ISCU_MOUSE
ID ISCU_MOUSE Reviewed; 168 AA.
AC Q9D7P6; Q4VBC7; Q8K344;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Iron-sulfur cluster assembly enzyme ISCU, mitochondrial;
DE AltName: Full=NifU-like N-terminal domain-containing protein;
DE AltName: Full=NifU-like protein;
DE Flags: Precursor;
GN Name=Iscu; Synonyms=Nifun;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hippocampus, Thymus, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary gland, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP STRUCTURE BY NMR OF 45-161.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of iron-sulfur cluster protein (ISCU).";
RL Submitted (NOV-2004) to the PDB data bank.
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 First, a [2Fe-2S] cluster is transiently assembled on the scaffold
CC protein ISCU. In a second step, the cluster is released from ISCU,
CC transferred to a glutaredoxin GLRX5, followed by the formation of
CC mitochondrial [2Fe-2S] proteins, the synthesis of [4Fe-4S] clusters and
CC their target-specific insertion into the recipient apoproteins. Cluster
CC assembly on ISCU depends on the function of the cysteine desulfurase
CC complex NFS1-LYRM4/ISD11, which serves as the sulfur donor for cluster
CC synthesis, the iron-binding protein frataxin as the putative iron
CC donor, and the electron transfer chain comprised of ferredoxin
CC reductase and ferredoxin, which receive their electrons from NADH (By
CC similarity). {ECO:0000250|UniProtKB:Q03020,
CC ECO:0000250|UniProtKB:Q9H1K1}.
CC -!- SUBUNIT: Binds NFS1. Interacts with HSCB. Interacts with GLRX5.
CC Interacts with HSPA9. Interacts with HSC20.
CC {ECO:0000250|UniProtKB:Q9H1K1}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9H1K1}.
CC -!- SIMILARITY: Belongs to the NifU family. {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; AK009021; BAB26031.1; -; mRNA.
DR EMBL; AK039834; BAC30464.1; -; mRNA.
DR EMBL; AK083247; BAC38830.1; -; mRNA.
DR EMBL; BC028800; AAH28800.1; -; mRNA.
DR EMBL; BC048409; AAH48409.1; -; mRNA.
DR EMBL; BC096049; AAH96049.1; -; mRNA.
DR CCDS; CCDS19553.1; -.
DR RefSeq; NP_079802.1; NM_025526.4.
DR PDB; 1WFZ; NMR; -; A=45-161.
DR PDBsum; 1WFZ; -.
DR AlphaFoldDB; Q9D7P6; -.
DR BMRB; Q9D7P6; -.
DR SMR; Q9D7P6; -.
DR BioGRID; 211430; 6.
DR ComplexPortal; CPX-5823; Mitochondrial NIAUFX iron-sulfur cluster assembly complex.
DR CORUM; Q9D7P6; -.
DR STRING; 10090.ENSMUSP00000026937; -.
DR iPTMnet; Q9D7P6; -.
DR PhosphoSitePlus; Q9D7P6; -.
DR EPD; Q9D7P6; -.
DR jPOST; Q9D7P6; -.
DR MaxQB; Q9D7P6; -.
DR PaxDb; Q9D7P6; -.
DR PeptideAtlas; Q9D7P6; -.
DR PRIDE; Q9D7P6; -.
DR ProteomicsDB; 269099; -.
DR DNASU; 66383; -.
DR Ensembl; ENSMUST00000026937; ENSMUSP00000026937; ENSMUSG00000025825.
DR GeneID; 66383; -.
DR KEGG; mmu:66383; -.
DR UCSC; uc008yyp.1; mouse.
DR CTD; 23479; -.
DR MGI; MGI:1913633; Iscu.
DR VEuPathDB; HostDB:ENSMUSG00000025825; -.
DR eggNOG; KOG3361; Eukaryota.
DR GeneTree; ENSGT00940000166181; -.
DR HOGENOM; CLU_079283_1_2_1; -.
DR InParanoid; Q9D7P6; -.
DR OMA; YKNPRNY; -.
DR OrthoDB; 1406557at2759; -.
DR PhylomeDB; Q9D7P6; -.
DR TreeFam; TF105422; -.
DR Reactome; R-MMU-1362409; Mitochondrial iron-sulfur cluster biogenesis.
DR BioGRID-ORCS; 66383; 25 hits in 68 CRISPR screens.
DR ChiTaRS; Iscu; mouse.
DR EvolutionaryTrace; Q9D7P6; -.
DR PRO; PR:Q9D7P6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9D7P6; protein.
DR Bgee; ENSMUSG00000025825; Expressed in adrenal gland and 61 other tissues.
DR ExpressionAtlas; Q9D7P6; baseline and differential.
DR Genevisible; Q9D7P6; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:1990229; C:iron-sulfur cluster assembly complex; IC:ComplexPortal.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
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:0060090; F:molecular adaptor activity; ISO:MGI.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IC:ComplexPortal.
DR GO; GO:1904439; P:negative regulation of iron ion import across plasma membrane; ISO:MGI.
DR GO; GO:1904234; P:positive regulation of aconitate hydratase activity; ISO:MGI.
DR GO; GO:1902958; P:positive regulation of mitochondrial electron transport, NADH to ubiquinone; ISO:MGI.
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 3D-structure; Iron; Metal-binding; Mitochondrion; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 36..168
FT /note="Iron-sulfur cluster assembly enzyme ISCU,
FT mitochondrial"
FT /id="PRO_0000019693"
FT STRAND 58..67
FT /evidence="ECO:0007829|PDB:1WFZ"
FT TURN 68..71
FT /evidence="ECO:0007829|PDB:1WFZ"
FT STRAND 72..80
FT /evidence="ECO:0007829|PDB:1WFZ"
FT STRAND 82..92
FT /evidence="ECO:0007829|PDB:1WFZ"
FT HELIX 97..110
FT /evidence="ECO:0007829|PDB:1WFZ"
FT HELIX 115..120
FT /evidence="ECO:0007829|PDB:1WFZ"
FT HELIX 123..130
FT /evidence="ECO:0007829|PDB:1WFZ"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:1WFZ"
FT HELIX 137..159
FT /evidence="ECO:0007829|PDB:1WFZ"
SQ SEQUENCE 168 AA; 18098 MW; 06B6350434FEAAF6 CRC64;
MAAATGAGRL RRAASALLLR SPRLPARELS APARLYHKKV VDHYENPRNV GSLDKTSKNV
GTGLVGAPAC GDVMKLQIQV DEKGKIVDAR FKTFGCGSAI ASSSLATEWV KGKTVEEALT
IKNTDIAKEL CLPPVKLHCS MLAEDAIKAA LADYKLKQES KKEEPEKQ
