NFXL2_ARATH
ID NFXL2_ARATH Reviewed; 883 AA.
AC Q9FFK8; F4K0S4;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=NF-X1-type zinc finger protein NFXL2;
DE Short=AtNFXL2;
DE EC=2.3.2.-;
DE AltName: Full=Protein EARLY BIRD;
GN Name=NFXL2; Synonyms=EBI; OrderedLocusNames=At5g05660; ORFNames=MJJ3.6;
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] (ISOFORMS NFXL2-100; NFXL2-97 AND NFXL2-78),
RP FUNCTION, ALTERNATIVE SPLICING, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION,
RP INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=22073231; DOI=10.1371/journal.pone.0026982;
RA Lisso J., Schroeder F., Fisahn J., Muessig C.;
RT "NFX1-LIKE2 (NFXL2) suppresses abscisic acid accumulation and stomatal
RT closure in Arabidopsis thaliana.";
RL PLoS ONE 6:E26982-E26982(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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] OF 3-883 (ISOFORM NFXL2-97).
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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND ALTERNATIVE SPLICING.
RX PubMed=16905136; DOI=10.1016/j.febslet.2006.07.079;
RA Lisso J., Altmann T., Muessig C.;
RT "The AtNFXL1 gene encodes a NF-X1 type zinc finger protein required for
RT growth under salt stress.";
RL FEBS Lett. 580:4851-4856(2006).
RN [6]
RP REVIEW.
RX PubMed=20522174; DOI=10.1111/j.1438-8677.2009.00303.x;
RA Muessig C., Schroeder F., Usadel B., Lisso J.;
RT "Structure and putative function of NFX1-like proteins in plants.";
RL Plant Biol. 12:381-394(2010).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF VAL-354.
RC STRAIN=cv. Wassilewskija;
RX PubMed=21429190; DOI=10.1186/gb-2011-12-3-r28;
RA Ashelford K., Eriksson M.E., Allen C.M., D'Amore R., Johansson M.,
RA Gould P., Kay S., Millar A.J., Hall N., Hall A.;
RT "Full genome re-sequencing reveals a novel circadian clock mutation in
RT Arabidopsis.";
RL Genome Biol. 12:RESEARCH28.1-RESEARCH28.12(2011).
RN [8]
RP FUNCTION, INDUCTION, AND INTERACTION WITH ADO1/ZTL.
RX PubMed=21300918; DOI=10.1104/pp.110.167155;
RA Johansson M., McWatters H.G., Bako L., Takata N., Gyula P., Hall A.,
RA Somers D.E., Millar A.J., Eriksson M.E.;
RT "Partners in time: EARLY BIRD associates with ZEITLUPE and regulates the
RT speed of the Arabidopsis clock.";
RL Plant Physiol. 155:2108-2122(2011).
RN [9]
RP FUNCTION.
RX PubMed=22516817; DOI=10.4161/psb.19838;
RA Lisso J., Schroeder F., Schippers J.H., Muessig C.;
RT "NFXL2 modifies cuticle properties in Arabidopsis.";
RL Plant Signal. Behav. 7:551-555(2012).
