SUF4_ARATH
ID SUF4_ARATH Reviewed; 367 AA.
AC Q9C5G0; F4I7U0; Q56YA6; Q8LE54; Q94BZ2; Q9FYI5;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Protein SUPPRESSOR OF FRI 4 {ECO:0000303|PubMed:17079264};
GN Name=SUF4 {ECO:0000303|PubMed:17079264};
GN OrderedLocusNames=At1g30970 {ECO:0000312|Araport:AT1G30970};
GN ORFNames=F17F8.14 {ECO:0000312|EMBL:AAF98186.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 150-367.
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=17079264; DOI=10.1242/dev.02684;
RA Kim S.Y., Michaels S.D.;
RT "SUPPRESSOR OF FRI 4 encodes a nuclear-localized protein that is required
RT for delayed flowering in winter-annual Arabidopsis.";
RL Development 133:4699-4707(2006).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INDUCTION, ALTERNATIVE
RP SPLICING, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, SUBUNIT, AND
RP INTERACTION WITH LD; FRI AND FRL1.
RX PubMed=17138694; DOI=10.1105/tpc.106.045179;
RA Kim S., Choi K., Park C., Hwang H.J., Lee I.;
RT "SUPPRESSOR OF FRIGIDA4, encoding a C2H2-Type zinc finger protein,
RT represses flowering by transcriptional activation of Arabidopsis FLOWERING
RT LOCUS C.";
RL Plant Cell 18:2985-2998(2006).
RN [8]
RP FUNCTION.
RX PubMed=19121105; DOI=10.1111/j.1365-313x.2008.03776.x;
RA Choi J., Hyun Y., Kang M.J., In Yun H., Yun J.Y., Lister C., Dean C.,
RA Amasino R.M., Noh B., Noh Y.S., Choi Y.;
RT "Resetting and regulation of Flowering Locus C expression during
RT Arabidopsis reproductive development.";
RL Plant J. 57:918-931(2009).
RN [9]
RP INTERACTION WITH ASHH2.
RX PubMed=20711170; DOI=10.1038/emboj.2010.198;
RA Ko J.H., Mitina I., Tamada Y., Hyun Y., Choi Y., Amasino R.M., Noh B.,
RA Noh Y.S.;
RT "Growth habit determination by the balance of histone methylation
RT activities in Arabidopsis.";
RL EMBO J. 29:3208-3215(2010).
RN [10]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY IN THE FRI-C COMPLEX, AND
RP INTERACTION WITH FRI; SWC6 AND FRL1.
RX PubMed=21282526; DOI=10.1105/tpc.110.075911;
RA Choi K., Kim J., Hwang H.J., Kim S., Park C., Kim S.Y., Lee I.;
RT "The FRIGIDA complex activates transcription of FLC, a strong flowering
RT repressor in Arabidopsis, by recruiting chromatin modification factors.";
RL Plant Cell 23:289-303(2011).
RN [11]
RP INTERACTION WITH MED18, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=24451981; DOI=10.1038/ncomms4064;
RA Lai Z., Schluttenhofer C.M., Bhide K., Shreve J., Thimmapuram J., Lee S.Y.,
RA Yun D.-J., Mengiste T.;
RT "MED18 interaction with distinct transcription factors regulates multiple
RT plant functions.";
RL Nat. Commun. 5:3064-3064(2014).
CC -!- FUNCTION: Sequence-specific DNA binding factor that recognizes the 5'-
CC CCAAATTTTAAGTTT-3' sequence. Recruits the FRI-C complex to the FLC
CC promoter. Required for FRI-mediated FLC activation, but has no effect
CC on the expression of MAF1, MAF2, MAF3, MAF5, UFC and CO. Dispensable
CC for the reactivation of FLC in early embryogenesis, but required to
CC maintain high levels of FLC expression in later embryonic and
CC vegetative development. {ECO:0000269|PubMed:17079264,
CC ECO:0000269|PubMed:17138694, ECO:0000269|PubMed:19121105,
CC ECO:0000269|PubMed:21282526}.
CC -!- SUBUNIT: Homodimer. Component of the transcription activator complex
CC FRI-C composed of FRI, FRL1, SUF4, FLX and FES1. Interacts with LD,
CC ASHH2, FRL1, (via C-terminus) with FRI (via C-terminus), and with SWC6,
CC a component of the SWR1 chromatin-remodeling complex. Binds to MED18 to
CC regulate flowering time; recruits MED18 to FLC promoter
CC (PubMed:24451981). {ECO:0000269|PubMed:17138694,
CC ECO:0000269|PubMed:20711170, ECO:0000269|PubMed:21282526,
CC ECO:0000269|PubMed:24451981}.
