RFI2_ARATH
ID RFI2_ARATH Reviewed; 358 AA.
AC O82239; A0A1P8B018;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=E3 ubiquitin-protein ligase RFI2 {ECO:0000303|PubMed:16384903};
DE EC=2.3.2.27 {ECO:0000269|PubMed:15644464};
DE AltName: Full=Protein RED AND FAR-RED INSENSITIVE 2 {ECO:0000303|PubMed:16384903};
GN Name=RFI2 {ECO:0000303|PubMed:16384903};
GN OrderedLocusNames=At2g47700 {ECO:0000312|Araport:AT2G47700};
GN ORFNames=F17A22.9 {ECO:0000312|EMBL:AAC63626.2};
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 [MRNA], CATALYTIC ACTIVITY, AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=15644464; DOI=10.1104/pp.104.052423;
RA Stone S.L., Hauksdottir H., Troy A., Herschleb J., Kraft E., Callis J.;
RT "Functional analysis of the RING-type ubiquitin ligase family of
RT Arabidopsis.";
RL Plant Physiol. 137:13-30(2005).
RN [2]
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 [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 FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY CIRCADIAN RHYTHM.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=16709197; DOI=10.1111/j.1365-313x.2006.02740.x;
RA Chen M., Ni M.;
RT "RFI2, a RING-domain zinc finger protein, negatively regulates CONSTANS
RT expression and photoperiodic flowering.";
RL Plant J. 46:823-833(2006).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=16384903; DOI=10.1104/pp.105.073163;
RA Chen M., Ni M.;
RT "RED AND FAR-RED INSENSITIVE 2, a RING-domain zinc finger protein, mediates
RT phytochrome-controlled seedling deetiolation responses.";
RL Plant Physiol. 140:457-465(2006).
CC -!- FUNCTION: Mediates phytochrome (phyA and phyB)-controlled seedling
CC deetiolation responses such as hypocotyl elongation in response to red
CC and far-red light (PubMed:16709197, PubMed:16384903). Required for
CC light-induced expression of LHCB3 and CHALCONE SYNTHASE (CHS)
CC (PubMed:16384903). Regulates negatively CONSTANS (CO) and FLOWERING
CC LOCUS T (FT) expression and photoperiodic flowering (PubMed:16709197).
CC {ECO:0000269|PubMed:16384903, ECO:0000269|PubMed:16709197}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:15644464};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000305|PubMed:15644464}.
CC -!- INTERACTION:
CC O82239; A9LNK9: CPSF30; NbExp=3; IntAct=EBI-4425094, EBI-962511;
CC O82239; Q94ID6: ERF12; NbExp=3; IntAct=EBI-4425094, EBI-4446727;
CC O82239; Q9MAI5: ERF8; NbExp=3; IntAct=EBI-4425094, EBI-2000137;
CC O82239; Q84WI0: GIS; NbExp=3; IntAct=EBI-4425094, EBI-15195983;
CC O82239; Q9C5X0: IAA34; NbExp=3; IntAct=EBI-4425094, EBI-3946459;
CC O82239; Q9LXU1: PIM1; NbExp=3; IntAct=EBI-4425094, EBI-15193025;
CC O82239; Q9S7W5: TCP13; NbExp=3; IntAct=EBI-4425094, EBI-4424877;
CC O82239; Q9C9L2: TCP15; NbExp=3; IntAct=EBI-4425094, EBI-4426144;
CC O82239; Q9LVG2: TOE2; NbExp=3; IntAct=EBI-4425094, EBI-4424568;
CC O82239; Q39262: ZFP3; NbExp=3; IntAct=EBI-4425094, EBI-15200178;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16384903}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O82239-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O82239-2; Sequence=VSP_058959, VSP_058960;
CC -!- INDUCTION: Levels are following a circadian rhythm oscillated under
CC day/night cycles with higher levels during the night.
CC {ECO:0000269|PubMed:16709197}.
CC -!- DISRUPTION PHENOTYPE: Photomorphogenic mutant insensitive to red and
CC far-red light leading to long hypocotyls. Flowers early particularly
CC under long days (PubMed:16709197, PubMed:16384903). Also impaired in
CC phytochrome-mediated end-of-day far-red light response, cotyledon
CC expansion, far-red light block of greening, and light-induced
CC expression of LHCB3 and CHALCONE SYNTHASE (CHS) (PubMed:16384903).