CC -!- FUNCTION: Probable transcriptional regulator. May mediate E2- or E3-
CC dependent ubiquitination. Required to gate light sensitivity during the
CC night. Regulates the speed of the clock by acting in the feedback loop
CC between CCA1, LHY and APRR1/TOC1. Promotes the expression of CCA1 at
CC night but not by days. This activational effect is enhanced by
CC interaction with ADO1/ZTL. Association with ADO1/ZTL is not leading to
CC the degradation of NFXL2. Confers sensitivity to osmotic stress such as
CC high salinity. Prevents H(2)O(2) production and abscisic acid
CC accumulation. Part of a regulatory network that integrates the
CC biosynthesis and action of abscisic acid, reactive oxygen species and
CC cuticle components. {ECO:0000269|PubMed:16905136,
CC ECO:0000269|PubMed:21300918, ECO:0000269|PubMed:21429190,
CC ECO:0000269|PubMed:22073231, ECO:0000269|PubMed:22516817}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with ADO1/ZTL. {ECO:0000269|PubMed:21300918}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22073231}. Membrane
CC {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=NFXL2-97;
CC IsoId=Q9FFK8-1; Sequence=Displayed;
CC Name=NFXL2-100;
CC IsoId=Q9FFK8-2; Sequence=VSP_046012;
CC Name=NFXL2-78;
CC IsoId=Q9FFK8-3; Sequence=VSP_046010, VSP_046011;
CC -!- TISSUE SPECIFICITY: Constitutively expressed in mesophyll and guard
CC cells. {ECO:0000269|PubMed:22073231}.
CC -!- INDUCTION: Circadian-regulation with a peak of expression at or before
CC dawn. Not regulated by biotic and abiotic stresses, by light and
CC nutrient conditions or upon treatment with elicitors, chemicals,
CC abscisic acid or phytohormones. {ECO:0000269|PubMed:21300918,
CC ECO:0000269|PubMed:22073231}.
CC -!- DOMAIN: The RING-type zinc finger domain interacts with an ubiquitin-
CC conjugating enzyme (E2) and facilitates ubiquitination. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No obvious morphological alterations. Enhanced
CC growth and survival under water or salt stress. Enhanced H(2)O(2)
CC production. Elevated abscisic acid levels and reduced stomatal
CC aperture. {ECO:0000269|PubMed:16905136, ECO:0000269|PubMed:22073231}.
CC -!- SIMILARITY: Belongs to the NFX1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK228690; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB09660.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB005237; BAB09660.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED90905.2; -; Genomic_DNA.
DR EMBL; AK228690; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_196185.4; NM_120648.6. [Q9FFK8-1]
DR AlphaFoldDB; Q9FFK8; -.
DR BioGRID; 15729; 2.
DR STRING; 3702.AT5G05660.1; -.
DR PaxDb; Q9FFK8; -.
DR PRIDE; Q9FFK8; -.
DR ProteomicsDB; 249434; -. [Q9FFK8-1]
DR EnsemblPlants; AT5G05660.1; AT5G05660.1; AT5G05660. [Q9FFK8-1]
DR GeneID; 830450; -.
DR Gramene; AT5G05660.1; AT5G05660.1; AT5G05660. [Q9FFK8-1]
DR KEGG; ath:AT5G05660; -.
DR Araport; AT5G05660; -.
DR eggNOG; KOG1952; Eukaryota.
DR HOGENOM; CLU_014224_0_0_1; -.
DR InParanoid; Q9FFK8; -.
DR OMA; PCPPCAQ; -.
DR OrthoDB; 299100at2759; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9FFK8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFK8; baseline and differential.
DR Genevisible; Q9FFK8; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0010310; P:regulation of hydrogen peroxide metabolic process; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0009651; P:response to salt stress; IMP:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR InterPro; IPR034078; NFX1_fam.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR000967; Znf_NFX1.
DR PANTHER; PTHR12360; PTHR12360; 1.
DR Pfam; PF01422; zf-NF-X1; 11.
DR SMART; SM00438; ZnF_NFX; 11.
DR PROSITE; PS00197; 2FE2S_FER_1; 2.
