ID   FLU_ARATH               Reviewed;         316 AA.
AC   Q940U6; B9DI70; Q9LJH7;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   24-JAN-2024, entry version 142.
DE   RecName: Full=Protein FLUORESCENT IN BLUE LIGHT, chloroplastic;
DE   Flags: Precursor;
GN   Name=FLU; OrderedLocusNames=At3g14110; ORFNames=MAG2.7;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(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 97-316 (ISOFORM 1).
RC   STRAIN=cv. Columbia; TISSUE=Flower, and Silique;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [6]
RP   FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ALA-146 AND ALA-262, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=11606728; DOI=10.1073/pnas.221252798;
RA   Meskauskiene R., Nater M., Goslings D., Kessler F., op den Camp R.G.L.,
RA   Apel K.;
RT   "FLU: a negative regulator of chlorophyll biosynthesis in Arabidopsis
RT   thaliana.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:12826-12831(2001).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=14508004; DOI=10.1105/tpc.014662;
RA   op den Camp R.G.L., Przybyla D., Ochsenbein C., Laloi C., Kim C., Danon A.,
RA   Wagner D., Hideg E., Goebel C., Feussner I., Nater M., Apel K.;
RT   "Rapid induction of distinct stress responses after the release of singlet
RT   oxygen in Arabidopsis.";
RL   Plant Cell 15:2320-2332(2003).
RN   [8]
RP   FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ALA-262, AND INTERACTION
RP   WITH HEMA1 AND HEMA2.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=15584960; DOI=10.1111/j.1365-313x.2004.02262.x;
RA   Goslings D., Meskauskiene R., Kim C., Lee K.P., Nater M., Apel K.;
RT   "Concurrent interactions of heme and FLU with Glu tRNA reductase (HEMA1),
RT   the target of metabolic feedback inhibition of tetrapyrrole biosynthesis,
RT   in dark- and light-grown Arabidopsis plants.";
RL   Plant J. 40:957-967(2004).
RN   [9]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia;
RX   PubMed=18182022; DOI=10.1111/j.1365-313x.2008.03409.x;
RA   Przybyla D., Goebel C., Imboden A., Hamberg M., Feussner I., Apel K.;
RT   "Enzymatic, but not non-enzymatic, 1O2-mediated peroxidation of
RT   polyunsaturated fatty acids forms part of the EXECUTER1-dependent stress
RT   response program in the flu mutant of Arabidopsis thaliana.";
RL   Plant J. 54:236-248(2008).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA   Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA   van Wijk K.J.;
RT   "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT   proteome.";
RL   PLoS ONE 3:E1994-E1994(2008).
RN   [11]
RP   SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE FLU-CONTAINING CHLOROPLAST
RP   MEMBRANE COMPLEX.
RX   PubMed=22212719; DOI=10.1016/j.febslet.2011.12.029;
RA   Kauss D., Bischof S., Steiner S., Apel K., Meskauskiene R.;
RT   "FLU, a negative feedback regulator of tetrapyrrole biosynthesis, is
RT   physically linked to the final steps of the Mg(++)-branch of this
RT   pathway.";
RL   FEBS Lett. 586:211-216(2012).
CC   -!- FUNCTION: Negative regulator of tetrapyrrole biosynthesis (including
CC       chlorophyll) in chloroplasts, probably via HEMA1 repression. Inhibits
CC       especially the magnesium ion Mg(2+) branch of tetrapyrrole
CC       biosynthesis, but independently of heme. {ECO:0000269|PubMed:11606728,
CC       ECO:0000269|PubMed:14508004, ECO:0000269|PubMed:15584960,
CC       ECO:0000269|PubMed:18182022}.
CC   -!- SUBUNIT: Part of the FLU-containing chloroplast membrane complex
CC       composed of FLU, CRD1, PORB, PORC, CHLP and HEMA1. Interacts with HEMA1
CC       (via C-terminus) only in the absence of light. No interaction with
CC       HEMA2. {ECO:0000269|PubMed:15584960, ECO:0000269|PubMed:22212719}.
CC   -!- INTERACTION:
CC       Q940U6; Q9M591: CRD1; NbExp=5; IntAct=EBI-2319882, EBI-7632098;
CC       Q940U6; P42804: HEMA1; NbExp=3; IntAct=EBI-2319882, EBI-2319900;
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC       {ECO:0000269|PubMed:18431481}; Single-pass membrane protein. Plastid,
CC       chloroplast thylakoid membrane; Single-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q940U6-1; Sequence=Displayed;
CC   -!- DISRUPTION PHENOTYPE: Loss of ability to restrict the accumulation of
CC       protochloro-phyllide (Pchlide) and delta-amin-olevulinic acid (ALA) in
CC       the dark, leading to a strong Pchlide fluorescence in etiolated mutant
CC       seedlings exposed to blue light. Rapid bleaching and death of plants
CC       transferred from the dark to the light, mediated by singlet oxygen
CC       production and enzymatic peroxidation of linolenic acid.
