ID   ISU2_ARATH              Reviewed;         163 AA.
AC   Q9MAB6; Q2WEB4;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Iron-sulfur cluster assembly protein 2;
DE            Short=AtISU2;
DE            Short=Protein ISCU-LIKE 2;
DE   AltName: Full=NifU-like N-terminal domain-containing protein ISU2;
DE   AltName: Full=NifU-like protein ISU2;
DE   Flags: Precursor;
GN   Name=ISU2; OrderedLocusNames=At3g01020; ORFNames=T4P13.30;
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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=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   FUNCTION, 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).
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, ECO:0000269|PubMed:17417719}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in leaves, pollen and flowers.
CC       {ECO:0000269|PubMed:15792798, ECO:0000269|PubMed:17417719}.
CC   -!- SIMILARITY: Belongs to the NifU family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAI29444.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ866968; CAI29444.1; ALT_INIT; mRNA.
DR   EMBL; AC008261; AAF26172.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE73596.1; -; Genomic_DNA.
DR   EMBL; DQ056583; AAY78732.1; -; mRNA.
DR   RefSeq; NP_186751.1; NM_110967.3.
DR   AlphaFoldDB; Q9MAB6; -.
DR   SMR; Q9MAB6; -.
DR   STRING; 3702.AT3G01020.1; -.
DR   PaxDb; Q9MAB6; -.
DR   PRIDE; Q9MAB6; -.
DR   ProteomicsDB; 238954; -.
DR   EnsemblPlants; AT3G01020.1; AT3G01020.1; AT3G01020.
DR   GeneID; 821316; -.
DR   Gramene; AT3G01020.1; AT3G01020.1; AT3G01020.
DR   KEGG; ath:AT3G01020; -.
DR   Araport; AT3G01020; -.
DR   TAIR; locus:2102122; AT3G01020.
DR   eggNOG; KOG3361; Eukaryota.
DR   HOGENOM; CLU_079283_5_0_1; -.
DR   InParanoid; Q9MAB6; -.
DR   OMA; VGSFNRN; -.
DR   OrthoDB; 1406557at2759; -.
DR   PhylomeDB; Q9MAB6; -.
DR   UniPathway; UPA00266; -.
DR   PRO; PR:Q9MAB6; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9MAB6; baseline and differential.
DR   Genevisible; Q9MAB6; 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..48
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           49..163
FT                   /note="Iron-sulfur cluster assembly protein 2"
FT                   /id="PRO_0000415321"
SQ   SEQUENCE   163 AA;  17745 MW;  55357B4245B397B0 CRC64;
     MMMLRQTSRK AYLGLQASPL GLGRRLYHEN VIDHFENPRN VGSFNRNDPN VGTGLVGAPA
     CGDLMSLQIK VDDSGQIIDT RFKTFGCGSA IASSSVASEW IKGKTLDEVM TIKNAEIAKH
     LRLPPVKLHC SMLAEDAIKS AVRDYKEKQA KTNAAAAEET VKA