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Q9NZ45 (CISD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CDGSH iron-sulfur domain-containing protein 1
Alternative name(s):
MitoNEET
Gene names
Name:CISD1
Synonyms:C10orf70, ZCD1
ORF Names:MDS029
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length108 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.6 Ref.12

Cofactor

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. Ref.6 Ref.7 Ref.11 Ref.12 Ref.13

Subunit structure

Homodimer. Ref.11 Ref.12 Ref.13

Subcellular location

Mitochondrion outer membrane; Single-pass type III membrane protein Ref.1 Ref.7 Ref.11 Ref.13.

Tissue specificity

Expression is reduced in cells derived from cystic fibrosis patients. Ref.1

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. Ref.1

Miscellaneous

Binds pioglitazone, an anti-diabetes drug. Binding increases the stability of the 2Fe-2S cluster.

Sequence similarities

Belongs to the CISD protein family.

Biophysicochemical properties

Redox potential:

E is 0 +/- 10 mV for 2Fe-2S at pH 7.5. Ref.8

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 108107CDGSH iron-sulfur domain-containing protein 1
PRO_0000089803

Regions

Transmembrane14 – 3118Helical; Signal-anchor for type III membrane protein; Potential
Topological domain32 – 10877Cytoplasmic Potential

Sites

Metal binding721Iron-sulfur (2Fe-2S)
Metal binding741Iron-sulfur (2Fe-2S)
Metal binding831Iron-sulfur (2Fe-2S)
Metal binding871Iron-sulfur (2Fe-2S); via pros nitrogen

Amino acid modifications

Modified residue21N-acetylserine Ref.10
Modified residue551N6-acetyllysine By similarity
Modified residue681N6-acetyllysine By similarity
Modified residue1041N6-acetyllysine By similarity

Experimental info

Mutagenesis721C → S: Abolishes absorption in the 300-500 nm range. Ref.6
Mutagenesis741C → S: Abolishes absorption in the 300-500 nm range. Ref.6
Mutagenesis831C → S: Abolishes absorption in the 300-500 nm range. Ref.6
Mutagenesis841D → N: Does not affect absorption in the 300-500 nm range. Ref.6
Mutagenesis871H → C: Affects absorption in the 300-500 nm range but it is not reduced. Increased stability of the 2Fe-2S cluster at low pH. Ref.6
Mutagenesis871H → Q: Abolishes absorption in the 300-500 nm range. Ref.6

Secondary structure

............... 108
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9NZ45 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 2E47000F0635CBB7

FASTA10812,199
        10         20         30         40         50         60 
MSLTSSSSVR VEWIAAVTIA AGTAAIGYLA YKRFYVKDHR NKAMINLHIQ KDNPKIVHAF 

