ISU3_ARATH
ID ISU3_ARATH Reviewed; 171 AA.
AC O81433;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Iron-sulfur cluster assembly protein 3;
DE Short=AtISU3;
DE Short=Protein ISCU-LIKE 3;
DE AltName: Full=NifU-like N-terminal domain-containing protein ISU3;
DE AltName: Full=NifU-like protein ISU3;
DE Flags: Precursor;
GN Name=ISU3; OrderedLocusNames=At4g04080; ORFNames=T24H24.11;
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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GENE
RP FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=15792798; DOI=10.1016/j.febslet.2005.02.038;
RA Leon S., Touraine B., Briat J.-F., Lobreaux S.;
RT "Mitochondrial localization of Arabidopsis thaliana Isu Fe-S scaffold
RT proteins.";
RL FEBS Lett. 579:1930-1934(2005).
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].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Bautista-Mercan V.R., Kim C.J., Chen H., Quan R., De Los Reyes C.,
RA Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=17417719; DOI=10.1007/s11103-007-9147-x;
RA Frazzon A.P.G., Ramirez M.V., Warek U., Balk J., Frazzon J., Dean D.R.,
RA Winkel B.S.J.;
RT "Functional analysis of Arabidopsis genes involved in mitochondrial iron-
RT sulfur cluster assembly.";
RL Plant Mol. Biol. 64:225-240(2007).
CC -!- FUNCTION: Scaffold protein for the de novo synthesis of iron-sulfur
CC (Fe-S) clusters within mitochondria, which is required for maturation
CC of both mitochondrial and cytoplasmic [2Fe-2S] and [4Fe-4S] proteins
CC (PubMed:17417719). First, a [2Fe-2S] cluster is transiently assembled
CC on the scaffold protein ISCU (ISU1, ISU2 or ISU3). In a second step,
CC the cluster is released from ISCU, transferred to a glutaredoxin,
CC followed by the formation of mitochondrial [2Fe-2S] proteins, the
CC synthesis of [4Fe-4S] clusters and their target-specific insertion into
CC the recipient apoproteins. Cluster assembly on ISCU depends on the
CC function of the cysteine desulfurase complex NFS1-ISD11, which serves
CC as the sulfur donor for cluster synthesis, the iron-binding protein
CC frataxin as the putative iron donor, and the electron transfer chain
CC comprised of ferredoxin reductase and ferredoxin, which receive their
CC electrons from NADH (By similarity). {ECO:0000250|UniProtKB:Q03020,
CC ECO:0000269|PubMed:17417719}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000250|UniProtKB:O49627};
CC Note=Binds 1 [2Fe-2S] cluster per subunit.
CC {ECO:0000250|UniProtKB:O49627};
CC -!- PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
CC {ECO:0000250|UniProtKB:Q03020}.
CC -!- SUBUNIT: Component of the core Fe-S cluster (ISC) assembly machinery.
CC {ECO:0000250|UniProtKB:Q03020}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:15792798}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in flowers and pollen, and, to a
CC lower extent, in leaves and roots. {ECO:0000269|PubMed:15792798,
CC ECO:0000269|PubMed:17417719}.
CC -!- SIMILARITY: Belongs to the NifU family. {ECO:0000305}.
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DR EMBL; AJ866967; CAI29443.1; -; mRNA.
DR EMBL; AF075598; AAC28213.1; -; Genomic_DNA.
DR EMBL; AL161499; CAB77876.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82367.1; -; Genomic_DNA.
DR EMBL; DQ056643; AAY78791.1; -; mRNA.
DR EMBL; BT030662; ABR46242.1; -; mRNA.
DR PIR; T01466; T01466.
DR RefSeq; NP_192317.1; NM_116646.3.
DR AlphaFoldDB; O81433; -.
DR SMR; O81433; -.
DR STRING; 3702.AT4G04080.1; -.
DR PaxDb; O81433; -.
DR PRIDE; O81433; -.
DR ProteomicsDB; 250685; -.
DR EnsemblPlants; AT4G04080.1; AT4G04080.1; AT4G04080.
DR GeneID; 825719; -.
DR Gramene; AT4G04080.1; AT4G04080.1; AT4G04080.
DR KEGG; ath:AT4G04080; -.
DR Araport; AT4G04080; -.
DR TAIR; locus:2136612; AT4G04080.
DR eggNOG; KOG3361; Eukaryota.
DR HOGENOM; CLU_079283_1_2_1; -.
DR InParanoid; O81433; -.
DR OMA; PQCGDVM; -.
DR OrthoDB; 1406557at2759; -.
DR PhylomeDB; O81433; -.
DR UniPathway; UPA00266; -.
DR PRO; PR:O81433; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O81433; baseline and differential.
DR Genevisible; O81433; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; ISS:TAIR.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR CDD; cd06664; IscU_like; 1.
DR InterPro; IPR011339; ISC_FeS_clus_asmbl_IscU.
DR InterPro; IPR002871; NIF_FeS_clus_asmbl_NifU_N.
DR PANTHER; PTHR10093; PTHR10093; 1.
DR Pfam; PF01592; NifU_N; 1.
DR TIGRFAMs; TIGR01999; iscU; 1.
PE 2: Evidence at transcript level;
KW 2Fe-2S; Iron; Iron-sulfur; Metal-binding; Mitochondrion;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..49
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 50..171
FT /note="Iron-sulfur cluster assembly protein 3"
FT /id="PRO_0000415322"
SQ SEQUENCE 171 AA; 18471 MW; A856AB636DC35CDE CRC64;
MLRQTTKRAF LGLASQNPTP FPVVSRLYHP NVIDHYDNPR NVGSFDKNDP NVGTGLVGAP
QCGDVMKLQV KFDGSGQIID AKFKTFGCGS AIAASSVATE WVKGKSVEEV LTIKNSQIAK
HLSLPPVKLH CSMLAEDAIK AAIKNYKEKQ DKANGETVET IDSTYLHGIG S