CC       {ECO:0000269|PubMed:11606728, ECO:0000269|PubMed:14508004,
CC       ECO:0000269|PubMed:15584960, ECO:0000269|PubMed:18182022}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB02975.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP000600; BAB02975.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE75470.1; -; Genomic_DNA.
DR   EMBL; AF446890; AAL38623.1; -; mRNA.
DR   EMBL; AY052677; AAK96581.1; -; mRNA.
DR   EMBL; AY087529; AAM65071.1; -; mRNA.
DR   EMBL; AK317782; BAH20437.1; -; mRNA.
DR   RefSeq; NP_566478.1; NM_112267.4. [Q940U6-1]
DR   PDB; 4YVO; X-ray; 1.45 A; A=189-316.
DR   PDB; 4YVQ; X-ray; 2.40 A; C=195-316.
DR   PDB; 5CHE; X-ray; 3.20 A; E/F=195-316.
DR   PDBsum; 4YVO; -.
DR   PDBsum; 4YVQ; -.
DR   PDBsum; 5CHE; -.
DR   AlphaFoldDB; Q940U6; -.
DR   SMR; Q940U6; -.
DR   BioGRID; 5962; 1.
DR   IntAct; Q940U6; 5.
DR   MINT; Q940U6; -.
DR   STRING; 3702.Q940U6; -.
DR   PaxDb; 3702-AT3G14110-3; -.
DR   ProteomicsDB; 230523; -. [Q940U6-1]
DR   EnsemblPlants; AT3G14110.1; AT3G14110.1; AT3G14110. [Q940U6-1]
DR   GeneID; 820628; -.
DR   Gramene; AT3G14110.1; AT3G14110.1; AT3G14110. [Q940U6-1]
DR   KEGG; ath:AT3G14110; -.
DR   Araport; AT3G14110; -.
DR   TAIR; AT3G14110; FLU.
DR   eggNOG; ENOG502QTEG; Eukaryota.
DR   InParanoid; Q940U6; -.
DR   PhylomeDB; Q940U6; -.
DR   PRO; PR:Q940U6; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q940U6; baseline and differential.
DR   GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR044243; FLU.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR47310; PROTEIN FLUORESCENT IN BLUE LIGHT, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR47310:SF2; PROTEIN FLUORESCENT IN BLUE LIGHT, CHLOROPLASTIC; 1.
DR   Pfam; PF13424; TPR_12; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50293; TPR_REGION; 1.
DR   Genevisible; Q940U6; AT.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Chloroplast; Coiled coil; Membrane;
KW   Plastid; Reference proteome; Repeat; Thylakoid; TPR repeat;
KW   Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..26
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..316
FT                   /note="Protein FLUORESCENT IN BLUE LIGHT, chloroplastic"
FT                   /id="PRO_0000407552"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REPEAT          203..236
FT                   /note="TPR 1"
FT   REPEAT          243..276
FT                   /note="TPR 2"
FT   REPEAT          283..316
FT                   /note="TPR 3"
FT   COILED          144..175
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         146
FT                   /note="A->V: In flu1-4; rapid bleaching and death when
FT                   transferred from the dark to the light, accumulation of
FT                   Pchlide and ALA."
FT                   /evidence="ECO:0000269|PubMed:11606728"
FT   MUTAGEN         262
FT                   /note="A->V: In flu1-1; rapid bleaching and death when
FT                   transferred from the dark to the light, accumulation of
FT                   Pchlide and ALA, and impaired HEMA1 interaction."
FT                   /evidence="ECO:0000269|PubMed:11606728,
FT                   ECO:0000269|PubMed:15584960"
FT   CONFLICT        97
FT                   /note="M -> L (in Ref. 5; BAH20437)"
FT                   /evidence="ECO:0000305"
FT   HELIX           199..215
FT                   /evidence="ECO:0007829|PDB:4YVO"
FT   HELIX           219..235
FT                   /evidence="ECO:0007829|PDB:4YVO"
FT   HELIX           239..255
FT                   /evidence="ECO:0007829|PDB:4YVO"
FT   HELIX           259..276
FT                   /evidence="ECO:0007829|PDB:4YVO"
FT   HELIX           282..295
FT                   /evidence="ECO:0007829|PDB:4YVO"
FT   HELIX           299..313
FT                   /evidence="ECO:0007829|PDB:4YVO"
SQ   SEQUENCE   316 AA;  34587 MW;  8A647B74684B6514 CRC64;
     MAALIRCCSS FSHTSGGQPP PRDKSRAPEI GKFATSIGYS VVRKPGDHPP FSKIIHSSSQ
     PKERQGKGIL QTPFASVGSL DKFSAFEGIG RLKLPVMAVL LTNSLQMATP LEALAAEICE
     PESSMFSMPI LLLVALIGAT VGGLLARQRK GELQRLNEQL RQINAALRRQ AKIESYAPSL
     SYAPVGARIP DSEIIVEPKK QELISKLKTG KTFLRNQEPE KAYTEFKIAL ELAQSLKDPT
     EEKKAARGLG ASLQRQGKYR EAIQYHSMVL AISKRESEDS GITEAYGAIA DCYTELGDLE
     KAGKFYDTYI ARLETD
//