:regulation of timing of transition from vegetative to reproductive phase; IMP:TAIR.
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:TAIR.
DR GO; GO:0048316; P:seed development; IMP:TAIR.
DR GO; GO:0010262; P:somatic embryogenesis; IMP:TAIR.
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; Alternative splicing; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..272
FT /note="Nuclear transcription factor Y subunit A-1"
FT /id="PRO_0000198771"
FT DNA_BIND 205..230
FT /note="NFYA/HAP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00966"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 34..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 175..198
FT /note="Subunit association domain (SAD)"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..224
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 93
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9662544"
FT /id="VSP_016046"
SQ SEQUENCE 272 AA; 30038 MW; E62BB1D022E7E5F2 CRC64;
MQSKPGRENE EEVNNHHAVQ QPMMYAEPWW KNNSFGVVPQ ARPSGIPSNS SSLDCPNGSE
SNDVHSASED GALNGENDGT WKDSQAATSS RSVDNHGMEG NDPALSIRNM HDQPLVQPPE
LVGHYIACVP NPYQDPYYGG LMGAYGHQQL GFRPYLGMPR ERTALPLDMA QEPVYVNAKQ
YEGILRRRKA RAKAELERKV IRDRKPYLHE SRHKHAMRRA RASGGRFAKK SEVEAGEDAG
GRDRERGSAT NSSGSEQVET DSNETLNSSG AP
