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UniProtKB/Swiss-Prot entry P28331


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NDUS1_HUMAN
Primary accession number P28331
Secondary accession numbers Q53TR8 Q8N1C4 Q8TCC9
Integrated into Swiss-Prot on December 1, 1992
Sequence was last modified on March 7, 2006 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 96)
Name and origin of the protein
Protein name NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial [Precursor]
Synonyms EC 1.6.5.3
EC 1.6.99.3
Complex I-75kD
CI-75kD
Gene name
Name: NDUFS1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PHE-649.
PubMed=1935949 [NCBI, ExPASy, EBI, Israel, Japan]
Chow W., Ragan I., Robinson B.H.;
"Determination of the cDNA sequence for the human mitochondrial 75-kDa Fe-S protein of NADH-coenzyme Q reductase.";
Eur. J. Biochem. 201:547-550(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03466; PubMed=15815621 [NCBI, ExPASy, EBI, Israel, Japan]
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and 4.";
Nature 434:724-731(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-241.
TISSUE=Brain, and Liver;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[4]
PROTEIN SEQUENCE OF 185-200 AND 519-538, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[5]
VARIANTS COMPLEX I DEFICIENCY TRP-241 AND GLY-252.
DOI=10.1086/320603; PubMed=11349233 [NCBI, ExPASy, EBI, Israel, Japan]
Benit P., Chretien D., Kadhom N., de Lonlay-Debeney P., Cormier-Daire V., Cabral A., Peudenier S., Rustin P., Munnich A., Roetig A.;
"Large-scale deletion and point mutations of the nuclear NDUFV1 and NDUFS1 genes in mitochondrial complex I deficiency.";
Am. J. Hum. Genet. 68:1344-1352(2001).
Comments
  • FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). This is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized.
  • CATALYTIC ACTIVITY: NADH + ubiquinone = NAD+ + ubiquinol.
  • CATALYTIC ACTIVITY: NADH + acceptor = NAD+ + reduced acceptor.
  • COFACTOR: Binds 1 2Fe-2S cluster per subunit (By similarity).
  • COFACTOR: Binds 2 4Fe-4S clusters per subunit (By similarity).
  • SUBUNIT: Complex I is composed of 45 different subunits.
  • SUBCELLULAR LOCATION: Mitochondrion inner membrane.
  • DISEASE: Defects in NDUFS1 are a cause of complex I mitochondrial respiratory chain deficiency [MIM:252010]. Complex I (NADH-ubiquinone oxidoreductase), the largest complex of the mitochondrial respiratory chain, contains more than 40 subunits. It is embedded in the inner mitochondrial membrane and is partly protruding in the matrix. Complex I deficiency is the most common cause of mitochondrial disorders. It represents largely one-third of all cases of respiratory chain deficiency and is responsible for a variety of clinical symptoms, ranging from neurological disorders to cardiomyopathy, liver failure, and myopathy.
  • SIMILARITY: Belongs to the complex I 75 kDa subunit family.
  • SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain.
  • WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=NDUFS1";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X61100; CAA43412.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC007383; AAY15061.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC022368; AAH22368.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC030833; AAH30833.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S17854; S17854.
RefSeq NP_004997.4; -.
UniGene Hs.471207
3D structure databases
ModBase P28331.
Protein-protein interaction databases
IntAct P28331; -.
PTM databases
PhosphoSite P28331; -.
Enzyme and pathway databases
Reactome REACT_6305; Electron Transport Chain.
2D gel databases
REPRODUCTION-2DPAGE IPI00604664; -.
P28331; -.
Organism-specific databases
H-InvDB HIX0002769; -.
HGNC HGNC:7707; NDUFS1.
GenAtlas NDUFS1.
MIM 157655; gene. [NCBI / EBI]
252010; phenotype. [NCBI / EBI]
Orphanet 506; Leigh syndrome.
2609; NADH-CoQ reductase deficiency.
PharmGKB PA31518; -.
GeneCards P28331.
Gene expression databases
ArrayExpress P28331; -.
CleanEx HS_NDUFS1; -.
GermOnline ENSG00000023228; Homo sapiens.
Ontologies
GO
GO:0005758; Cellular component: mitochondrial intermembrane space (inferred from direct assay from UniProtKB).
GO:0005747; Cellular component: mitochondrial respiratory chain complex I (inferred from mutant phenotype from UniProtKB).
GO:0051537; Molecular function: 2 iron, 2 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051539; Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009055; Molecular function: electron carrier activity (non-traceable author statement from UniProtKB).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008137; Molecular function: NADH dehydrogenase (ubiquinone) activity (non-traceable author statement from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0006915; Biological process: apoptosis (inferred from direct assay from UniProtKB).
GO:0046034; Biological process: ATP metabolic process (inferred from mutant phenotype from UniProtKB).
GO:0045333; Biological process: cellular respiration (inferred from mutant phenotype from UniProtKB).
GO:0006120; Biological process: mitochondrial electron transport, NADH to ubiquinone (non-traceable author statement from UniProtKB).
GO:0006800; Biological process: oxygen and reactive oxygen species metabolic process (inferred from mutant phenotype from UniProtKB).
GO:0051881; Biological process: regulation of mitochondrial membrane potential (inferred from mutant phenotype from UniProtKB).
GO:0006810; Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR006058; 2Fe2S_fd_BS.
IPR001041; Ferredoxin.
IPR006656; Mopterin_OxRdtase.
IPR000283; NADH_DHase_75KDa_su_CS.
IPR010228; NADH_quinone_OxRdtase_G.
IPR015405; NuoG_C.
Graphical view of domain structure.
Pfam PF09326; DUF1982; 1.
PF00111; Fer2; 1.
PF00384; Molybdopterin; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01973; NuoG; 1.
PROSITE PS00197; 2FE2S_FER_1; FALSE_NEG.
PS51085; 2FE2S_FER_2; 1.
PS00641; COMPLEX1_75K_1; 1.
PS00642; COMPLEX1_75K_2; 1.
PS00643; COMPLEX1_75K_3; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P28331.
ProtoNet P28331.
Proteomic databases
PeptideAtlas P28331; -.
Genome annotation databases
Ensembl ENSG00000023228; Homo sapiens. [Contig view]
GeneID 4719; -.
KEGG hsa:4719; -.
NMPDR fig|9606.3.peg.19217; -.
Phylogenomic databases
HOVERGEN P28331; -.
Other
DrugBank DB00157; NADH.
NextBio 18202; -.
SOURCE NDUFS1; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
2Fe-2S; 4Fe-4S; Acetylation; Direct protein sequencing; Disease mutation; Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; NAD; Oxidoreductase; Polymorphism; Respiratory chain; Transit peptide; Transport; Ubiquinone.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    23  23     Mitochondrion (By similarity). 
CHAIN   24   727  704     NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial. PRO_0000019968
DOMAIN   30   108  79     2Fe-2S ferredoxin-type. 
METAL   64    64        Iron-sulfur 1 (2Fe-2S) (By similarity). 
METAL   75    75        Iron-sulfur 1 (2Fe-2S) (By similarity). 
METAL   78    78        Iron-sulfur 1 (2Fe-2S) (By similarity). 
METAL   92    92        Iron-sulfur 1 (2Fe-2S) (By similarity). 
METAL   124   124        Iron-sulfur 2 (4Fe-4S); via pros nitrogen (By similarity). 
METAL   128   128        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   131   131        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   137   137        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   176   176        Iron-sulfur 3 (4Fe-4S) (By similarity). 
METAL   179   179        Iron-sulfur 3 (4Fe-4S) (By similarity). 
METAL   182   182        Iron-sulfur 3 (4Fe-4S) (By similarity). 
METAL   226   226        Iron-sulfur 3 (4Fe-4S) (By similarity). 
MOD_RES   84    84        N6-acetyllysine (By similarity). 
VARIANT   241   241  1     R -> Q (in dbSNP:rs17856901 [NCBI]). VAR_025511 
VARIANT   241   241  1     R -> W (in complex I deficiency). VAR_019532 
VARIANT   252   252  1     D -> G (in complex I deficiency). VAR_019533 
VARIANT   649   649  1     V -> F (in dbSNP:rs1044049 [NCBI]). VAR_018463 
CONFLICT   8     8        K -> R (in Ref. 1; CAA43412). 
CONFLICT   417   417        R -> W (in Ref. 1; CAA43412). 
CONFLICT   691   691        I -> L (in Ref. 1; CAA43412). 
Sequence information
Length: 727 AA [This is the length of the unprocessed precursor] Molecular weight: 79468 Da [This is the MW of the unprocessed precursor] CRC64: 9C35F4B8294771FB [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLRIPVRKAL VGLSKSPKGC VRTTATAASN LIEVFVDGQS VMVEPGTTVL QACEKVGMQI 

