ISU1_ARATH
ID ISU1_ARATH Reviewed; 167 AA.
AC O49627; Q8L984;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Iron-sulfur cluster assembly protein 1;
DE Short=AtISU1 {ECO:0000303|PubMed:15507320};
DE Short=AtIscU1 {ECO:0000303|PubMed:19865480};
DE Short=Protein ISCU-LIKE 1;
DE AltName: Full=NifU-like N-terminal domain-containing protein ISU1;
DE AltName: Full=NifU-like protein ISU1;
DE Flags: Precursor;
GN Name=ISU1; Synonyms=ISCU1 {ECO:0000303|PubMed:19865480};
GN OrderedLocusNames=At4g22220 {ECO:0000312|Araport:AT4G22220};
GN ORFNames=T10I14.50 {ECO:0000312|EMBL:CAA16772.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15507320; DOI=10.1016/j.bbaexp.2004.09.005;
RA Tone Y., Kawai-Yamada M., Uchimiya H.;
RT "Isolation and characterization of Arabidopsis thaliana ISU1 gene.";
RL Biochim. Biophys. Acta 1680:171-175(2004).
RN [2]
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 [3]
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 [4]
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 [5]
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).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.
RN [7]
RP FUNCTION, COFACTOR, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
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).
RN [8]
RP INTERACTION WITH HSCB, AND SUBCELLULAR LOCATION.
RX PubMed=19865480; DOI=10.1371/journal.pone.0007662;
RA Xu X.M., Lin H., Latijnhouwers M., Moeller S.G.;
RT "Dual localized AtHscB involved in iron sulfur protein biogenesis in
RT Arabidopsis.";
RL PLoS ONE 4:E7662-E7662(2009).
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:15507320, PubMed:17417719). First, a [2Fe-2S] cluster is
CC transiently assembled on the scaffold protein ISCU (ISU1, ISU2 or
CC ISU3). In a second step, the cluster is released from ISCU, transferred
CC to a glutaredoxin, followed by the formation of mitochondrial [2Fe-2S]
CC proteins, the synthesis of [4Fe-4S] clusters and their target-specific
CC insertion into the recipient apoproteins. Cluster assembly on ISCU
CC depends on the function of the cysteine desulfurase complex NFS1-ISD11,
CC which serves as the sulfur donor for cluster synthesis, the iron-
CC binding protein frataxin as the putative iron donor, and the electron
CC transfer chain comprised of ferredoxin reductase and ferredoxin, which
CC receive their electrons from NADH (By similarity).
CC {ECO:0000250|UniProtKB:Q03020, ECO:0000269|PubMed:15507320,
CC ECO:0000269|PubMed:17417719}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:17417719};
CC Note=Binds 1 [2Fe-2S] cluster per subunit.
CC {ECO:0000269|PubMed:17417719};
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 (By similarity). Interacts with HSCB (PubMed:19865480).
CC {ECO:0000250|UniProtKB:Q03020, ECO:0000269|PubMed:19865480}.
CC -!- INTERACTION:
CC O49627; Q9LPR8: SCL3; NbExp=4; IntAct=EBI-4435514, EBI-4429250;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:15792798, ECO:0000269|PubMed:17417719,
CC ECO:0000269|PubMed:19865480}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:19865480}. Note=Localizes to the cytosol when
CC interacting with HSCB. {ECO:0000269|PubMed:19865480}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers, pollen
CC and siliques. {ECO:0000269|PubMed:15507320,
CC ECO:0000269|PubMed:15792798, ECO:0000269|PubMed:17417719}.
CC -!- SIMILARITY: Belongs to the NifU family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM66114.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ866966; CAI29442.1; -; mRNA.
DR EMBL; AL021712; CAA16772.1; -; Genomic_DNA.
DR EMBL; AL161556; CAB79177.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84576.1; -; Genomic_DNA.
DR EMBL; AF361579; AAK32747.1; -; mRNA.
DR EMBL; AY081721; AAL87374.1; -; mRNA.
DR EMBL; AY088584; AAM66114.1; ALT_INIT; mRNA.
DR PIR; T04903; T04903.
DR RefSeq; NP_193953.1; NM_118347.3.
DR AlphaFoldDB; O49627; -.
DR SMR; O49627; -.
DR BioGRID; 13605; 5.
DR IntAct; O49627; 6.
DR STRING; 3702.AT4G22220.1; -.
DR MetOSite; O49627; -.
DR SwissPalm; O49627; -.
DR PaxDb; O49627; -.
DR PRIDE; O49627; -.
DR ProteomicsDB; 238953; -.
DR EnsemblPlants; AT4G22220.1; AT4G22220.1; AT4G22220.
DR GeneID; 828316; -.
DR Gramene; AT4G22220.1; AT4G22220.1; AT4G22220.
DR KEGG; ath:AT4G22220; -.
DR Araport; AT4G22220; -.
DR TAIR; locus:2132090; AT4G22220.
DR eggNOG; KOG3361; Eukaryota.
DR HOGENOM; CLU_079283_5_0_1; -.
DR InParanoid; O49627; -.
DR OMA; YKNPRNY; -.
DR OrthoDB; 1406557at2759; -.
DR PhylomeDB; O49627; -.
DR UniPathway; UPA00266; -.
DR PRO; PR:O49627; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O49627; baseline and differential.
DR Genevisible; O49627; 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 1: Evidence at protein level;
KW 2Fe-2S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Mitochondrion;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..50
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 51..167
FT /note="Iron-sulfur cluster assembly protein 1"
FT /id="PRO_0000415320"
FT CONFLICT 24..26
FT /note="GIL -> SIF (in Ref. 6; AAM66114)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 167 AA; 17915 MW; 13C8C3A028781990 CRC64;
MMLKQAAKKA LGLTSRQSTP WSVGILRTYH ENVIDHYDNP RNVGSFDKND PNVGTGLVGA
PACGDVMKLQ IKVDEKTGQI VDARFKTFGC GSAIASSSVA TEWVKGKAME DVLTIKNTEI
AKHLSLPPVK LHCSMLAEDA IKAAVKDYKE KRVKTNGAAA AGETTQA
