CISD1_RAT
ID CISD1_RAT Reviewed; 108 AA.
AC B0K020;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=CDGSH iron-sulfur domain-containing protein 1;
DE AltName: Full=MitoNEET;
GN Name=Cisd1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Plays a key role in regulating maximal capacity for electron
CC transport and oxidative phosphorylation. May be involved in Fe-S
CC cluster shuttling and/or in redox reactions. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. The [2Fe-2S] cluster is
CC redox-active and pH labile and is significantly less stable at pH 4.5
CC as compared with pH 7.0. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC Single-pass type III membrane protein {ECO:0000250}.
CC -!- PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation
CC and enhancement of mitophagy. Deubiquitinated by USP30.
CC {ECO:0000250|UniProtKB:Q9NZ45}.
CC -!- SIMILARITY: Belongs to the CISD protein family. {ECO:0000305}.
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DR EMBL; CH473988; EDL97255.1; -; Genomic_DNA.
DR EMBL; BC159419; AAI59420.1; -; mRNA.
DR RefSeq; NP_001099855.1; NM_001106385.2.
DR AlphaFoldDB; B0K020; -.
DR SMR; B0K020; -.
DR BioGRID; 254688; 1.
DR IntAct; B0K020; 1.
DR MINT; B0K020; -.
DR STRING; 10116.ENSRNOP00000000749; -.
DR BindingDB; B0K020; -.
DR ChEMBL; CHEMBL3308979; -.
DR CarbonylDB; B0K020; -.
DR iPTMnet; B0K020; -.
DR PhosphoSitePlus; B0K020; -.
DR SwissPalm; B0K020; -.
DR jPOST; B0K020; -.
DR PaxDb; B0K020; -.
DR PeptideAtlas; B0K020; -.
DR PRIDE; B0K020; -.
DR GeneID; 294362; -.
DR KEGG; rno:294362; -.
DR UCSC; RGD:1309529; rat.
DR CTD; 55847; -.
DR RGD; 1309529; Cisd1.
DR VEuPathDB; HostDB:ENSRNOG00000000610; -.
DR eggNOG; KOG3461; Eukaryota.
DR HOGENOM; CLU_132293_1_0_1; -.
DR InParanoid; B0K020; -.
DR OMA; VVDMIDI; -.
DR OrthoDB; 1393750at2759; -.
DR PhylomeDB; B0K020; -.
DR TreeFam; TF324661; -.
DR PRO; PR:B0K020; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Proteomes; UP000234681; Chromosome 20.
DR Bgee; ENSRNOG00000000610; Expressed in kidney and 20 other tissues.
DR Genevisible; B0K020; RN.
DR GO; GO:0032473; C:cytoplasmic side of mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0010506; P:regulation of autophagy; IEA:InterPro.
DR GO; GO:0043457; P:regulation of cellular respiration; ISO:RGD.
DR Gene3D; 3.40.5.90; -; 1.
DR InterPro; IPR045131; CISD1/2.
DR InterPro; IPR018967; FeS-contain_CDGSH-typ.
DR InterPro; IPR019610; FeS-contain_mitoNEET_N.
DR InterPro; IPR042216; MitoNEET_CISD.
DR PANTHER; PTHR13680; PTHR13680; 1.
DR Pfam; PF10660; MitoNEET_N; 1.
DR Pfam; PF09360; zf-CDGSH; 1.
DR SMART; SM00704; ZnF_CDGSH; 1.
PE 3: Inferred from homology;
KW 2Fe-2S; Acetylation; Iron; Iron-sulfur; Isopeptide bond; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion outer membrane;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT CHAIN 1..108
FT /note="CDGSH iron-sulfur domain-containing protein 1"
FT /id="PRO_0000354705"
FT TRANSMEM 13..31
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..108
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 72
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT MOD_RES 55
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91WS0"
FT MOD_RES 68
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91WS0"
FT MOD_RES 104
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91WS0"
FT CROSSLNK 42
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9NZ45"
FT CROSSLNK 55
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9NZ45"
FT CROSSLNK 68
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9NZ45"
FT CROSSLNK 78
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9NZ45"
FT CROSSLNK 79
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9NZ45"
FT CROSSLNK 89
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9NZ45"
FT CROSSLNK 104
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9NZ45"
FT CROSSLNK 105
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9NZ45"
FT CROSSLNK 106
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9NZ45"
SQ SEQUENCE 108 AA; 12097 MW; 72B2548F490E5FA3 CRC64;
MGLSSDSPVR VEWIAAVTFA AGTAALGYLA YKKFYAKESR TKAMVNLQIQ KDNPKVVHAF
DMEDLGDKAV YCRCWRSKKF PFCDGAHIKH NEETGDNVGP LIIKKKET