        70         80         90        100        110        120 
PRFCYHERLS VAGNCRMCLV EIEKAPKVVA ACAMPVMKGW NILTNSEKSK KAREGVMEFL 

       130        140        150        160        170        180 
LANHPLDCPI CDQGGECDLQ DQSMMFGNDR SRFLEGKRAV EDKNIGPLVK TIMTRCIQCT 

       190        200        210        220        230        240 
RCIRFASEIA GVDDLGTTGR GNDMQVGTYI EKMFMSELSG NIIDICPVGA LTSKPYAFTA 

       250        260        270        280        290        300 
RPWETRKTES IDVMDAVGSN IVVSTRTGEV MRILPRMHED INEEWISDKT RFAYDGLKRQ 

       310        320        330        340        350        360 
RLTEPMVRNE KGLLTYTSWE DALSRVAGML QSFQGKDVAA IAGGLVDAEA LVALKDLLNR 

       370        380        390        400        410        420 
VDSDTLCTEE VFPTAGAGTD LRSNYLLNTT IAGVEEADVV LLVGTNPRFE APLFNARIRK 

       430        440        450        460        470        480 
SWLHNDLKVA LIGSPVDLTY TYDHLGDSPK ILQDIASGSH PFSQVLKEAK KPMVVLGSSA 

       490        500        510        520        530        540 
LQRNDGAAIL AAVSSIAQKI RMTSGVTGDW KVMNILHRIA SQVAALDLGY KPGVEAIRKN 

       550        560        570        580        590        600 
PPKVLFLLGA DGGCITRQDL PKDCFIIYQG HHGDVGAPIA DVILPGAAYT EKSATYVNTE 

       610        620        630        640        650        660 
GRAQQTKVAV TPPGLAREDW KIIRALSEIA GMTLPYDTLD QVRNRLEEVS PNLVRYDDIE 

       670        680        690        700        710        720 
GANYFQQANE LSKLVNQQLL ADPLVPPQLT IKDFYMTDSI SRASQTMAKC VKAVTEGAQA 


VEEPSIC 

P28331 in FASTA format

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