FRS2_ARATH
ID FRS2_ARATH Reviewed; 807 AA.
AC Q3EBQ3; Q0WQG7; Q56Y20; Q9ZV55;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Protein FAR1-RELATED SEQUENCE 2;
GN Name=FRS2; OrderedLocusNames=At2g32250; ORFNames=T32F6.23;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 2).
RC STRAIN=cv. Columbia;
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP TISSUE SPECIFICITY, INDUCTION, SUBCELLULAR LOCATION, GENE FAMILY, AND
RP NOMENCLATURE.
RX PubMed=15591448; DOI=10.1104/pp.104.052191;
RA Lin R., Wang H.;
RT "Arabidopsis FHY3/FAR1 gene family and distinct roles of its members in
RT light control of Arabidopsis development.";
RL Plant Physiol. 136:4010-4022(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
CC -!- FUNCTION: Putative transcription activator involved in regulating light
CC control of development.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15591448}. Note=The
CC nuclear localization is independent of the light treatment.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3EBQ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3EBQ3-2; Sequence=VSP_036307;
CC -!- TISSUE SPECIFICITY: Expressed in hypocotyls, rosette and cauline
CC leaves, inflorescences stems, flowers and siliques.
CC {ECO:0000269|PubMed:15591448}.
CC -!- INDUCTION: Up-regulated in hypocotyls by far-red light treatment.
CC {ECO:0000269|PubMed:15591448}.
CC -!- SIMILARITY: Belongs to the FHY3/FAR1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC69951.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC005700; AAC69951.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC08655.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08656.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08657.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08658.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62405.1; -; Genomic_DNA.
DR EMBL; AK228730; BAF00632.1; -; mRNA.
DR EMBL; AK221503; BAD94730.1; -; mRNA.
DR PIR; G84730; G84730.
DR RefSeq; NP_001077991.1; NM_001084522.2. [Q3EBQ3-1]
DR RefSeq; NP_001118431.1; NM_001124959.2. [Q3EBQ3-2]
DR RefSeq; NP_001324564.1; NM_001336380.1. [Q3EBQ3-1]
DR RefSeq; NP_180784.2; NM_128784.4. [Q3EBQ3-1]
DR RefSeq; NP_973580.1; NM_201851.2. [Q3EBQ3-2]
DR AlphaFoldDB; Q3EBQ3; -.
DR BioGRID; 3132; 2.
DR IntAct; Q3EBQ3; 2.
DR STRING; 3702.AT2G32250.1; -.
DR PaxDb; Q3EBQ3; -.
DR PRIDE; Q3EBQ3; -.
DR ProteomicsDB; 230550; -. [Q3EBQ3-1]
DR EnsemblPlants; AT2G32250.1; AT2G32250.1; AT2G32250. [Q3EBQ3-1]
DR EnsemblPlants; AT2G32250.2; AT2G32250.2; AT2G32250. [Q3EBQ3-2]
DR EnsemblPlants; AT2G32250.3; AT2G32250.3; AT2G32250. [Q3EBQ3-1]
DR EnsemblPlants; AT2G32250.4; AT2G32250.4; AT2G32250. [Q3EBQ3-2]
DR EnsemblPlants; AT2G32250.6; AT2G32250.6; AT2G32250. [Q3EBQ3-1]
DR GeneID; 817785; -.
DR Gramene; AT2G32250.1; AT2G32250.1; AT2G32250. [Q3EBQ3-1]
DR Gramene; AT2G32250.2; AT2G32250.2; AT2G32250. [Q3EBQ3-2]
DR Gramene; AT2G32250.3; AT2G32250.3; AT2G32250. [Q3EBQ3-1]
DR Gramene; AT2G32250.4; AT2G32250.4; AT2G32250. [Q3EBQ3-2]
DR Gramene; AT2G32250.6; AT2G32250.6; AT2G32250. [Q3EBQ3-1]
DR KEGG; ath:AT2G32250; -.
DR Araport; AT2G32250; -.
DR TAIR; locus:2062606; AT2G32250.
DR eggNOG; ENOG502QSAM; Eukaryota.
DR HOGENOM; CLU_008459_7_1_1; -.
DR InParanoid; Q3EBQ3; -.
DR OrthoDB; 197084at2759; -.
DR PhylomeDB; Q3EBQ3; -.
DR PRO; PR:Q3EBQ3; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q3EBQ3; baseline and differential.
DR Genevisible; Q3EBQ3; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR004330; FAR1_DNA_bnd_dom.
DR InterPro; IPR031052; FHY3/FAR1.
DR InterPro; IPR018289; MULE_transposase_dom.
DR InterPro; IPR006564; Znf_PMZ.
DR InterPro; IPR007527; Znf_SWIM.
DR PANTHER; PTHR31669; PTHR31669; 1.
DR Pfam; PF03101; FAR1; 1.
DR Pfam; PF10551; MULE; 1.
DR Pfam; PF04434; SWIM; 1.
DR SMART; SM00575; ZnF_PMZ; 1.
DR PROSITE; PS50966; ZF_SWIM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Metal-binding; Nucleus;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..807
FT /note="Protein FAR1-RELATED SEQUENCE 2"
FT /id="PRO_0000363480"
FT DOMAIN 52..138
FT /note="FAR1"
FT DOMAIN 219..315
FT /note="MULE"
FT ZN_FING 499..535
FT /note="SWIM-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00325"
FT REGION 788..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 660..680
FT /evidence="ECO:0000255"
FT VAR_SEQ 761..762
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_036307"
SQ SEQUENCE 807 AA; 91968 MW; C465B9A8100EA71F CRC64;
MDDEDVEIDL LTKSSNVDVF CEASTSGNVA QCATVSELRN GMDFESKEAA YYFYREYARS
VGFGITIKAS RRSKRSGKFI DVKIACSRFG TKREKATAIN PRSCPKTGCK AGLHMKRKED
EKWVIYNFVK EHNHEICPDD FYVSVRGKNK PAGALAIKKG LQLALEEEDL KLLLEHFMEM
QDKQPGFFYA VDFDSDKRVR NVFWLDAKAK HDYCSFSDVV LFDTFYVRNG YRIPFAPFIG
VSHHRQYVLL GCALIGEVSE STYSWLFRTW LKAVGGQAPG VMITDQDKLL SDIVVEVFPD
VRHIFCLWSV LSKISEMLNP FVSQDDGFME SFGNCVASSW TDEHFERRWS NMIGKFELNE
NEWVQLLFRD RKKWVPHYFH GICLAGLSGP ERSGSIASHF DKYMNSEATF KDFFELYMKF
LQYRCDVEAK DDLEYQSKQP TLRSSLAFEK QLSLIYTDAA FKKFQAEVPG VVSCQLQKER
EDGTTAIFRI EDFEERQNFF VALNNELLDA CCSCHLFEYQ GFLCKHAILV LQSADVSRVP
SQYILKRWSK KGNNKEDKND KCATIDNRMA RFDDLCRRFV KLGVVASLSD EACKTALKLL
EETVKHCVSM DNSSKFPSEP DKLMTGGSIG LENEGVLDCA SKVSKKKKIQ KKRKVYCGPE
DATNRSEELR QETEQVSSRA PTFENCYIPQ ANMEEPELGS RATTLGVYYS TQQTNQGFPS
ISSIQNGYYG HPPTIQAMGN LHSIHERMSQ YETQPSMQGA FQGQTGFRGS AIRGCYDIEE
TLHDMTMGSS QFQGSDSSHP SDHRLSN
