NIFU4_ARATH
ID NIFU4_ARATH Reviewed; 283 AA.
AC Q9LIG6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=NifU-like protein 4, mitochondrial;
DE Short=AtNfu-III;
DE Short=AtNfu4;
DE Flags: Precursor;
GN Name=NIFU4; Synonyms=NFU2, NFU4; OrderedLocusNames=At3g20970;
GN ORFNames=MFD22.10;
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], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP 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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
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).
CC -!- FUNCTION: Molecular scaffold for [Fe-S] cluster assembly of
CC mitochondrial iron-sulfur proteins. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12553879}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LIG6-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in roots.
CC {ECO:0000269|PubMed:12553879}.
CC -!- SIMILARITY: Belongs to the NifU family. {ECO:0000305}.
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DR EMBL; AJ512936; CAD55561.1; -; mRNA.
DR EMBL; AP001304; BAB01907.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76448.1; -; Genomic_DNA.
DR EMBL; AF370537; AAK48964.1; -; mRNA.
DR EMBL; AY072509; AAL66924.1; -; mRNA.
DR RefSeq; NP_566673.1; NM_112989.3. [Q9LIG6-1]
DR AlphaFoldDB; Q9LIG6; -.
DR SMR; Q9LIG6; -.
DR BioGRID; 6979; 2.
DR IntAct; Q9LIG6; 2.
DR STRING; 3702.AT3G20970.1; -.
DR iPTMnet; Q9LIG6; -.
DR MetOSite; Q9LIG6; -.
DR PaxDb; Q9LIG6; -.
DR PRIDE; Q9LIG6; -.
DR ProteomicsDB; 251161; -. [Q9LIG6-1]
DR EnsemblPlants; AT3G20970.1; AT3G20970.1; AT3G20970. [Q9LIG6-1]
DR GeneID; 821647; -.
DR Gramene; AT3G20970.1; AT3G20970.1; AT3G20970. [Q9LIG6-1]
DR KEGG; ath:AT3G20970; -.
DR Araport; AT3G20970; -.
DR TAIR; locus:2088781; AT3G20970.
DR eggNOG; KOG2358; Eukaryota.
DR HOGENOM; CLU_060555_0_1_1; -.
DR InParanoid; Q9LIG6; -.
DR OMA; DTAINDD; -.
DR OrthoDB; 1016782at2759; -.
DR PhylomeDB; Q9LIG6; -.
DR PRO; PR:Q9LIG6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LIG6; baseline and differential.
DR Genevisible; Q9LIG6; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
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:0005198; F:structural molecule activity; TAS:TAIR.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IBA:GO_Central.
DR Gene3D; 3.30.1370.70; -; 1.
DR Gene3D; 3.30.300.130; -; 1.
DR InterPro; IPR034904; FSCA_dom_sf.
DR InterPro; IPR014824; Nfu/NifU_N.
DR InterPro; IPR036498; Nfu/NifU_N_sf.
DR InterPro; IPR001075; NIF_FeS_clus_asmbl_NifU_C.
DR Pfam; PF08712; Nfu_N; 1.
DR Pfam; PF01106; NifU; 1.
DR SMART; SM00932; Nfu_N; 1.
DR SUPFAM; SSF110836; SSF110836; 1.
DR SUPFAM; SSF117916; SSF117916; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..48
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 49..283
FT /note="NifU-like protein 4, mitochondrial"
FT /id="PRO_0000255238"
SQ SEQUENCE 283 AA; 30504 MW; FEB967EB8B5785A2 CRC64;
MKGIARLVTS LSRIGGRKVV SGTSTVTSSS SSSLLLSRRS LFISATNLLN SRTKDSALPS
LNSSLLAQKW NFLGGQRRTM FIQTQSTPNP SSLMFYPGKP VMEVGSADFP NVRSALGSPL
AKSIYSIDGV VRVFFGSDFV TVTKSDDVSW DILKPEIFAA VMDFYSSGQP LFLDSQAAAA
KDTAISEDDS ETVAMIKELL ETRIRPAVQD DGGDIEYCGF DPESGIVKLR MQGACSGCPS
SSVTLKSGIE NMLMHYVSEV KGVEQEFDGE DEEGTLSGEM RVE