        70         80         90        100 
DMEDLGDKAV YCRCWRSKKF PFCDGAHTKH NEETGDNVGP LIIKKKET 

« Hide

References

« Hide 'large scale' references
[1]"CISD1 codifies a mitochondrial protein upregulated by the CFTR channel."
Taminelli G.L., Sotomayor V., Valdivieso A.G., Teiber M.L., Marin M.C., Santa-Coloma T.A.
Biochem. Biophys. Res. Commun. 365:856-862(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
[2]"Novel genes expressed in hematopoietic stem/progenitor cells from myelodysplastic syndrome patients."
Zhao M., Gu J., Li N., Peng Y., Han Z., Chen Z.
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Hematopoietic stem cell.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Spleen.
[4]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Bone marrow, Brain and Lung.
[6]"The outer mitochondrial membrane protein mitoNEET contains a novel redox-active 2Fe-2S cluster."
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.
J. Biol. Chem. 282:23745-23749(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, COFACTOR, MUTAGENESIS OF CYS-72; CYS-74; CYS-83; ASP-84 AND HIS-87.
[7]"MitoNEET is an iron-containing outer mitochondrial membrane protein that regulates oxidative capacity."
Wiley S.E., Murphy A.N., Ross S.A., van der Geer P., Dixon J.E.
Proc. Natl. Acad. Sci. U.S.A. 104:5318-5323(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, COFACTOR.
[8]"Crystal structure of Miner1: The redox-active 2Fe-2S protein causative in Wolfram Syndrome 2."
Conlan A.R., Axelrod H.L., Cohen A.E., Abresch E.C., Zuris J., Yee D., Nechushtai R., Jennings P.A., Paddock M.L.
J. Mol. Biol. 392:143-153(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[11]"Crystallographic studies of human MitoNEET."
Hou X., Liu R., Ross S., Smart E.J., Zhu H., Gong W.
J. Biol. Chem. 282:33242-33246(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 33-108, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
[12]"MitoNEET is a uniquely folded 2Fe 2S outer mitochondrial membrane protein stabilized by pioglitazone."
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.
Proc. Natl. Acad. Sci. U.S.A. 104:14342-14347(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 33-108, FUNCTION, COFACTOR, SUBUNIT.
[13]"Crystal structure of human mitoNEET reveals distinct groups of iron sulfur proteins."
Lin J., Zhou T., Ye K., Wang J.
Proc. Natl. Acad. Sci. U.S.A. 104:14640-14645(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 32-108, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY960578 mRNA. Translation: AAY32336.1.
AF220049 mRNA. Translation: AAF67642.1.
AK312017 mRNA. Translation: BAG34955.1.
CH471083 Genomic DNA. Translation: EAW54163.1.
BC005962 mRNA. Translation: AAH05962.1.
BC007043 mRNA. Translation: AAH07043.1.
BC008474 mRNA. Translation: AAH08474.1.
BC059168 mRNA. Translation: AAH59168.1.
CCDSCCDS7251.1.
RefSeqNP_060934.1. NM_018464.4.
UniGeneHs.370102.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QD0X-ray1.81A/B32-108[»]
2QH7X-ray1.50A/B33-108[»]
2R13X-ray1.80A33-108[»]
3EW0X-ray1.40A/B33-108[»]
3LPQX-ray1.70A/B33-107[»]
3REEX-ray1.76A32-108[»]
4EZFX-ray1.19A/B33-108[»]
4F1EX-ray2.40A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R33-108[»]
4F28X-ray1.55A/B33-108[»]
4F2CX-ray1.35A/B33-108[»]
ProteinModelPortalQ9NZ45.
SMRQ9NZ45. Positions 33-107.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120949. 8 interactions.
DIPDIP-46446N.
IntActQ9NZ45. 2 interactions.
STRING9606.ENSP00000363041.

Chemistry

BindingDBQ9NZ45.
ChEMBLCHEMBL1795168.

PTM databases

PhosphoSiteQ9NZ45.

Polymorphism databases

DMDM25453105.

Proteomic databases

MaxQBQ9NZ45.
PaxDbQ9NZ45.
PeptideAtlasQ9NZ45.
PRIDEQ9NZ45.

Protocols and materials databases

DNASU55847.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000333926; ENSP00000363041; ENSG00000122873.
GeneID55847.
KEGGhsa:55847.
UCSCuc001jkc.5. human.

Organism-specific databases

CTD55847.
GeneCardsGC10P060028.
H-InvDBHIX0201471.
HGNCHGNC:30880. CISD1.
HPACAB045965.
MIM611932. gene.
neXtProtNX_Q9NZ45.
PharmGKBPA162382289.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG236423.
HOGENOMHOG000242301.
HOVERGENHBG052444.
InParanoidQ9NZ45.
OMAKDHRNKS.
OrthoDBEOG7GQXZ6.
PhylomeDBQ9NZ45.
TreeFamTF324661.

Gene expression databases

BgeeQ9NZ45.
CleanExHS_CISD1.
GenevestigatorQ9NZ45.

Family and domain databases

InterProIPR018967. FeS-contain_CDGSH-typ.
IPR006622. FeS-contain_CDGSH-typ_subfam.
IPR019610. FeS-contain_mitoNEET_N.
[Graphical view]
PfamPF10660. MitoNEET_N. 1 hit.
PF09360. zf-CDGSH. 1 hit.
[Graphical view]
SMARTSM00704. ZnF_CDGSH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCISD1. human.
EvolutionaryTraceQ9NZ45.
GenomeRNAi55847.
NextBio61099.
PROQ9NZ45.
SOURCESearch...

Entry information

Entry nameCISD1_HUMAN
AccessionPrimary (citable) accession number: Q9NZ45
Secondary accession number(s): Q1X902
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM