NFXL1_ARATH
ID NFXL1_ARATH Reviewed; 1188 AA.
AC Q9SY59;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=NF-X1-type zinc finger protein NFXL1;
DE Short=AtNFXL1;
DE EC=2.3.2.-;
GN Name=NFXL1; OrderedLocusNames=At1g10170; ORFNames=F14N23.5;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND INDUCTION BY OSMOTIC STRESS AND BRASSINOSTEROIDS.
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND INDUCTION BY
RP TRICHOTHECENES; BIOTIC AND ABIOTIC STRESSES.
RX PubMed=18069941; DOI=10.1111/j.1365-313x.2007.03353.x;
RA Asano T., Masuda D., Yasuda M., Nakashita H., Kudo T., Kimura M.,
RA Yamaguchi K., Nishiuchi T.;
RT "AtNFXL1, an Arabidopsis homologue of the human transcription factor NF-X1,
RT functions as a negative regulator of the trichothecene phytotoxin-induced
RT defense response.";
RL Plant J. 53:450-464(2008).
RN [5]
RP FUNCTION, INDUCTION BY TRICHOTHECENES, AND DISRUPTION PHENOTYPE.
RX PubMed=19704430; DOI=10.4161/psb.6291;
RA Asano T., Yasuda M., Nakashita H., Kimura M., Yamaguchi K., Nishiuchi T.;
RT "The AtNFXL1 gene functions as a signaling component of the type A
RT trichothecene-dependent response.";
RL Plant Signal. Behav. 3:991-992(2008).
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).
CC -!- FUNCTION: Mediates E2-dependent ubiquitination (By similarity). Confers
CC resistance to osmotic stress such as high salinity. Promotes H(2)O(2)
CC production. Negative regulator of some defense-related genes via an
CC salicylic acid (SA)-dependent signaling pathway. Confers susceptibility
CC to the compatible phytopathogen Pseudomonas syringae pv. tomato strain
CC DC3000 (Pst DC3000). Mediates resistance to type A trichothecenes
CC (phytotoxins produced by phytopathogenic fungi). {ECO:0000250,
CC ECO:0000269|PubMed:16905136, ECO:0000269|PubMed:18069941,
CC ECO:0000269|PubMed:19704430}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- INTERACTION:
CC Q9SY59; Q9ZW36: At2g29580; NbExp=3; IntAct=EBI-15201298, EBI-15195245;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16905136,
CC ECO:0000269|PubMed:18069941}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, stems, leaves, buds,
CC flowers and siliques. {ECO:0000269|PubMed:16905136}.
CC -!- INDUCTION: By brassinosteroids, osmotic stress and high salinity.
CC Accumulates in response to SA, ethylene, methyl jasmonate (MeJA),
CC flagellin (e.g. flg22), and type A trichothecenes such as T-2 toxin and
CC diacetoxyscirpenol (DAS), but not in response to type B trichothecenes
CC such as deoxynivalenol (DON). {ECO:0000269|PubMed:16905136,
CC ECO:0000269|PubMed:18069941, ECO:0000269|PubMed:19704430}.
CC -!- DOMAIN: The RING-type zinc finger domain interacts with an ubiquitin-
CC conjugating enzyme (E2) and facilitates ubiquitination. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Impaired growth and survival under salt stress.
CC Reduced H(2)O(2) production. Hypersensitivity to T-2 toxin and DAS (but
CC not to DON), accompanied by enhanced SA accumulation and several plant
CC defense gene induction. Less susceptible to Pst DC3000.
CC {ECO:0000269|PubMed:16905136, ECO:0000269|PubMed:18069941,
CC ECO:0000269|PubMed:19704430}.
CC -!- SIMILARITY: Belongs to the NFX1 family. {ECO:0000305}.
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DR EMBL; AC005489; AAD32867.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28549.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60817.1; -; Genomic_DNA.
DR PIR; D86236; D86236.
DR RefSeq; NP_001318968.1; NM_001331888.1.
DR RefSeq; NP_172488.1; NM_100891.3.
DR AlphaFoldDB; Q9SY59; -.
DR BioGRID; 22795; 5.
DR IntAct; Q9SY59; 5.
DR STRING; 3702.AT1G10170.1; -.
DR PaxDb; Q9SY59; -.
DR PRIDE; Q9SY59; -.
DR ProteomicsDB; 249433; -.
DR EnsemblPlants; AT1G10170.1; AT1G10170.1; AT1G10170.
DR EnsemblPlants; AT1G10170.3; AT1G10170.3; AT1G10170.
DR GeneID; 837555; -.
DR Gramene; AT1G10170.1; AT1G10170.1; AT1G10170.
DR Gramene; AT1G10170.3; AT1G10170.3; AT1G10170.
DR KEGG; ath:AT1G10170; -.
DR Araport; AT1G10170; -.