CC -!- INTERACTION:
CC Q9C5G0; Q9FDW0: FRI; NbExp=3; IntAct=EBI-2126140, EBI-2126171;
CC Q9C5G0; Q9FFF1: FRL1; NbExp=3; IntAct=EBI-2126140, EBI-2126272;
CC Q9C5G0; Q38796: LD; NbExp=3; IntAct=EBI-2126140, EBI-2126221;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17079264,
CC ECO:0000269|PubMed:17138694, ECO:0000269|PubMed:24451981}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C5G0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C5G0-2; Sequence=VSP_053263;
CC -!- TISSUE SPECIFICITY: Expressed in root, shoot apex, leaves, stem and
CC flowers. Expressed in expanding leaves, in the vasculature of fully
CC expanded leaves, in the inflorescence, throughout young floral
CC primordia, in the carpels of older flowers and in fertilized ovules.
CC {ECO:0000269|PubMed:17079264, ECO:0000269|PubMed:17138694}.
CC -!- DEVELOPMENTAL STAGE: Barely detectable in 3-days-old seedling, and then
CC increases. {ECO:0000269|PubMed:17138694}.
CC -!- INDUCTION: Not regulated by photoperiod or vernalization.
CC {ECO:0000269|PubMed:17079264, ECO:0000269|PubMed:17138694}.
CC -!- DISRUPTION PHENOTYPE: Early flowering. {ECO:0000269|PubMed:17079264,
CC ECO:0000269|PubMed:17138694}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF98186.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD94400.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC000107; AAF98186.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31298.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31299.1; -; Genomic_DNA.
DR EMBL; AF360277; AAK25987.1; -; mRNA.
DR EMBL; AY051039; AAK93716.1; -; mRNA.
DR EMBL; AY085612; AAM62833.1; -; mRNA.
DR EMBL; AY039540; AAK62595.1; -; mRNA.
DR EMBL; AK221417; BAD94400.1; ALT_INIT; mRNA.
DR RefSeq; NP_001077634.1; NM_001084165.1. [Q9C5G0-2]
DR RefSeq; NP_564369.1; NM_102836.3. [Q9C5G0-1]
DR AlphaFoldDB; Q9C5G0; -.
DR SMR; Q9C5G0; -.
DR BioGRID; 25219; 17.
DR IntAct; Q9C5G0; 12.
DR MINT; Q9C5G0; -.
DR STRING; 3702.AT1G30970.1; -.
DR PaxDb; Q9C5G0; -.
DR PRIDE; Q9C5G0; -.
DR ProteomicsDB; 228399; -. [Q9C5G0-1]
DR EnsemblPlants; AT1G30970.1; AT1G30970.1; AT1G30970. [Q9C5G0-1]
DR EnsemblPlants; AT1G30970.2; AT1G30970.2; AT1G30970. [Q9C5G0-2]
DR GeneID; 839984; -.
DR Gramene; AT1G30970.1; AT1G30970.1; AT1G30970. [Q9C5G0-1]
DR Gramene; AT1G30970.2; AT1G30970.2; AT1G30970. [Q9C5G0-2]
DR KEGG; ath:AT1G30970; -.
DR Araport; AT1G30970; -.
DR TAIR; locus:2015776; AT1G30970.
DR eggNOG; KOG2893; Eukaryota.
DR HOGENOM; CLU_037132_1_0_1; -.
DR InParanoid; Q9C5G0; -.
DR OMA; GITHMPQ; -.
DR PhylomeDB; Q9C5G0; -.
DR PRO; PR:Q9C5G0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C5G0; baseline and differential.
DR Genevisible; Q9C5G0; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:TAIR.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR GO; GO:0051568; P:histone H3-K4 methylation; IDA:TAIR.
DR GO; GO:0009910; P:negative regulation of flower development; IGI:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:TAIR.
DR InterPro; IPR003656; Znf_BED.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS50808; ZF_BED; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Differentiation; DNA-binding;
KW Flowering; Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..367
FT /note="Protein SUPPRESSOR OF FRI 4"
FT /id="PRO_0000423725"
FT ZN_FING 7..66
FT /note="BED-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT REGION 246..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT VAR_SEQ 1..65
FT /note="MGKKKKRATEKVWCYYCDREFDDEKILVQHQKAKHFKCHVCHKKLSTASGMV
FT IHVLQVHKENVTK -> MFFRFIKRMLQSI (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_053263"
FT CONFLICT 154
FT /note="P -> F (in Ref. 3; AAK62595)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="D -> N (in Ref. 4; AAM62833)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 367 AA; 39801 MW; B9B2356EC3D063EE CRC64;
MGKKKKRATE KVWCYYCDRE FDDEKILVQH QKAKHFKCHV CHKKLSTASG MVIHVLQVHK
ENVTKVPNAK DGRDSTDIEI YGMQGIPPHV LTAHYGEEED EPPAKVAKVE IPSAPLGGVV
PRPYGMVYPP QQVPGAVPAR PMYYPGPPMR HPAPVWQMPP PRPQQWYPQN PALSVPPAAH
LGYRPQPLFP VQNMGMTPTP TSAPAIQPSP VTGVTPPGIP TSSPAMPVPQ PLFPVVNNSI
PSQAPPFSAP LPVGGAQQPS HADALGSADA YPPNNSIPGG TNAHSYASGP NTSGPSIGPP
PVIANKAPSN QPNEVYLVWD DEAMSMEERR MSLPKYKVHD ETSQMNSINA AIDRRISESR
LAGRMAF
