FWA_ARATH
ID FWA_ARATH Reviewed; 686 AA.
AC Q9FVI6; O65608; Q9M0K7;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Homeobox-leucine zipper protein HDG6;
DE AltName: Full=HD-ZIP protein HDG6;
DE AltName: Full=Homeobox protein FWA;
DE AltName: Full=Homeodomain GLABRA 2-like protein 6;
DE AltName: Full=Homeodomain transcription factor HDG6;
DE AltName: Full=Protein HOMEODOMAIN GLABROUS 6;
GN Name=HDG6; Synonyms=FWA, HDGL2-6; OrderedLocusNames=At4g25530;
GN ORFNames=M7J2.100;
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].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=11090618; DOI=10.1016/s1097-2765(05)00090-0;
RA Soppe W.J.J., Jacobsen S.E., Alonso-Blanco C., Jackson J.P., Kakutani T.,
RA Koornneef M., Peeters A.J.M.;
RT "The late flowering phenotype of fwa mutants is caused by gain-of-function
RT epigenetic alleles of a homeodomain gene.";
RL Mol. Cell 6:791-802(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 GENE FAMILY.
RX PubMed=10809443; DOI=10.1023/a:1006368316413;
RA Tavares R., Aubourg S., Lecharny A., Kreis M.;
RT "Organization and structural evolution of four multigene families in
RT Arabidopsis thaliana: AtLCAD, AtLGT, AtMYST and AtHD-GL2.";
RL Plant Mol. Biol. 42:703-717(2000).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16778018; DOI=10.1104/pp.106.077388;
RA Nakamura M., Katsumata H., Abe M., Yabe N., Komeda Y., Yamamoto K.T.,
RA Takahashi T.;
RT "Characterization of the class IV homeodomain-leucine zipper gene family in
RT Arabidopsis.";
RL Plant Physiol. 141:1363-1375(2006).
RN [6]
RP REGULATION.
RX PubMed=17921315; DOI=10.1105/tpc.107.052373;
RA Jiang D., Yang W., He Y., Amasino R.M.;
RT "Arabidopsis relatives of the human lysine-specific demethylase1 repress
RT the expression of FWA and FLOWERING LOCUS C and thus promote the floral
RT transition.";
RL Plant Cell 19:2975-2987(2007).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH FT.
RX PubMed=17189287; DOI=10.1093/pcp/pcl061;
RA Ikeda Y., Kobayashi Y., Yamaguchi A., Abe M., Araki T.;
RT "Molecular basis of late-flowering phenotype caused by dominant epi-alleles
RT of the FWA locus in Arabidopsis.";
RL Plant Cell Physiol. 48:205-220(2007).
CC -!- FUNCTION: Probable transcription factor involved in the regulation of
CC time of flowering through the photoperiod flowering pathway. May
CC repress FT. {ECO:0000269|PubMed:17189287}.
CC -!- SUBUNIT: Interacts with FT. {ECO:0000269|PubMed:17189287}.
CC -!- INTERACTION:
CC Q9FVI6; Q9SXZ2: FT; NbExp=2; IntAct=EBI-1393271, EBI-636490;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in siliques, ovules and germinating
CC seeds. {ECO:0000269|PubMed:17189287}.
CC -!- DEVELOPMENTAL STAGE: Detected in siliques from 3 days after pollination
CC until maturity of seeds.
CC -!- MISCELLANEOUS: Under epigenetic control. In wild-type plant, FWA is
CC silenced in the sporophyte. The epi-allele fwa mutants (which do not
CC have a change in the nucleotide sequence of FWA) cause a late-flowering
CC phenotype due to ectopic FWA expression in sporophytic tissues.
CC Repression of FWA is dependent on histone H3 'Lys-4' methylation and
CC cytosine methylation which are partly controlled by the lysine-specific
CC demthylase 1 (LSD1) homologs, LDL1 and LDL2.
CC -!- SIMILARITY: Belongs to the HD-ZIP homeobox family. Class IV subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18173.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81363.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF178688; AAG09302.1; -; Genomic_DNA.
DR EMBL; AF243535; AAK28350.1; -; mRNA.
