NFYC4_ARATH
ID NFYC4_ARATH Reviewed; 250 AA.
AC Q9FMV5;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Nuclear transcription factor Y subunit C-4;
DE Short=AtNF-YC-4;
GN Name=NFYC4; OrderedLocusNames=At5g63470; ORFNames=MLE2.10;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=17322342; DOI=10.1104/pp.106.089904;
RA Warpeha K.M., Upadhyay S., Yeh J., Adamiak J., Hawkins S.I., Lapik Y.R.,
RA Anderson M.B., Kaufman L.S.;
RT "The GCR1, GPA1, PRN1, NF-Y signal chain mediates both blue light and
RT abscisic acid responses in Arabidopsis.";
RL Plant Physiol. 143:1590-1600(2007).
CC -!- FUNCTION: Stimulates the transcription of various genes by recognizing
CC and binding to a CCAAT motif in promoters (By similarity). Involved in
CC the abscisic acid (ABA) signaling pathway. {ECO:0000250,
CC ECO:0000269|PubMed:17322342}.
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 -!- INTERACTION:
CC Q9FMV5; Q8L500: APRR9; NbExp=3; IntAct=EBI-2466018, EBI-7920168;
CC Q9FMV5; Q9LRH6: GATA25; NbExp=3; IntAct=EBI-2466018, EBI-2460434;
CC Q9FMV5; Q7XA73: TIFY4A; NbExp=3; IntAct=EBI-2466018, EBI-15199673;
CC Q9FMV5; Q8GY55: TIFY4B; NbExp=3; IntAct=EBI-2466018, EBI-15206004;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Present in etiolated seedlings.
CC {ECO:0000269|PubMed:11250072, ECO:0000269|PubMed:17322342}.
CC -!- DISRUPTION PHENOTYPE: Altered response to abscisic acid (ABA).
CC {ECO:0000269|PubMed:17322342}.
CC -!- SIMILARITY: Belongs to the NFYC/HAP5 subunit family. {ECO:0000305}.
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DR EMBL; AB007649; BAB08812.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97755.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97756.1; -; Genomic_DNA.
DR EMBL; AY072402; AAL62394.1; -; mRNA.
DR EMBL; BT000218; AAN15537.1; -; mRNA.
DR RefSeq; NP_001032130.1; NM_001037053.2.
DR RefSeq; NP_201152.1; NM_125742.6.
DR PDB; 7CVO; X-ray; 2.60 A; A/F=72-156.
DR PDBsum; 7CVO; -.
DR AlphaFoldDB; Q9FMV5; -.
DR SMR; Q9FMV5; -.
DR BioGRID; 21708; 30.
DR IntAct; Q9FMV5; 5.
DR STRING; 3702.AT5G63470.1; -.
DR PaxDb; Q9FMV5; -.
DR PRIDE; Q9FMV5; -.
DR EnsemblPlants; AT5G63470.1; AT5G63470.1; AT5G63470.
DR EnsemblPlants; AT5G63470.2; AT5G63470.2; AT5G63470.
DR GeneID; 836466; -.
DR Gramene; AT5G63470.1; AT5G63470.1; AT5G63470.
DR Gramene; AT5G63470.2; AT5G63470.2; AT5G63470.
DR KEGG; ath:AT5G63470; -.
DR Araport; AT5G63470; -.
DR TAIR; locus:2167306; AT5G63470.
DR eggNOG; KOG1657; Eukaryota.
DR HOGENOM; CLU_045277_0_1_1; -.
DR InParanoid; Q9FMV5; -.
DR OMA; EDNSYAG; -.
DR OrthoDB; 1558176at2759; -.
DR PhylomeDB; Q9FMV5; -.
DR PRO; PR:Q9FMV5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FMV5; baseline and differential.
DR Genevisible; Q9FMV5; AT.
DR GO; GO:0005829; C:cytosol; IPI:TAIR.
DR GO; GO:0005634; C:nucleus; IPI:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0009740; P:gibberellic acid mediated signaling pathway; IGI:TAIR.
DR GO; GO:2000905; P:negative regulation of starch metabolic process; IMP:TAIR.
DR GO; GO:2000306; P:positive regulation of photomorphogenesis; IMP:TAIR.
DR GO; GO:0051247; P:positive regulation of protein metabolic process; IMP:TAIR.
DR GO; GO:0010468; P:regulation of gene expression; IMP:TAIR.
DR GO; GO:0048586; P:regulation of long-day photoperiodism, flowering; IGI:TAIR.
DR GO; GO:0010029; P:regulation of seed germination; IGI:TAIR.
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; IPR009072; Histone-fold.
DR Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Abscisic acid signaling pathway; Activator; DNA-binding;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..250
FT /note="Nuclear transcription factor Y subunit C-4"
FT /id="PRO_0000218253"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..27
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 81..89
FT /evidence="ECO:0007829|PDB:7CVO"
FT HELIX 100..126
FT /evidence="ECO:0007829|PDB:7CVO"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:7CVO"
FT HELIX 134..143
FT /evidence="ECO:0007829|PDB:7CVO"
FT HELIX 145..150
FT /evidence="ECO:0007829|PDB:7CVO"
SQ SEQUENCE 250 AA; 27032 MW; CA8C247594A3509C CRC64;
MDNNNNNNNQ QPPPTSVYPP GSAVTTVIPP PPSGSASIVT GGGATYHHLL QQQQQQLQMF
WTYQRQEIEQ VNDFKNHQLP LARIKKIMKA DEDVRMISAE APILFAKACE LFILELTIRS
WLHAEENKRR TLQKNDIAAA ITRTDIFDFL VDIVPREEIK EEEDAASALG GGGMVAPAAS
GVPYYYPPMG QPAVPGGMMI GRPAMDPSGV YAQPPSQAWQ SVWQNSAGGG DDVSYGSGGS
SGHGNLDSQG
