NIFU3_ARATH
ID NIFU3_ARATH Reviewed; 236 AA.
AC Q84RQ7; Q0WN92; Q8LCL7; Q9SZG6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=NifU-like protein 3, chloroplastic;
DE Short=AtCNfu3;
DE Short=AtCnfU-IVa;
DE Flags: Precursor;
GN Name=NIFU3; Synonyms=CNFU3, NFU3; OrderedLocusNames=At4g25910;
GN ORFNames=F20B18.20;
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] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=12553879; DOI=10.1042/bj20021946;
RA Leon S., Touraine B., Ribot C., Briat J.-F., Lobreaux S.;
RT "Iron-sulphur cluster assembly in plants: distinct NFU proteins in
RT mitochondria and plastids from Arabidopsis thaliana.";
RL Biochem. J. 371:823-830(2003).
RN [2]
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 [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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Molecular scaffold for [Fe-S] cluster assembly of
CC chloroplastic iron-sulfur proteins. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:12553879}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q84RQ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q84RQ7-2; Sequence=VSP_021276;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in leaves and floral
CC stalks. {ECO:0000269|PubMed:12553879}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NifU family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB39656.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB79446.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ512935; CAD55560.1; -; mRNA.
DR EMBL; AL049483; CAB39656.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL161564; CAB79446.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002687; AEE85132.1; -; Genomic_DNA.
DR EMBL; BT024624; ABD43022.1; -; mRNA.
DR EMBL; AK229555; BAF01408.1; -; mRNA.
DR EMBL; AY086527; AAM63593.1; -; mRNA.
DR PIR; T04246; T04246.
DR RefSeq; NP_567735.1; NM_118724.4. [Q84RQ7-1]
DR AlphaFoldDB; Q84RQ7; -.
DR SMR; Q84RQ7; -.
DR BioGRID; 13984; 1.
DR STRING; 3702.AT4G25910.1; -.
DR PaxDb; Q84RQ7; -.
DR PRIDE; Q84RQ7; -.
DR ProteomicsDB; 248933; -. [Q84RQ7-1]
DR EnsemblPlants; AT4G25910.1; AT4G25910.1; AT4G25910. [Q84RQ7-1]
DR GeneID; 828697; -.
DR Gramene; AT4G25910.1; AT4G25910.1; AT4G25910. [Q84RQ7-1]
DR KEGG; ath:AT4G25910; -.
DR Araport; AT4G25910; -.
DR TAIR; locus:2120745; AT4G25910.
DR eggNOG; KOG2358; Eukaryota.
DR HOGENOM; CLU_080894_2_1_1; -.
DR InParanoid; Q84RQ7; -.
DR OMA; GYVVKIR; -.
DR PhylomeDB; Q84RQ7; -.
DR PRO; PR:Q84RQ7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q84RQ7; baseline and differential.
DR Genevisible; Q84RQ7; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IBA:GO_Central.
DR GO; GO:0060090; F:molecular adaptor activity; IDA:TAIR.
DR GO; GO:0005198; F:structural molecule activity; TAS:TAIR.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
DR GO; GO:0048564; P:photosystem I assembly; IMP:TAIR.
DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IBA:GO_Central.
DR Gene3D; 3.30.300.130; -; 2.
DR InterPro; IPR034904; FSCA_dom_sf.
DR InterPro; IPR001075; NIF_FeS_clus_asmbl_NifU_C.
DR Pfam; PF01106; NifU; 2.
DR SUPFAM; SSF117916; SSF117916; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Chloroplast; Disulfide bond; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..99
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 100..236
FT /note="NifU-like protein 3, chloroplastic"
FT /id="PRO_0000255237"
FT DISULFID 125
FT /note="Interchain (with C-128)"
FT /evidence="ECO:0000250"
FT DISULFID 128
FT /note="Interchain (with C-125)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..81
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_021276"
FT CONFLICT 27..29
FT /note="RSS -> CSA (in Ref. 6; AAM63593)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 236 AA; 25657 MW; 7E25AFBBBB889239 CRC64;
MGSVSGQTRI TTMNLSLSTA EKNPNFRSSL LNSKNAISDT LGVSSKCSTF LRGQFQRIHF
SWLQHTRPLR KRTVFGHVSC VMPLTEENVE RVLDEVRPSL MADGGNVALH EIDGLVVVLK
LQGACGSCPS SSMTLKMGIE SRLRDKIPEI MSVEQFLESE TGGLELNDEN IEKVLSELRP
YLSGTGGGGL ELVEIDGYVV KVRLTGPAAG VMTVRVALTQ KLRETIPSIG AVQLLE
