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CDGSH iron-sulfur domain-containing protein 1 (MitoNEET)

 CISD1_HUMAN             Reviewed;         108 AA.
Q9NZ45; Q1X902;
25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 146.
RecName: Full=CDGSH iron-sulfur domain-containing protein 1;
AltName: Full=MitoNEET;
Name=CISD1; Synonyms=C10orf70, ZCD1; ORFNames=MDS029;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
AND INDUCTION.
PubMed=18047834; DOI=10.1016/j.bbrc.2007.11.076;
Taminelli G.L., Sotomayor V., Valdivieso A.G., Teiber M.L.,
Marin M.C., Santa-Coloma T.A.;
"CISD1 codifies a mitochondrial protein upregulated by the CFTR
channel.";
Biochem. Biophys. Res. Commun. 365:856-862(2008).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Hematopoietic stem cell;
Zhao M., Gu J., Li N., Peng Y., Han Z., Chen Z.;
"Novel genes expressed in hematopoietic stem/progenitor cells from
myelodysplastic syndrome patients.";
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Spleen;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Bone marrow, Brain, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, COFACTOR, AND MUTAGENESIS OF CYS-72; CYS-74; CYS-83; ASP-84
AND HIS-87.
PubMed=17584744; DOI=10.1074/jbc.C700107200;
Wiley S.E., Paddock M.L., Abresch E.C., Gross L., van der Geer P.,
Nechushtai R., Murphy A.N., Jennings P.A., Dixon J.E.;
"The outer mitochondrial membrane protein mitoNEET contains a novel
redox-active 2Fe-2S cluster.";
J. Biol. Chem. 282:23745-23749(2007).
[7]
SUBCELLULAR LOCATION, AND COFACTOR.
PubMed=17376863; DOI=10.1073/pnas.0701078104;
Wiley S.E., Murphy A.N., Ross S.A., van der Geer P., Dixon J.E.;
"MitoNEET is an iron-containing outer mitochondrial membrane protein
that regulates oxidative capacity.";
Proc. Natl. Acad. Sci. U.S.A. 104:5318-5323(2007).
[8]
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=19580816; DOI=10.1016/j.jmb.2009.06.079;
Conlan A.R., Axelrod H.L., Cohen A.E., Abresch E.C., Zuris J., Yee D.,
Nechushtai R., Jennings P.A., Paddock M.L.;
"Crystal structure of Miner1: The redox-active 2Fe-2S protein
causative in Wolfram Syndrome 2.";
J. Mol. Biol. 392:143-153(2009).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[12]
UBIQUITINATION AT LYS-42; LYS-55; LYS-68; LYS-78; LYS-79; LYS-89;
LYS-104; LYS-105 AND LYS-106.
PubMed=25621951; DOI=10.1038/ncb3097;
Cunningham C.N., Baughman J.M., Phu L., Tea J.S., Yu C., Coons M.,
Kirkpatrick D.S., Bingol B., Corn J.E.;
"USP30 and parkin homeostatically regulate atypical ubiquitin chains
on mitochondria.";
Nat. Cell Biol. 17:160-169(2015).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[14]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 33-108, COFACTOR, SUBUNIT,
AND SUBCELLULAR LOCATION.
PubMed=17905743; DOI=10.1074/jbc.C700172200;
Hou X., Liu R., Ross S., Smart E.J., Zhu H., Gong W.;
"Crystallographic studies of human MitoNEET.";
J. Biol. Chem. 282:33242-33246(2007).
[15]
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 33-108, FUNCTION, COFACTOR,
AND SUBUNIT.
PubMed=17766440; DOI=10.1073/pnas.0707189104;
Paddock M.L., Wiley S.E., Axelrod H.L., Cohen A.E., Roy M.,
Abresch E.C., Capraro D., Murphy A.N., Nechushtai R., Dixon J.E.,
Jennings P.A.;
"MitoNEET is a uniquely folded 2Fe 2S outer mitochondrial membrane
protein stabilized by pioglitazone.";
Proc. Natl. Acad. Sci. U.S.A. 104:14342-14347(2007).
