FRIGI_ARATH
ID FRIGI_ARATH Reviewed; 609 AA.
AC P0DH90; O65274; Q9FDW0;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Protein FRIGIDA {ECO:0000303|PubMed:11030654};
GN Name=FRI {ECO:0000303|PubMed:11030654};
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 / MRNA], AND VARIANTS EDI-0; SF-2 AND SHA.
RC STRAIN=cv. Edi-0, cv. H51, cv. Sf-2, and cv. Sha;
RX PubMed=11030654; DOI=10.1126/science.290.5490.344;
RA Johanson U., West J., Lister C., Michaels S., Amasino R.M., Dean C.;
RT "Molecular analysis of FRIGIDA, a major determinant of natural variation in
RT Arabidopsis flowering time.";
RL Science 290:344-347(2000).
RN [2]
RP FUNCTION, AND GENE 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 [3]
RP SUBCELLULAR LOCATION, INTERACTION WITH SUF4, AND SUBUNIT.
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 [4]
RP FUNCTION.
RX PubMed=19567704; DOI=10.1105/tpc.109.067967;
RA Jiang D., Gu X., He Y.;
RT "Establishment of the winter-annual growth habit via FRIGIDA-mediated
RT histone methylation at FLOWERING LOCUS C in Arabidopsis.";
RL Plant Cell 21:1733-1746(2009).
RN [5]
RP FUNCTION, INDUCTION BY VERNALIZATION, AND TISSUE SPECIFICITY.
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 [6]
RP INTERACTION WITH CBP20; FIP1 AND FIP2.
RX PubMed=19429606; DOI=10.1104/pp.109.137448;
RA Geraldo N., Baeurle I., Kidou S., Hu X., Dean C.;
RT "FRIGIDA delays flowering in Arabidopsis via a cotranscriptional mechanism
RT involving direct interaction with the nuclear cap-binding complex.";
RL Plant Physiol. 150:1611-1618(2009).
RN [7]
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 [8]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY IN THE FRI-C COMPLEX, AND
RP INTERACTION WITH RIN1; FLX; SUF4; FRL1 AND FES1.
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 the regulation of flowering time in the late-
CC flowering phenotype. Involved in the enrichment of a WDR5A-containing
CC COMPASS-like complex at the 'FLOWERING LOCUS C' that trimethylates
CC histone H3 'Lys-4', leading to FLC up-regulation and RNA levels
CC increase (PubMed:19567704). Variants with an early-flowering phenotype
CC (Including cv. Columbia, cv. Landsberg Erecta and cv. Wassilewskija)
CC show loss-of-function mutations of FRI. Able to delay flowering
CC independently of FRL1 activity. Dispensable for the reactivation of FLC
CC in early embryogenesis, but required to maintain high levels of FLC
CC expression in later embryonic and vegetative development. Suppresses
CC the repression of FLC by the autonomous pathway, but has no effect on
CC the expression of the genes involved in this pathway.
CC {ECO:0000269|PubMed:14973192, ECO:0000269|PubMed:19121105,
CC ECO:0000269|PubMed:19567704, 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 (via N-
CC terminus) with FRL1 and (via C-terminus) with FLX (via N-terminus),
CC SUF4 (via C-terminus) and FES1 (via C-terminus). Interacts with ASHH2
CC and RIN1, a component of the SWR1 chromatin-remodeling complex
CC (PubMed:17138694, PubMed:20711170, PubMed:21282526). Interacts with
CC CBP20, FIP1 and FIP2 (PubMed:19429606). {ECO:0000269|PubMed:17138694,
CC ECO:0000269|PubMed:19429606, ECO:0000269|PubMed:20711170,
CC ECO:0000269|PubMed:21282526}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:17138694}.
CC -!- TISSUE SPECIFICITY: Expressed in ovules, but not in stamens.
CC {ECO:0000269|PubMed:19121105}.
CC -!- INDUCTION: Not regulated by vernalization.
CC {ECO:0000269|PubMed:19121105}.
CC -!- SIMILARITY: Belongs to the Frigida family. {ECO:0000305}.
CC -!- CAUTION: Has been shown to be inactive in cv. Columbia (AC Q67Z93), cv.
CC Landsberg Erecta and cv. Wassilewskija due to loss-of-function
CC mutations. The sequence shown is from strain cv. H51. {ECO:0000305}.
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DR EMBL; AF228500; AAG23415.1; -; mRNA.
DR EMBL; AF228499; AAG23414.1; -; Genomic_DNA.
DR AlphaFoldDB; P0DH90; -.
DR SMR; P0DH90; -.
DR PRIDE; P0DH90; -.
DR PhylomeDB; P0DH90; -.
DR ExpressionAtlas; P0DH90; baseline and differential.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
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; Nucleus.
FT CHAIN 1..609
FT /note="Protein FRIGIDA"
FT /id="PRO_0000087336"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 60..97
FT /evidence="ECO:0000255"
FT COILED 409..440
FT /evidence="ECO:0000255"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 55
FT /note="F -> I (in strain: cv. Sha)"
FT VARIANT 79
FT /note="L -> I (in strain: cv. SF-2)"
FT VARIANT 146
FT /note="G -> E (in strain: cv. Edi-0)"
FT VARIANT 148
FT /note="M -> I (in strain: cv. Edi-0)"
SQ SEQUENCE 609 AA; 68443 MW; FE8572DFF3E6726F CRC64;
MSNYPPTVAA QPTTTANPLL QRHQSEQRRR ELPKIVETES TSMDITIGQS KQPQFLKSID
ELAAFSVAVE TFKRQFDDLQ KHIESIENAI DSKLESNGVV LAARNNNFHQ PMLSPPRNNV
SVETTVTVSQ PSQEIVPETS NKPEGGRMCE LMCSKGLRKY IYANISDQAK LMEEIPSALK
LAKEPAKFVL DCIGKFYLQG RRAFTKESPM SSARQVSLLI LESFLLMPDR GKGKVKIESW
IKDEAETAAV AWRKRLMTEG GLAAAEKMDA RGLLLLVACF GVPSNFRSTD LLDLIRMSGS
NEIAGALKRS QFLVPMVSGI VESSIKRGMH IEALEMVYTF GMEDKFSAAL VLTSFLKMSK
ESFERAKRKA QSPLAFKEAA TKQLAVLSSV MQCMETHKLD PAKELPGWQI KEQIVSLEKD
TLQLDKEMEE KARSLSLMEE AALAKRMYNQ QIKRPRLSPM EMPPVTSSSY SPIYRDRSFP
SQRDDDQDEI SALVSSYLGP STSFPHRSRR SPEYMVPLPH GGLGRSVYAY EHLAPNSYSP
GHGHRLHRQY SPSLVHGQRH PLQYSPPIHG QQQLPYGIQR VYRHSPSEER YLGLSNQRSP
RSNSSLDPK
