NAR1_ARATH
ID NAR1_ARATH Reviewed; 474 AA.
AC Q94CL6; Q8GXY2;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Protein NAR1 {ECO:0000303|PubMed:23734982};
DE AltName: Full=Nuclear architecture related 1 {ECO:0000303|PubMed:23734982};
DE AltName: Full=Protein GROWTH AT DIFFERENT OXYGEN LEVELS INFLUENCES MORPHOGENESIS {ECO:0000303|PubMed:18329103};
DE AltName: Full=[FeFe]-hydrogenase-like protein GOLLUM {ECO:0000303|PubMed:18329103};
GN Name=NAR1 {ECO:0000303|PubMed:23734982};
GN Synonyms=GOLLUM {ECO:0000303|PubMed:18329103};
GN OrderedLocusNames=At4g16440 {ECO:0000312|Araport:AT4G16440};
GN ORFNames=dl4245c {ECO:0000312|EMBL:CAB10420.1},
GN FCAALL.367 {ECO:0000312|EMBL:CAB78686.1};
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 {ECO:0000312|EMBL:CAC44620.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Mondy S.;
RT "T-DNA tagging of the Narf like gene in M. truncatula.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Ratet P.;
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 256-474.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 272-474.
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 [8]
RP IDENTIFICATION, AND REVIEW.
RX PubMed=18493040; DOI=10.1534/genetics.107.086033;
RA Godman J., Balk J.;
RT "Genome analysis of Chlamydomonas reinhardtii reveals the existence of
RT multiple, compartmentalized iron-sulfur protein assembly machineries of
RT different evolutionary origins.";
RL Genetics 179:59-68(2008).
RN [9]
RP MUTAGENESIS OF CYS-61; CYS-64; CYS-390 AND CYS-394.
RX PubMed=18329103; DOI=10.1016/j.jinorgbio.2008.01.027;
RA Cavazza C., Martin L., Mondy S., Gaillard J., Ratet P.,
RA Fontecilla-Camps J.C.;
RT "The possible role of an [FeFe]-hydrogenase-like protein in the plant
RT responses to changing atmospheric oxygen levels.";
RL J. Inorg. Biochem. 102:1359-1365(2008).
RN [10]
RP FUNCTION, INTERACTION WITH CIA1, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=23104832; DOI=10.1105/tpc.112.102608;
RA Luo D., Bernard D.G., Balk J., Hai H., Cui X.;
RT "The DUF59 family gene AE7 acts in the cytosolic iron-sulfur cluster
RT assembly pathway to maintain nuclear genome integrity in Arabidopsis.";
RL Plant Cell 24:4135-4148(2012).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=23734982; DOI=10.1111/nph.12350;
RA Nakamura M., Buzas D.M., Kato A., Fujita M., Kurata N., Kinoshita T.;
RT "The role of Arabidopsis thaliana NAR1, a cytosolic iron-sulfur cluster
RT assembly component, in gametophytic gene expression and oxidative stress
RT responses in vegetative tissue.";
RL New Phytol. 199:925-935(2013).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, 3D-STRUCTURE MODELING,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=23639116; DOI=10.1111/pce.12128;
RA Mondy S., Lenglet A., Cosson V., Pelletier S., Pateyron S., Gilard F.,
RA Scholte M., Brocard L., Couzigou J.M., Tcherkez G., Pean M., Ratet P.;
RT "GOLLUM [FeFe]-hydrogenase-like proteins are essential for plant
RT development in normoxic conditions and modulate energy metabolism.";
RL Plant Cell Environ. 37:54-69(2014).
CC -!- FUNCTION: Essential component of the cytosolic iron-sulfur (Fe-S)
CC protein assembly (CIA) machinery (PubMed:23104832). Required for the
CC maturation of extramitochondrial Fe/S proteins (By similarity).
CC Required for expression of the imprinted FWA gene, for seed development
CC and is involved in the oxidative stress response in vegetative tissues
CC (PubMed:23734982). Involved in the regulation of cell size, ploidy and
CC cell cycle progression (PubMed:23639116). Required for growth under
CC normoxic conditions and necessary for recovery after hypoxic treatment
CC but its action is reactive oxygen species (ROS) independent
CC (PubMed:23639116). {ECO:0000250|UniProtKB:Q9H6Q4,
CC ECO:0000269|PubMed:23104832, ECO:0000269|PubMed:23639116,
CC ECO:0000269|PubMed:23734982}.
CC -!- SUBUNIT: Part of a complex composed of AE7, CIA1, MMS19 and NAR1.
CC Interacts with CIA1. {ECO:0000269|PubMed:23104832}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23639116}. Cytoplasm
CC {ECO:0000269|PubMed:23639116}.
CC -!- TISSUE SPECIFICITY: Expressed in developing tissues, including shoot
CC apex, young leaves, vascular tissues, root tips, pedicels, carpels and
CC developing seeds. {ECO:0000269|PubMed:23639116,
CC ECO:0000269|PubMed:23734982}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout plant development.
CC {ECO:0000269|PubMed:23734982}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality when homozygous
CC (PubMed:23104832, PubMed:23734982, PubMed:23639116).