[16]
X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 32-108, COFACTOR, SUBUNIT,
AND SUBCELLULAR LOCATION.
PubMed=17766439; DOI=10.1073/pnas.0702426104;
Lin J., Zhou T., Ye K., Wang J.;
"Crystal structure of human mitoNEET reveals distinct groups of iron
sulfur proteins.";
Proc. Natl. Acad. Sci. U.S.A. 104:14640-14645(2007).
-!- FUNCTION: Plays a key role in regulating maximal capacity for
electron transport and oxidative phosphorylation (By similarity).
May be involved in Fe-S cluster shuttling and/or in redox
reactions. {ECO:0000250, ECO:0000269|PubMed:17584744,
ECO:0000269|PubMed:17766440}.
-!- COFACTOR:
Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
Evidence={ECO:0000269|PubMed:17376863,
ECO:0000269|PubMed:17584744, ECO:0000269|PubMed:17766439,
ECO:0000269|PubMed:17766440, ECO:0000269|PubMed:17905743};
Note=Binds 1 [2Fe-2S] cluster per subunit. The [2Fe-2S] cluster is
redox-active and pH labile and is significantly less stable at pH
4.5 as compared with pH 7.0. {ECO:0000269|PubMed:17376863,
ECO:0000269|PubMed:17584744, ECO:0000269|PubMed:17766439,
ECO:0000269|PubMed:17766440, ECO:0000269|PubMed:17905743};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Redox potential:
E is 0 +/- 10 mV for 2Fe-2S at pH 7.5.
{ECO:0000269|PubMed:19580816};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17766439,
ECO:0000269|PubMed:17766440, ECO:0000269|PubMed:17905743}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-1050885, EBI-1050885;
-!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
{ECO:0000269|PubMed:17376863, ECO:0000269|PubMed:17766439,
ECO:0000269|PubMed:17905743, ECO:0000269|PubMed:18047834}; Single-
pass type III membrane protein {ECO:0000269|PubMed:17376863,
ECO:0000269|PubMed:17766439, ECO:0000269|PubMed:17905743,
ECO:0000269|PubMed:18047834}.
-!- TISSUE SPECIFICITY: Expression is reduced in cells derived from
cystic fibrosis patients. {ECO:0000269|PubMed:18047834}.
-!- INDUCTION: Expression is down-regulated by glibenclamide and 5-
[(4-carboxyphenyl)methylene]-2-thioxo-3-(3-trifluoromethyl)phenyl-
4-thiazolidinone (CFTR(inh)172), and up-regulated by
cAMP/isoproterenol/IBMX, components that inhibit and stimulate
chloride transport activity respectively.
{ECO:0000269|PubMed:18047834}.
-!- PTM: Ubiquitinated by PRKN during mitophagy, leading to its
degradation and enhancement of mitophagy. Deubiquitinated by
USP30. {ECO:0000269|PubMed:25621951}.
-!- MISCELLANEOUS: Binds pioglitazone, an anti-diabetes drug. Binding
increases the stability of the 2Fe-2S cluster.
-!- SIMILARITY: Belongs to the CISD protein family. {ECO:0000305}.
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EMBL; AY960578; AAY32336.1; -; mRNA.
EMBL; AF220049; AAF67642.1; -; mRNA.
EMBL; AK312017; BAG34955.1; -; mRNA.
EMBL; CH471083; EAW54163.1; -; Genomic_DNA.
EMBL; BC005962; AAH05962.1; -; mRNA.
EMBL; BC007043; AAH07043.1; -; mRNA.
EMBL; BC008474; AAH08474.1; -; mRNA.
EMBL; BC059168; AAH59168.1; -; mRNA.
CCDS; CCDS7251.1; -.
RefSeq; NP_060934.1; NM_018464.4.
UniGene; Hs.370102; -.
PDB; 2QD0; X-ray; 1.81 A; A/B=32-108.
PDB; 2QH7; X-ray; 1.50 A; A/B=33-108.
PDB; 2R13; X-ray; 1.80 A; A=33-108.
PDB; 3EW0; X-ray; 1.40 A; A/B=33-108.
