CISD1_MOUSE
ID CISD1_MOUSE Reviewed; 108 AA.
AC Q91WS0; Q3V2I3; Q8WUQ5;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=CDGSH iron-sulfur domain-containing protein 1;
DE AltName: Full=MitoNEET;
GN Name=Cisd1; Synonyms=D10Ertd214e, Zcd1;
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=BALB/cJ, and C57BL/6J; TISSUE=Pancreas, 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 TISSUE=Kidney, and Liver;
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 PROTEIN SEQUENCE OF 43-51; 56-68 AND 90-104, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55; LYS-68 AND LYS-104, 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: 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, ECO:0000269|PubMed:17376863}.
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:17376863}; Single-pass type III membrane protein
CC {ECO:0000269|PubMed:17376863}.
CC -!- TISSUE SPECIFICITY: Liver, adipose, skeletal muscle and heart (at
CC protein level). Widely expressed. Expressed at the highest levels in
CC the heart. {ECO:0000269|PubMed:17376863}.
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; AK075907; BAC36046.1; -; mRNA.
DR EMBL; AK131605; BAE20715.1; -; mRNA.
DR EMBL; AK131812; BAE20814.1; -; mRNA.
DR EMBL; AK131995; BAE20925.1; -; mRNA.
DR EMBL; AK167898; BAE39909.1; -; mRNA.
DR EMBL; BC013522; AAH13522.1; -; mRNA.
DR EMBL; BC019860; AAH19860.1; -; mRNA.
DR EMBL; BC021952; AAH21952.1; -; mRNA.
DR CCDS; CCDS23917.1; -.
DR RefSeq; NP_598768.1; NM_134007.4.
DR AlphaFoldDB; Q91WS0; -.
DR SMR; Q91WS0; -.
DR BioGRID; 206706; 34.
DR IntAct; Q91WS0; 1.
DR STRING; 10090.ENSMUSP00000043559; -.
DR iPTMnet; Q91WS0; -.
DR PhosphoSitePlus; Q91WS0; -.
DR SwissPalm; Q91WS0; -.
DR EPD; Q91WS0; -.
DR jPOST; Q91WS0; -.
DR MaxQB; Q91WS0; -.
DR PaxDb; Q91WS0; -.
DR PeptideAtlas; Q91WS0; -.
DR PRIDE; Q91WS0; -.
DR ProteomicsDB; 283623; -.
DR ABCD; Q91WS0; 2 sequenced antibodies.
DR Antibodypedia; 45107; 256 antibodies from 29 providers.
DR DNASU; 52637; -.
DR Ensembl; ENSMUST00000045887; ENSMUSP00000043559; ENSMUSG00000037710.
DR GeneID; 52637; -.
DR KEGG; mmu:52637; -.
DR UCSC; uc007foq.1; mouse.
DR CTD; 55847; -.
DR MGI; MGI:1261855; Cisd1.
DR VEuPathDB; HostDB:ENSMUSG00000037710; -.
DR eggNOG; KOG3461; Eukaryota.
DR GeneTree; ENSGT00940000154445; -.
DR HOGENOM; CLU_132293_1_0_1; -.
DR InParanoid; Q91WS0; -.
DR OMA; VVDMIDI; -.
DR OrthoDB; 1393750at2759; -.
DR PhylomeDB; Q91WS0; -.
DR TreeFam; TF324661; -.
DR BioGRID-ORCS; 52637; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Cisd1; mouse.
DR PRO; PR:Q91WS0; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q91WS0; protein.
DR Bgee; ENSMUSG00000037710; Expressed in interventricular septum and 266 other tissues.
DR Genevisible; Q91WS0; MM.
DR GO; GO:0032473; C:cytoplasmic side of mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005506; F:iron ion binding; ISO:MGI.
DR GO; GO:0010506; P:regulation of autophagy; IEA:InterPro.
DR GO; GO:0043457; P:regulation of cellular respiration; IMP:MGI.
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 CHAIN 1..108
FT /note="CDGSH iron-sulfur domain-containing protein 1"
FT /id="PRO_0000089804"
FT TRANSMEM 14..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:0007744|PubMed:23576753"
FT MOD_RES 68
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 104
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
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; 16F88E40729C1B49 CRC64;
MGLSSNSAVR VEWIAAVTFA AGTAALGYLA YKKFYAKENR TKAMVNLQIQ KDNPKVVHAF
DMEDLGDKAV YCRCWRSKKF PFCDGAHIKH NEETGDNVGP LIIKKKET