DR EMBL; AL022197; CAA18173.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161563; CAB81363.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85074.1; -; Genomic_DNA.
DR PIR; A85295; A85295.
DR RefSeq; NP_567722.1; NM_118685.3.
DR AlphaFoldDB; Q9FVI6; -.
DR SMR; Q9FVI6; -.
DR BioGRID; 13945; 9.
DR IntAct; Q9FVI6; 2.
DR STRING; 3702.AT4G25530.1; -.
DR PaxDb; Q9FVI6; -.
DR PRIDE; Q9FVI6; -.
DR ProteomicsDB; 247380; -.
DR EnsemblPlants; AT4G25530.1; AT4G25530.1; AT4G25530.
DR GeneID; 828658; -.
DR Gramene; AT4G25530.1; AT4G25530.1; AT4G25530.
DR KEGG; ath:AT4G25530; -.
DR Araport; AT4G25530; -.
DR TAIR; locus:2131814; AT4G25530.
DR eggNOG; ENOG502QWUC; Eukaryota.
DR HOGENOM; CLU_015002_2_1_1; -.
DR InParanoid; Q9FVI6; -.
DR OMA; FRYISSP; -.
DR OrthoDB; 834743at2759; -.
DR PhylomeDB; Q9FVI6; -.
DR PRO; PR:Q9FVI6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9FVI6; baseline and differential.
DR Genevisible; Q9FVI6; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:TAIR.
DR GO; GO:0031047; P:gene silencing by RNA; IMP:TAIR.
DR GO; GO:0009911; P:positive regulation of flower development; IMP:TAIR.
DR GO; GO:0006349; P:regulation of gene expression by genomic imprinting; IEP:TAIR.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR042160; GLABRA2/ANL2/PDF2/ATML1-like.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR002913; START_lipid-bd_dom.
DR PANTHER; PTHR45654; PTHR45654; 1.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF01852; START; 1.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00234; START; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS50848; START; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Developmental protein; DNA-binding; Homeobox; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..686
FT /note="Homeobox-leucine zipper protein HDG6"
FT /id="PRO_0000048877"
FT DOMAIN 206..439
FT /note="START"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT DNA_BIND 38..98
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 103..170
FT /evidence="ECO:0000255"
FT CONFLICT 311
FT /note="L -> I (in Ref. 1; AAG09302/AAK28350)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 686 AA; 76253 MW; D4E506F66532B184 CRC64;
MNGQGDLDAV GNIPKPGEAE GDEIDMINDM SGVNDQDGGR MRRTHRRTAY QTQELENFYM
ENPHPTEEQR YELGQRLNMG VNQVKNWFQN KRNLEKINND HLENVTLREE HDRLLATQDQ
LRSAMLRSLC NICGKATNCG DTEYEVQKLM AENANLEREI DQFNSRYLSH PKQRMVSTSE
QAPSSSSNPG INATPVLDFS GGTRTSEKET SIFLNLAITA LRELITLGEV DCPFWMIDPI
VRSKGVSKIY EKYRSSFNNV TKPPGQIVEA SRAKGLVPMT CVTLVKTLMD TGKWVNVFAP
IVPVASTHKV LSTGSGGTKS GSLQQIQAEF QVISPLVPKR KVTFIRYCKE IRQGLWVVVD
VTPTQNPTLL PYGCSKRLPS GLIIDDLSNG YSQVTWIEQA EYNESHIHQL YQPLIGYGIG
LGAKRWLATL QRHCESLSTL SSTNLTEISP GLSAKGATEI VKLAQRMTLN YYRGITSPSV
DKWQKIQVEN VAQNMSFMIR KNVNEPGELT GIVLSASTSV WLPVNQHTLF AFISHLSFRH
EWDILTNDTT MEETIRIQKA KRHGNIISLL KIVNNGMLVL QEIWNDASGA MVVYAPVETN
SIELVKRGEN SDSVKFLPSG FSIVPDGVNG SYHRGNTGGG CLLTFGLQIL VGINPTAALI
QGTVKSVETL MAHTIVKIKS ALDLQT