PDB; 3LPQ; X-ray; 1.70 A; A/B=33-107.
PDB; 3REE; X-ray; 1.76 A; A=32-108.
PDB; 4EZF; X-ray; 1.19 A; A/B=33-108.
PDB; 4F1E; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=33-108.
PDB; 4F28; X-ray; 1.55 A; A/B=33-108.
PDB; 4F2C; X-ray; 1.35 A; A/B=33-108.
PDBsum; 2QD0; -.
PDBsum; 2QH7; -.
PDBsum; 2R13; -.
PDBsum; 3EW0; -.
PDBsum; 3LPQ; -.
PDBsum; 3REE; -.
PDBsum; 4EZF; -.
PDBsum; 4F1E; -.
PDBsum; 4F28; -.
PDBsum; 4F2C; -.
ProteinModelPortal; Q9NZ45; -.
SMR; Q9NZ45; -.
BioGrid; 120949; 30.
DIP; DIP-46446N; -.
IntAct; Q9NZ45; 4.
STRING; 9606.ENSP00000363041; -.
BindingDB; Q9NZ45; -.
ChEMBL; CHEMBL1795168; -.
iPTMnet; Q9NZ45; -.
PhosphoSitePlus; Q9NZ45; -.
SwissPalm; Q9NZ45; -.
BioMuta; CISD1; -.
DMDM; 25453105; -.
EPD; Q9NZ45; -.
MaxQB; Q9NZ45; -.
PaxDb; Q9NZ45; -.
PeptideAtlas; Q9NZ45; -.
PRIDE; Q9NZ45; -.
TopDownProteomics; Q9NZ45; -.
DNASU; 55847; -.
Ensembl; ENST00000333926; ENSP00000363041; ENSG00000122873.
GeneID; 55847; -.
KEGG; hsa:55847; -.
UCSC; uc001jkc.6; human.
CTD; 55847; -.
DisGeNET; 55847; -.
EuPathDB; HostDB:ENSG00000122873.11; -.
GeneCards; CISD1; -.
H-InvDB; HIX0201471; -.
HGNC; HGNC:30880; CISD1.
HPA; CAB045965; -.
HPA; HPA074383; -.
MIM; 611932; gene.
neXtProt; NX_Q9NZ45; -.
OpenTargets; ENSG00000122873; -.
PharmGKB; PA162382289; -.
eggNOG; KOG3461; Eukaryota.
eggNOG; ENOG41122II; LUCA.
GeneTree; ENSGT00390000001233; -.
HOGENOM; HOG000242301; -.
HOVERGEN; HBG052444; -.
InParanoid; Q9NZ45; -.
OMA; KDHRNKS; -.
OrthoDB; EOG091G0XB4; -.
PhylomeDB; Q9NZ45; -.
TreeFam; TF324661; -.
ChiTaRS; CISD1; human.
EvolutionaryTrace; Q9NZ45; -.
GenomeRNAi; 55847; -.
PRO; PR:Q9NZ45; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000122873; -.
CleanEx; HS_CISD1; -.
ExpressionAtlas; Q9NZ45; baseline and differential.
Genevisible; Q9NZ45; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0043457; P:regulation of cellular respiration; IEA:Ensembl.
InterPro; IPR018967; FeS-contain_CDGSH-typ.
InterPro; IPR019610; FeS-contain_mitoNEET_N.
Pfam; PF10660; MitoNEET_N; 1.
Pfam; PF09360; zf-CDGSH; 1.
SMART; SM00704; ZnF_CDGSH; 1.
1: Evidence at protein level;
2Fe-2S; 3D-structure; Acetylation; Complete proteome; Iron;
Iron-sulfur; Isopeptide bond; Membrane; Metal-binding; Mitochondrion;
Mitochondrion outer membrane; Reference proteome; Signal-anchor;
Transmembrane; Transmembrane helix; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 108 CDGSH iron-sulfur domain-containing
protein 1.
/FTId=PRO_0000089803.
TRANSMEM 14 31 Helical; Signal-anchor for type III
membrane protein. {ECO:0000255}.