CC {ECO:0000269|PubMed:23104832, ECO:0000269|PubMed:23639116,
CC ECO:0000269|PubMed:23734982}.
CC -!- MISCELLANEOUS: Coordinates probably two (Fe-S) clusters with different
CC magnetic properties (PubMed:18329103). Knockdown mutants have a dwarf
CC phenotype, but are indistinguishable from wild type under hypoxic
CC conditions (PubMed:18329103, PubMed:23639116).
CC {ECO:0000269|PubMed:18329103, ECO:0000269|PubMed:23639116}.
CC -!- SIMILARITY: Belongs to the NARF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC42607.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB10420.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g16440 has been split into 3 genes: At4g16440, At4g16442 and At4g16444.; Evidence={ECO:0000305};
CC Sequence=CAB78686.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g16440 has been split into 3 genes: At4g16440, At4g16442 and At4g16444.; Evidence={ECO:0000305};
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DR EMBL; AJ320258; CAC44620.1; -; Genomic_DNA.
DR EMBL; Z97341; CAB10420.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161544; CAB78686.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83748.1; -; Genomic_DNA.
DR EMBL; AK117970; BAC42607.1; ALT_INIT; mRNA.
DR EMBL; BT008777; AAP68216.1; -; mRNA.
DR RefSeq; NP_567496.4; NM_117739.4.
DR AlphaFoldDB; Q94CL6; -.
DR SMR; Q94CL6; -.
DR STRING; 3702.AT4G16440.1; -.
DR PaxDb; Q94CL6; -.
DR PRIDE; Q94CL6; -.
DR ProteomicsDB; 251045; -.
DR EnsemblPlants; AT4G16440.1; AT4G16440.1; AT4G16440.
DR GeneID; 827338; -.
DR Gramene; AT4G16440.1; AT4G16440.1; AT4G16440.
DR KEGG; ath:AT4G16440; -.
DR Araport; AT4G16440; -.
DR TAIR; locus:2130634; AT4G16440.
DR eggNOG; KOG2439; Eukaryota.
DR HOGENOM; CLU_018240_0_0_1; -.
DR InParanoid; Q94CL6; -.
DR OMA; PHEQRAW; -.
DR OrthoDB; 705416at2759; -.
DR PhylomeDB; Q94CL6; -.
DR PRO; PR:Q94CL6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q94CL6; baseline and differential.
DR Genevisible; Q94CL6; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070482; P:response to oxygen levels; IMP:TAIR.
DR InterPro; IPR009016; Fe_hydrogenase.
DR InterPro; IPR004108; Fe_hydrogenase_lsu_C.
DR InterPro; IPR003149; Fe_hydrogenase_ssu.
DR Pfam; PF02906; Fe_hyd_lg_C; 1.
DR Pfam; PF02256; Fe_hyd_SSU; 1.
DR SMART; SM00902; Fe_hyd_SSU; 1.
DR SUPFAM; SSF53920; SSF53920; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..474
FT /note="Protein NAR1"
FT /id="PRO_0000433518"
FT BINDING 24
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 61
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 64
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 67
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 177
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 233
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 390
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 394
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT MUTAGEN 61
FT /note="C->A: No effect on UV-visible spectrum; when
FT associated with A-64."
FT /evidence="ECO:0000269|PubMed:18329103"
FT MUTAGEN 64
FT /note="C->A: No effect on UV-visible spectrum; when
FT associated with A-61."
FT /evidence="ECO:0000269|PubMed:18329103"
FT MUTAGEN 390
FT /note="C->A: Loss of (Fe-S) clusters coordination; when
FT associated with A-394."
FT /evidence="ECO:0000269|PubMed:18329103"
FT MUTAGEN 394
FT /note="C->A: Loss of (Fe-S) clusters coordination; when
FT associated with A-390."
FT /evidence="ECO:0000269|PubMed:18329103"
SQ SEQUENCE 474 AA; 52504 MW; 4CF66FFF17D8CA55 CRC64;
MSEKFSPTLR LGDLNDFIAP SQACVISLKD SKPIVKKSDR PQVVIAPKQQ LEPVKISLKD
CLACSGCITS AETVMLEKQS LDEFLSALSK GKDVVVSVSP QSRASLAVHY DISPLQVFKK
LTTFLKSLGV KAVFDTSCSR DLVLIESCNE FVSRYKQANS DDGENSQSPL PVLSSACPGW
ICYAEKQLGS YVLPYVSSVK SPQQAIGAAI KHHLCQALGL RLHEVYHVTV MPCYDKKLEA
ARDDFVFDDG TQDNGDLKLT EVDSVLTTGE IMDLIKLKGV DFKDLEESPL DRVLTNVTEE
GDLYGVAGSS GGYAETIFRH AAKALFGQTI EGPLEFKTLR NSDFREVTLQ LEGKTVLKFA
LCYGFQNLQN IVRRVKTRKC DYQYVEIMAC PAGCLNGGGQ IKPKTGQSQK ELIHSLEATY
MNDTTLNTDP YQNPTAKRLF EEWLKEPGSN EAKKYLHTQY HPVVKSVTSQ LNNW