DR PROSITE; PS01359; ZF_PHD_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Biological rhythms; Membrane; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..883
FT /note="NF-X1-type zinc finger protein NFXL2"
FT /id="PRO_0000396836"
FT TRANSMEM 841..863
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 87..152
FT /note="RING-type; degenerate"
FT ZN_FING 198..216
FT /note="NF-X1-type 1"
FT ZN_FING 250..269
FT /note="NF-X1-type 2"
FT ZN_FING 303..322
FT /note="NF-X1-type 3"
FT ZN_FING 357..377
FT /note="NF-X1-type 4"
FT ZN_FING 410..429
FT /note="NF-X1-type 5"
FT ZN_FING 437..456
FT /note="NF-X1-type 6"
FT ZN_FING 494..515
FT /note="NF-X1-type 7"
FT ZN_FING 523..568
FT /note="NF-X1-type 8"
FT ZN_FING 605..636
FT /note="NF-X1-type 9"
FT ZN_FING 646..664
FT /note="NF-X1-type 10"
FT ZN_FING 709..738
FT /note="NF-X1-type 11"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 698..714
FT /note="CRGPCHRKLPNCTHLCP -> SLVIPTVRANYRWLNRC (in isoform
FT NFXL2-78)"
FT /evidence="ECO:0000303|PubMed:22073231"
FT /id="VSP_046010"
FT VAR_SEQ 715..883
FT /note="Missing (in isoform NFXL2-78)"
FT /evidence="ECO:0000303|PubMed:22073231"
FT /id="VSP_046011"
FT VAR_SEQ 730
FT /note="K -> KKVSICQFISIWDAVSVTSEILLVSILSWI (in isoform
FT NFXL2-100)"
FT /evidence="ECO:0000303|PubMed:22073231"
FT /id="VSP_046012"
FT MUTAGEN 354
FT /note="V->I: In ebi-1; altered circadian clock function."
FT /evidence="ECO:0000269|PubMed:21429190"
FT CONFLICT 270
FT /note="R -> H (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="E -> G (in Ref. 4; AK228690)"
FT /evidence="ECO:0000305"
FT CONFLICT 552
FT /note="H -> N (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 660
FT /note="P -> L (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 883 AA; 99229 MW; 65CA28E09D161CB7 CRC64;
MTNMAGTATT EFRWKSPPQP PSQEQPISDS DSDSGSDSEN HQHRHNDLSN SIFEAYLDCH
SSSSPSSIDL AKIQSFLASS SSGAVSCLIC LERIKRTDPT WSCTSSCFAV FHLFCIQSWA
RQCLDLQAAR AVTRPSSNPT EPEAVWNCPK CRSSYQKSKI PRRYLCYCGK EEDPPADNPW
ILPHSCGEVC ERPLSNNCGH CCLLLCHPGP CASCPKLVKA KCFCGGVEDV RRCGHKQFSC
GDVCERVLDC NIHNCREICH DGECPPCRER AVYKCSCGKV KEEKDCCERV FRCEASCENM
LNCGKHVCER GCHAGECGLC PYQGKRSCPC GKRFYQGLSC DVVAPLCGGT CDKVLGCGYH
RCPERCHRGP CLETCRIVVT KSCRCGVTKK QVPCHQELAC ERKCQRVRDC ARHACRRRCC
DGECPPCSEI CGKKLRCRNH KCQSPCHQGP CAPCPIMVTI SCACGETHFE VPCGTETNQK
PPRCRKLCHI TPLCRHGQNQ KPHKCHYGAC PPCRLLCDEE YPCGHKCKLR CHGPRPPPNR
EFILKPTKKM LHIQAESTPG SPCPRCPEPV WRPCVGHHLA AEKRMICSDR TQFACDNLCG
NPLPCGNHYC SYFCHALDIR SSSLDKRSES CEKCDLRCQK ERTPRCQHPC PRRCHPEDCP
PCKTLVKRSC HCGAMVHAFE CIYYNTMSEK DQMKARSCRG PCHRKLPNCT HLCPEICHPG
QCPLPEKCGK KVVVRCKCLT LKKEWVCQDV QAAHRATGSD PKEVPKNQFG VGLLPCDSNC
KSKLQVAESV LTQRNVKEIE EKEEPSGKNA SKRRKRRGRG QDIQETTRLQ KLAVTTKRIL
MVVMLVAMLA AVSYYGYKGL LWLSDWMNEV EEQRQKSRRY PRI