TOPO_DOM 32 108 Cytoplasmic. {ECO:0000255}.
METAL 72 72 Iron-sulfur (2Fe-2S).
METAL 74 74 Iron-sulfur (2Fe-2S).
METAL 83 83 Iron-sulfur (2Fe-2S).
METAL 87 87 Iron-sulfur (2Fe-2S); via pros nitrogen.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 55 55 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q91WS0}.
MOD_RES 68 68 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q91WS0}.
MOD_RES 104 104 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q91WS0}.
CROSSLNK 42 42 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:25621951}.
CROSSLNK 55 55 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate. {ECO:0000269|PubMed:25621951}.
CROSSLNK 68 68 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate. {ECO:0000269|PubMed:25621951}.
CROSSLNK 78 78 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:25621951}.
CROSSLNK 79 79 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:25621951}.
CROSSLNK 89 89 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:25621951}.
CROSSLNK 104 104 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate. {ECO:0000269|PubMed:25621951}.
CROSSLNK 105 105 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:25621951}.
CROSSLNK 106 106 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:25621951}.
MUTAGEN 72 72 C->S: Abolishes absorption in the 300-500
nm range. {ECO:0000269|PubMed:17584744}.
MUTAGEN 74 74 C->S: Abolishes absorption in the 300-500
nm range. {ECO:0000269|PubMed:17584744}.
MUTAGEN 83 83 C->S: Abolishes absorption in the 300-500
nm range. {ECO:0000269|PubMed:17584744}.
MUTAGEN 84 84 D->N: Does not affect absorption in the
300-500 nm range.
{ECO:0000269|PubMed:17584744}.
MUTAGEN 87 87 H->C: Affects absorption in the 300-500
nm range but it is not reduced. Increased
stability of the 2Fe-2S cluster at low
pH. {ECO:0000269|PubMed:17584744}.
MUTAGEN 87 87 H->Q: Abolishes absorption in the 300-500
nm range. {ECO:0000269|PubMed:17584744}.
STRAND 47 49 {ECO:0000244|PDB:4EZF}.
STRAND 53 66 {ECO:0000244|PDB:4EZF}.
STRAND 68 71 {ECO:0000244|PDB:4EZF}.
STRAND 73 75 {ECO:0000244|PDB:4EZF}.
TURN 78 81 {ECO:0000244|PDB:4EZF}.
HELIX 86 94 {ECO:0000244|PDB:4EZF}.
STRAND 98 104 {ECO:0000244|PDB:4EZF}.
SEQUENCE 108 AA; 12199 MW; 2E47000F0635CBB7 CRC64;
MSLTSSSSVR VEWIAAVTIA AGTAAIGYLA YKRFYVKDHR NKAMINLHIQ KDNPKIVHAF
DMEDLGDKAV YCRCWRSKKF PFCDGAHTKH NEETGDNVGP LIIKKKET


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CSB-EL005442HU Human CDGSH iron-sulfur domain-containing protein 1(CISD1) ELISA kit 96T
CSB-EL005443HU Human CDGSH iron-sulfur domain-containing protein 2(CISD2) ELISA kit 96T
E1998b Human ELISA Kit FOR CDGSH iron-sulfur domain-containing protein 3, mitochondrial 96T
CSB-EL005443MO Mouse CDGSH iron-sulfur domain-containing protein 2(CISD2) ELISA kit 96T
CSB-EL005443BO Bovine CDGSH iron-sulfur domain-containing protein 2(CISD2) ELISA kit 96T
CSB-EL005443HU Human CDGSH iron-sulfur domain-containing protein 2(CISD2) ELISA kit SpeciesHuman 96T
CSB-EL005444HU Human CDGSH iron-sulfur domain-containing protein 3, mitochondrial(CISD3) ELISA kit 96T
CSB-EL005442HU Human CDGSH iron-sulfur domain-containing protein 1(CISD1) ELISA kit SpeciesHuman 96T
CSB-EL005442BO Bovine CDGSH iron-sulfur domain-containing protein 1(CISD1) ELISA kit SpeciesBovine 96T


 

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