CC Enhanced expression of CONSTANS (CO) and FLOWERING LOCUS T (FT) under
CC long days and short days (PubMed:16709197).
CC {ECO:0000269|PubMed:16384903, ECO:0000269|PubMed:16709197}.
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; DQ086859; AAZ14075.1; -; mRNA.
DR EMBL; AC005309; AAC63626.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC10878.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62259.1; -; Genomic_DNA.
DR EMBL; BT002412; AAO00772.1; -; mRNA.
DR EMBL; BT008845; AAP68284.1; -; mRNA.
DR PIR; E84918; E84918.
DR RefSeq; NP_001324431.1; NM_001337272.1. [O82239-2]
DR RefSeq; NP_850478.1; NM_180147.3. [O82239-1]
DR AlphaFoldDB; O82239; -.
DR IntAct; O82239; 52.
DR STRING; 3702.AT2G47700.1; -.
DR PaxDb; O82239; -.
DR PRIDE; O82239; -.
DR EnsemblPlants; AT2G47700.1; AT2G47700.1; AT2G47700. [O82239-1]
DR EnsemblPlants; AT2G47700.2; AT2G47700.2; AT2G47700. [O82239-2]
DR GeneID; 819383; -.
DR Gramene; AT2G47700.1; AT2G47700.1; AT2G47700. [O82239-1]
DR Gramene; AT2G47700.2; AT2G47700.2; AT2G47700. [O82239-2]
DR KEGG; ath:AT2G47700; -.
DR Araport; AT2G47700; -.
DR TAIR; locus:2043438; AT2G47700.
DR eggNOG; ENOG502SJ7I; Eukaryota.
DR HOGENOM; CLU_037685_0_0_1; -.
DR InParanoid; O82239; -.
DR OMA; QHHANGP; -.
DR OrthoDB; 1199074at2759; -.
DR PhylomeDB; O82239; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:O82239; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O82239; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0009585; P:red, far-red light phototransduction; IEA:UniProtKB-KW.
DR GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
DR GO; GO:2000028; P:regulation of photoperiodism, flowering; IMP:UniProtKB.
DR GO; GO:0090227; P:regulation of red or far-red light signaling pathway; IMP:UniProtKB.
DR GO; GO:0010218; P:response to far red light; IMP:UniProtKB.
DR GO; GO:0010114; P:response to red light; IMP:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR044274; RFI2.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46798; PTHR46798; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Biological rhythms; Flowering; Metal-binding;
KW Nucleus; Phytochrome signaling pathway; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..358
FT /note="E3 ubiquitin-protein ligase RFI2"
FT /id="PRO_0000440167"
FT ZN_FING 38..83
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..312
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 248..272
FT /note="SNQRSSPAINSYQGSSTQMREQHHA -> LASQTPYCSQLLAECFTIFFWNW
FT AL (in isoform 2)"
FT /id="VSP_058959"
FT VAR_SEQ 273..358
FT /note="Missing (in isoform 2)"
FT /id="VSP_058960"
SQ SEQUENCE 358 AA; 39937 MW; 2F9689C68B752F79 CRC64;
MAGAKDSGCD DDLRIAGGCD PGKRGNPEDS SSPVEVSCSI CLESVLDDGT RSKAKLQCGH
QFHLDCIGSA FNMKGAMQCP NCRNVEKGQW LYANGSTRPF PEFSMEDWIP EEDLYGLSYP
EMQYRVHWCP FGELSQAAAS FEELEPATTT YHTEFHGHHA AAVNHSYLAY VGPGPAATPR
TSDNNSTDDH PWNSHSNDHF HQLPVAPQYH HHSPSFSLPA AHVVDGEVDS SAARGLPYAH
PFLFSHRSNQ RSSPAINSYQ GSSTQMREQH HAYNHQRQQH HANGPTLASP LISMTRRGLP
PPPPPPPMPD QNVGFFIYPG GHHEPETDQI HAWERDWFPH FPVPSNHRTI PSLWHRHF
