CISD3_HUMAN
ID CISD3_HUMAN Reviewed; 127 AA.
AC P0C7P0;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=CDGSH iron-sulfur domain-containing protein 3, mitochondrial;
DE AltName: Full=MitoNEET-related protein 2;
DE Short=Miner2;
DE AltName: Full=Mitochondrial inner NEET protein {ECO:0000303|PubMed:29259115};
DE Short=MiNT {ECO:0000303|PubMed:29259115};
DE Flags: Precursor;
GN Name=CISD3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hippocampus;
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 COFACTOR, AND SUBCELLULAR LOCATION.
RX PubMed=17376863; DOI=10.1073/pnas.0701078104;
RA Wiley S.E., Murphy A.N., Ross S.A., van der Geer P., Dixon J.E.;
RT "MitoNEET is an iron-containing outer mitochondrial membrane protein that
RT regulates oxidative capacity.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5318-5323(2007).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [5] {ECO:0007744|PDB:6AVJ}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 36-127, FUNCTION, COFACTOR,
RP SUBUNIT, AND MUTAGENESIS OF HIS-75 AND HIS-113.
RX PubMed=29259115; DOI=10.1073/pnas.1715842115;
RA Lipper C.H., Karmi O., Sohn Y.S., Darash-Yahana M., Lammert H., Song L.,
RA Liu A., Mittler R., Nechushtai R., Onuchic J.N., Jennings P.A.;
RT "Structure of the human monomeric NEET protein MiNT and its role in
RT regulating iron and reactive oxygen species in cancer cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:272-277(2018).
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:0000269|PubMed:29259115}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:29259115, ECO:0000305|PubMed:17376863};
CC Note=Binds 2 [2Fe-2S] clusters per subunit.
CC {ECO:0000269|PubMed:29259115, ECO:0000305|PubMed:17376863};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:29259115}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:17376863}.
CC -!- SIMILARITY: Belongs to the CISD protein family. {ECO:0000305}.
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DR EMBL; AC006449; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BM546511; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS45662.1; -.
DR RefSeq; NP_001129970.1; NM_001136498.1.
DR PDB; 6AVJ; X-ray; 1.90 A; A/B/C=36-127.
DR PDBsum; 6AVJ; -.
DR AlphaFoldDB; P0C7P0; -.
DR SMR; P0C7P0; -.
DR BioGRID; 129759; 84.
DR IntAct; P0C7P0; 91.
DR STRING; 9606.ENSP00000483781; -.
DR iPTMnet; P0C7P0; -.
DR PhosphoSitePlus; P0C7P0; -.
DR BioMuta; CISD3; -.
DR DMDM; 190358744; -.
DR EPD; P0C7P0; -.
DR jPOST; P0C7P0; -.
DR MassIVE; P0C7P0; -.
DR MaxQB; P0C7P0; -.
DR PaxDb; P0C7P0; -.
DR PeptideAtlas; P0C7P0; -.
DR PRIDE; P0C7P0; -.
DR ProteomicsDB; 52352; -.
DR Antibodypedia; 75426; 8 antibodies from 4 providers.
DR DNASU; 284106; -.
DR Ensembl; ENST00000613478.2; ENSP00000483781.1; ENSG00000277972.2.
DR Ensembl; ENST00000620783.2; ENSP00000484950.1; ENSG00000274768.2.
DR GeneID; 284106; -.
DR KEGG; hsa:284106; -.
DR MANE-Select; ENST00000613478.2; ENSP00000483781.1; NM_001136498.2; NP_001129970.1.
DR UCSC; uc010wds.2; human.
DR CTD; 284106; -.
DR DisGeNET; 284106; -.
DR GeneCards; CISD3; -.
DR HGNC; HGNC:27578; CISD3.
DR HPA; ENSG00000277972; Low tissue specificity.
DR MIM; 611933; gene.
DR neXtProt; NX_P0C7P0; -.
DR OpenTargets; ENSG00000277972; -.
DR PharmGKB; PA162382311; -.
DR VEuPathDB; HostDB:ENSG00000277972; -.
DR eggNOG; KOG4605; Eukaryota.
DR GeneTree; ENSGT00390000004574; -.
DR HOGENOM; CLU_145019_1_0_1; -.
DR InParanoid; P0C7P0; -.
DR OMA; RRDITSW; -.
DR OrthoDB; 1565094at2759; -.
DR PhylomeDB; P0C7P0; -.
DR TreeFam; TF313111; -.
DR PathwayCommons; P0C7P0; -.
DR SignaLink; P0C7P0; -.
DR BioGRID-ORCS; 284106; 18 hits in 1074 CRISPR screens.
DR ChiTaRS; CISD3; human.
DR GenomeRNAi; 284106; -.
DR Pharos; P0C7P0; Tbio.
DR PRO; PR:P0C7P0; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P0C7P0; protein.
DR Bgee; ENSG00000277972; Expressed in mucosa of transverse colon and 95 other tissues.
DR Genevisible; P0C7P0; HS.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
DR GO; GO:0106034; P:protein maturation by [2Fe-2S] cluster transfer; IDA: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; 3D-structure; Acetylation; Iron; Iron-sulfur; Metal-binding;
KW Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..14
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 15..127
FT /note="CDGSH iron-sulfur domain-containing protein 3,
FT mitochondrial"
FT /id="PRO_0000341405"
FT BINDING 60
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29259115,
FT ECO:0007744|PDB:6AVJ"
FT BINDING 62
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29259115,
FT ECO:0007744|PDB:6AVJ"
FT BINDING 71
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29259115,
FT ECO:0007744|PDB:6AVJ"
FT BINDING 75
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:29259115,
FT ECO:0007744|PDB:6AVJ"
FT BINDING 98
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29259115,
FT ECO:0007744|PDB:6AVJ"
FT BINDING 100
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29259115,
FT ECO:0007744|PDB:6AVJ"
FT BINDING 109
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29259115,
FT ECO:0007744|PDB:6AVJ"
FT BINDING 113
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:29259115,
FT ECO:0007744|PDB:6AVJ"
FT MOD_RES 55
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 55
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:B1AR13"
FT MOD_RES 86
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:B1AR13"
FT MUTAGEN 75
FT /note="H->C: Increases iron-sulfur cluster stability; when
FT associated with C-113."
FT /evidence="ECO:0000269|PubMed:29259115"
FT MUTAGEN 113
FT /note="H->C: Increases iron-sulfur cluster stability; when
FT associated with C-75."
FT /evidence="ECO:0000269|PubMed:29259115"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:6AVJ"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:6AVJ"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:6AVJ"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:6AVJ"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:6AVJ"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:6AVJ"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:6AVJ"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:6AVJ"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:6AVJ"
SQ SEQUENCE 127 AA; 14216 MW; D6D1FC5D7466ACEF CRC64;
MRGAGAILRP AARGARDLNP RRDISSWLAQ WFPRTPARSV VALKTPIKVE LVAGKTYRWC
VCGRSKKQPF CDGSHFFQRT GLSPLKFKAQ ETRMVALCTC KATQRPPYCD GTHRSERVQK
AEVGSPL
