FRL1A_ARATH
ID FRL1A_ARATH Reviewed; 470 AA.
AC Q9FFF1;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=FRIGIDA-like protein 1;
DE Short=AtFRIL1;
DE AltName: Full=Protein SUPPRESSOR OF FRI 8;
GN Name=FRL1; Synonyms=SUF8; OrderedLocusNames=At5g16320; ORFNames=MQK4.4;
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 [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND GENE
RP FAMILY.
RX PubMed=14973192; DOI=10.1073/pnas.0306778101;
RA Michaels S.D., Bezerra I.C., Amasino R.M.;
RT "FRIGIDA-related genes are required for the winter-annual habit in
RT Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:3281-3285(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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 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 [5]
RP INTERACTION WITH SUF4.
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 [6]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=17056759; DOI=10.1104/pp.106.085571;
RA Schlappi M.R.;
RT "FRIGIDA LIKE 2 is a functional allele in Landsberg erecta and compensates
RT for a nonsense allele of FRIGIDA LIKE 1.";
RL Plant Physiol. 142:1728-1738(2006).
RN [7]
RP GENE FAMILY, NOMENCLATURE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=20405310; DOI=10.1007/s11103-010-9635-2;
RA Risk J.M., Laurie R.E., Macknight R.C., Day C.L.;
RT "FRIGIDA and related proteins have a conserved central domain and family
RT specific N- and C- terminal regions that are functionally important.";
RL Plant Mol. Biol. 73:493-505(2010).
RN [8]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE FRI-C
RP COMPLEX, AND INTERACTION WITH FRI AND SUF4.
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).
CC -!- FUNCTION: Required for FRI-mediated up-regulation of FLC transcripts,
CC but not redundant with FRI and only partially redundant with FRL2.
CC Required for the stabilization of the FRI-C complex.
CC {ECO:0000269|PubMed:14973192, ECO:0000269|PubMed:17056759,
CC ECO:0000269|PubMed:21282526}.
CC -!- SUBUNIT: Component of the transcription activator complex FRI-C
CC composed of FRI, FRL1, SUF4, FLX and FES1. Interacts with FRI and SUF4.
CC {ECO:0000269|PubMed:17138694, ECO:0000269|PubMed:21282526}.
CC -!- INTERACTION:
CC Q9FFF1; Q9C5G0: SUF4; NbExp=3; IntAct=EBI-2126272, EBI-2126140;
CC -!- TISSUE SPECIFICITY: Expressed during seed development and in dry seed.
CC Preferentially expressed in the chalazal endosperm during early stages
CC of seed development. {ECO:0000269|PubMed:20405310}.
CC -!- DISRUPTION PHENOTYPE: Reduced levels of FLC expression and early
CC flowering, but not redundant with FRI. Frl1 and frl2 double mutants
CC flower earlier than frl1 single mutant, due to a partial redundancy.
CC {ECO:0000269|PubMed:14973192}.
CC -!- MISCELLANEOUS: In cv. Columbia and cv. Landsberg erecta, either FRL1 or
CC FRL2, but not both, is functional and required for FRI-mediated up-
CC regulation of FLC (PubMed:17056759). {ECO:0000305|PubMed:17056759}.
CC -!- SIMILARITY: Belongs to the Frigida family. {ECO:0000305}.
CC -!- CAUTION: In cv. Landsberg erecta, FRL1 (AC P0DKC9) is not functional
CC due to a naturally occurring premature stop codon at position 279.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BK004884; DAA05285.1; -; Genomic_DNA.
DR EMBL; AB005242; BAB09599.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92279.1; -; Genomic_DNA.
DR EMBL; AY075663; AAL77670.1; -; mRNA.
DR EMBL; AY101525; AAM26646.1; -; mRNA.
DR RefSeq; NP_197136.1; NM_121637.4.
DR AlphaFoldDB; Q9FFF1; -.
DR SMR; Q9FFF1; -.
DR BioGRID; 16769; 8.
DR IntAct; Q9FFF1; 9.
DR STRING; 3702.AT5G16320.1; -.
DR PaxDb; Q9FFF1; -.
DR PRIDE; Q9FFF1; -.
DR EnsemblPlants; AT5G16320.1; AT5G16320.1; AT5G16320.
DR GeneID; 831493; -.
DR Gramene; AT5G16320.1; AT5G16320.1; AT5G16320.
DR KEGG; ath:AT5G16320; -.
DR Araport; AT5G16320; -.
DR TAIR; locus:2171327; AT5G16320.
DR eggNOG; ENOG502QUKS; Eukaryota.
DR HOGENOM; CLU_032433_0_0_1; -.
DR InParanoid; Q9FFF1; -.
DR OMA; FIFEFGL; -.
DR OrthoDB; 1089519at2759; -.
DR PhylomeDB; Q9FFF1; -.
DR PRO; PR:Q9FFF1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFF1; baseline and differential.
DR Genevisible; Q9FFF1; AT.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR InterPro; IPR012474; Frigida.
DR Pfam; PF07899; Frigida; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Developmental protein; Differentiation; Flowering;
KW Reference proteome.
FT CHAIN 1..470
FT /note="FRIGIDA-like protein 1"
FT /id="PRO_0000423738"
FT REGION 355..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 336..369
FT /evidence="ECO:0000255"
SQ SEQUENCE 470 AA; 52831 MW; 2924997BB01366D6 CRC64;
MTASETIATA INQIDEKKEK LKKAFDDLQA HRSLLSPSFS LSWSEIDSHF SSLQSSLASR
FRLLHSTSPL EHDSYRIDAS DAGKSSSSEE VSEQPVVEPE LRALCEKIDG IGLIKYLIRI
WDDETPLNQE VSAAIRYSPD TASMVLDAIE GSNYTPSSSG RSFDVRRVFV LLMEVLIEIN
ANITVDTRNR AKKLAYHWKS KVGVKPFEAL VFLHLVAAFE LGSEFDTEEL SDYVFMIAKY
KQATLVCNKI GVDRKRVGKL IKTLLDSGKP ILAVKFMYEC GMTDEFEPIP VLKSYIKDCR
EAALRVCVED NYSLKSQNEA SDKEVSALKP LIKIIKDQNL ESEFTQEKVE ERVEELEKNK
ALRKRNTTNP PKQEPQQKGK KRTRDCKNGS QVPVPSQQLL SRPEALLMPE HSHHGLQLNP
YGLMTSAFSG VVVNPLTGLF GSGATPQSLY YAQQTGYVLP PQYHPPYYSQ
