CISD1_BOVIN
ID CISD1_BOVIN Reviewed; 106 AA.
AC Q3ZBU2;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=CDGSH iron-sulfur domain-containing protein 1;
DE AltName: Full=MitoNEET;
GN Name=CISD1; Synonyms=ZCD1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 60-71, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain;
RX PubMed=14570702; DOI=10.1152/ajpendo.00424.2003;
RA Colca J.R., McDonald W.G., Waldon D.J., Leone J.W., Lull J.M., Bannow C.A.,
RA Lund E.T., Mathews W.R.;
RT "Identification of a novel mitochondrial protein ('mitoNEET') cross-linked
RT specifically by a thiazolidinedione photoprobe.";
RL Am. J. Physiol. 286:E252-E260(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 (By similarity).
CC {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. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:14570702}; Single-pass type III membrane protein
CC {ECO:0000269|PubMed:14570702}.
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 -!- MISCELLANEOUS: Binds pioglitazone, an anti-diabetes drug.
CC -!- SIMILARITY: Belongs to the CISD protein family. {ECO:0000305}.
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DR EMBL; BC103105; AAI03106.1; -; mRNA.
DR RefSeq; NP_001029229.1; NM_001034057.1.
DR AlphaFoldDB; Q3ZBU2; -.
DR SMR; Q3ZBU2; -.
DR STRING; 9913.ENSBTAP00000004739; -.
DR PaxDb; Q3ZBU2; -.
DR PeptideAtlas; Q3ZBU2; -.
DR PRIDE; Q3ZBU2; -.
DR Ensembl; ENSBTAT00000004739; ENSBTAP00000004739; ENSBTAG00000003634.
DR GeneID; 531444; -.
DR KEGG; bta:531444; -.
DR CTD; 55847; -.
DR VEuPathDB; HostDB:ENSBTAG00000003634; -.
DR VGNC; VGNC:27371; CISD1.
DR eggNOG; KOG3461; Eukaryota.
DR GeneTree; ENSGT00940000154445; -.
DR HOGENOM; CLU_132293_1_0_1; -.
DR InParanoid; Q3ZBU2; -.
DR OMA; VVDMIDI; -.
DR OrthoDB; 1393750at2759; -.
DR TreeFam; TF324661; -.
DR Proteomes; UP000009136; Chromosome 26.
DR Bgee; ENSBTAG00000003634; Expressed in spermatid and 105 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IBA:GO_Central.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0010506; P:regulation of autophagy; IEA:InterPro.
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 1: Evidence at protein level;
KW 2Fe-2S; Acetylation; Direct protein sequencing; Iron; Iron-sulfur;
KW Isopeptide bond; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion outer membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NZ45"
FT CHAIN 2..106
FT /note="CDGSH iron-sulfur domain-containing protein 1"
FT /id="PRO_0000246997"
FT TRANSMEM 10..29
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 84..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 70
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZ45"
FT MOD_RES 53
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91WS0"
FT MOD_RES 66
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91WS0"
FT MOD_RES 102
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91WS0"
FT CROSSLNK 40
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9NZ45"
FT CROSSLNK 53
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9NZ45"
FT CROSSLNK 66
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9NZ45"
FT CROSSLNK 76
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9NZ45"
FT CROSSLNK 77
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9NZ45"
FT CROSSLNK 87
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9NZ45"
FT CROSSLNK 102
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9NZ45"
FT CROSSLNK 103
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)"
FT /evidence="ECO:0000250|UniProtKB:Q9NZ45"
SQ SEQUENCE 106 AA; 11983 MW; 039C4FFB6F3DF625 CRC64;
MSMTSSVRVE WIAAVTIAAG TAAIGYLAYK RFYVKDHRNK SMVNPHIQKD NPKVVHAFDM
EDLGDKAVYC RCWRSKKFPL CDGSHTKHNE ETGDNVGPLI IKKKDT
