CISD3_MOUSE
ID CISD3_MOUSE Reviewed; 137 AA.
AC B1AR13; B1AR11; B1AR12;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=CDGSH iron-sulfur domain-containing protein 3, mitochondrial;
DE AltName: Full=Melanoma nuclear protein 13;
DE Flags: Precursor;
GN Name=Cisd3; Synonyms=Mel-13, Mel13;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP IDENTIFICATION.
RX PubMed=8597592; DOI=10.1016/0167-4781(95)00229-4;
RA Tetsu O., Kanno R., Isono K., Taniguchi M., Kanno M.;
RT "Cloning and characterization of two transcripts generated from the mel-13
RT gene positioned adjacent to the mammalian Polycomb group-related gene mel-
RT 18.";
RL Biochim. Biophys. Acta 1305:109-112(1996).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, and Liver;
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 SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-65 AND LYS-124, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-96 AND LYS-124, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Can transfer its iron-sulfur clusters to the apoferrodoxins
CC FDX1 and FDX2. Contributes to mitochondrial iron homeostasis and in
CC maintaining normal levels of free iron and reactive oxygen species, and
CC thereby contributes to normal mitochondrial function.
CC {ECO:0000250|UniProtKB:P0C7P0}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000250|UniProtKB:P0C7P0};
CC Note=Binds 2 [2Fe-2S] clusters per subunit.
CC {ECO:0000250|UniProtKB:P0C7P0};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P0C7P0}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P0C7P0}.
CC -!- SIMILARITY: Belongs to the CISD protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM27408.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM27409.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL596123; CAM27408.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL596123; CAM27409.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL596123; CAM27410.1; -; Genomic_DNA.
DR CCDS; CCDS48896.1; -.
DR RefSeq; NP_001078969.2; NM_001085500.2.
DR AlphaFoldDB; B1AR13; -.
DR SMR; B1AR13; -.
DR BioGRID; 229853; 3.
DR STRING; 10090.ENSMUSP00000103209; -.
DR iPTMnet; B1AR13; -.
DR PhosphoSitePlus; B1AR13; -.
DR SwissPalm; B1AR13; -.
DR EPD; B1AR13; -.
DR jPOST; B1AR13; -.
DR MaxQB; B1AR13; -.
DR PaxDb; B1AR13; -.
DR PeptideAtlas; B1AR13; -.
DR PRIDE; B1AR13; -.
DR ProteomicsDB; 279084; -.
DR Antibodypedia; 75426; 8 antibodies from 4 providers.
DR Ensembl; ENSMUST00000107583; ENSMUSP00000103209; ENSMUSG00000078695.
DR GeneID; 217149; -.
DR KEGG; mmu:217149; -.
DR UCSC; uc007lek.2; mouse.
DR CTD; 284106; -.
DR MGI; MGI:101788; Cisd3.
DR VEuPathDB; HostDB:ENSMUSG00000078695; -.
DR eggNOG; KOG4605; Eukaryota.
DR GeneTree; ENSGT00390000004574; -.
DR InParanoid; B1AR13; -.
DR OrthoDB; 1565094at2759; -.
DR PhylomeDB; B1AR13; -.
DR TreeFam; TF313111; -.
DR BioGRID-ORCS; 217149; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Cisd3; mouse.
DR PRO; PR:B1AR13; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; B1AR13; protein.
DR Bgee; ENSMUSG00000078695; Expressed in white adipose tissue and 60 other tissues.
DR ExpressionAtlas; B1AR13; baseline and differential.
DR Genevisible; B1AR13; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
DR GO; GO:0106034; P:protein maturation by [2Fe-2S] cluster transfer; ISS:UniProtKB.
DR Gene3D; 3.40.5.90; -; 2.
DR InterPro; IPR018967; FeS-contain_CDGSH-typ.
DR InterPro; IPR042216; MitoNEET_CISD.
DR Pfam; PF09360; zf-CDGSH; 2.
DR SMART; SM00704; ZnF_CDGSH; 2.
PE 1: Evidence at protein level;
KW 2Fe-2S; Acetylation; Iron; Iron-sulfur; Metal-binding; Mitochondrion;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..137
FT /note="CDGSH iron-sulfur domain-containing protein 3,
FT mitochondrial"
FT /id="PRO_0000341406"
FT BINDING 70
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0C7P0"
FT BINDING 72
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0C7P0"
FT BINDING 81
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0C7P0"
FT BINDING 85
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0C7P0"
FT BINDING 108
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0C7P0"
FT BINDING 110
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0C7P0"
FT BINDING 119
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0C7P0"
FT BINDING 123
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0C7P0"
FT MOD_RES 65
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C7P0"
FT MOD_RES 65
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 96
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 124
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 124
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 137 AA; 15676 MW; 526B8680019C135D CRC64;
MGFRRLSFPT DFIFLFPNHI CLPALSKPYQ RREISSWLAR WFPKDPAKPV VAQKTPIRLE
LVAGKTYRWC VCGRSKNQPF CDGSHFFQRT GLSPLKFKAQ ETRTVALCTC KATQRPPYCD
GTHKSEQVQK AEVGSPL