DR TAIR; locus:2012753; AT1G10170.
DR eggNOG; KOG1952; Eukaryota.
DR HOGENOM; CLU_005714_4_0_1; -.
DR InParanoid; Q9SY59; -.
DR OMA; WCEKEVD; -.
DR PhylomeDB; Q9SY59; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9SY59; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SY59; baseline and differential.
DR Genevisible; Q9SY59; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
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:0042742; P:defense response to bacterium; IMP:TAIR.
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:0009642; P:response to light intensity; IMP:TAIR.
DR GO; GO:0010188; P:response to microbial phytotoxin; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0009697; P:salicylic acid biosynthetic process; IMP:TAIR.
DR InterPro; IPR034078; NFX1_fam.
DR InterPro; IPR000967; Znf_NFX1.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR12360; PTHR12360; 2.
DR Pfam; PF01422; zf-NF-X1; 9.
DR SMART; SM00438; ZnF_NFX; 9.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Plant defense; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1188
FT /note="NF-X1-type zinc finger protein NFXL1"
FT /id="PRO_0000396835"
FT DOMAIN 894..963
FT /note="R3H"
FT ZN_FING 223..279
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 335..353
FT /note="NF-X1-type 1"
FT ZN_FING 390..409
FT /note="NF-X1-type 2"
FT ZN_FING 454..473
FT /note="NF-X1-type 3"
FT ZN_FING 513..532
FT /note="NF-X1-type 4"
FT ZN_FING 572..607
FT /note="NF-X1-type 5"
FT ZN_FING 611..630
FT /note="NF-X1-type 6"
FT ZN_FING 668..686
FT /note="NF-X1-type 7"
FT ZN_FING 721..751
FT /note="NF-X1-type 8"
FT ZN_FING 760..781
FT /note="NF-X1-type 9"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1100..1188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1109..1171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1188 AA; 130716 MW; 906B703583E8FFCA CRC64;
MSFQVRRDRS DDRSHRFNHQ QTWIPRNSST SSVVVNEPLL PPNTDRNSET LDAGSASRPV
YLQRQHNASG PPSYNHHQRS SNIGPPPPNQ HRRYNAPDNQ HQRSDNIGPP QPNQHRRYNA
PDNQHQRSDN SGPPQPYRHR RNNAPENQHQ RSDNIGPPPP NRQRRNNASG TLPDNRQRVA
SRTRPVNQGK RVAKEENVVL TDPNLPQLVQ ELQEKLVKSS IECMICYDKV GRSANIWSCS
SCYSIFHINC IKRWARAPTS VDLLAEKNQG DNWRCPGCQS VQLTSSKEIS YRCFCGKRRD
PPSDPYLTPH SCGEPCGKPL EKEFAPAETT EEDLCPHVCV LQCHPGPCPP CKAFAPPRSC
PCGKKMVTTR CSERRSDLVC GQRCDKLLSC GRHQCERTCH VGPCDPCQVL VNATCFCKKK
VETVICGDMN VKGELKAEDG VYSCSFNCGK PLGCGNHFCS EVCHPGPCGD CDLLPSRVKT
CYCGNTRLEE QIRQSCLDPI PSCSNVCRKL LPCRLHTCNE MCHAGDCPPC LVQVNQKCRC
GSTSRAVECY ITTSSEAEKF VCAKPCGRKK NCGRHRCSER CCPLLNGKKN DLSGDWDPHV
CQIPCQKKLR CGQHSCESLC HSGHCPPCLE MIFTDLTCAC GRTSIPPPLS CGTPVPSCQL
PCPIPQPCGH SDTHGCHFGD CPPCSTPVEK KCVGGHVVLR NIPCGLKDIR CTKICGKTRR
CGMHACARTC HPEPCDSFNE SEAGMRVTCR QKCGAPRTDC RHTCAALCHP SAPCPDLRCE
FSVTITCSCG RITATVPCDA GGRSANGSNV YCAAYDEASV LQKLPAPLQP VESSGNRIPL
GQRKLSCDDE CAKLERKRVL QDAFDITPPN LEALHFSENS AMTEIISDLY RRDPKWVLAV
EERCKFLVLG KARGSTSALK VHIFCPMQKD KRDTVRLIAE RWKLGVSNAG WEPKRFTVVH
VTAKSKPPTR IIGARGGAIS IGGPHPPFYD SLVDMDPGLV VSFLDLPREA NISALVLRFG
GECELVWLND KNALAVFHDH ARAATAMRRL EHGSVYHGAV VVQSGGQSPS LNNVWGKLPG
SSAWDVDKGN PWRRAVIQES DDSWGAEDSP IGGSSTDAQA SALRSAKSNS PIVTSVNRWS
VLEPKKASTS TLEPIAQIEE SSSSKTTGKQ PVEGSGEEVV DDWEKVCE
