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NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial (Complex I-18 kDa) (CI-18 kDa) (Complex I-AQDQ) (CI-AQDQ) (NADH-ubiquinone oxidoreductase 18 kDa subunit)

 NDUS4_HUMAN             Reviewed;         175 AA.
O43181; Q9BS69;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
27-SEP-2017, entry version 156.
RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial;
AltName: Full=Complex I-18 kDa;
Short=CI-18 kDa;
AltName: Full=Complex I-AQDQ;
Short=CI-AQDQ;
AltName: Full=NADH-ubiquinone oxidoreductase 18 kDa subunit;
Flags: Precursor;
Name=NDUFS4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INVOLVEMENT IN MT-C1D.
PubMed=9463323; DOI=10.1086/301716;
van den Heuvel L., Ruitenbeek W., Smeets R., Gelman-Kohan Z.,
Elpeleg O., Loeffen J., Trijbels F., Mariman E., de Bruijn D.,
Smeitink J.;
"Demonstration of a new pathogenic mutation in human complex I
deficiency: a 5-bp duplication in the nuclear gene encoding the 18-kD
(AQDQ) subunit.";
Am. J. Hum. Genet. 62:262-268(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Urinary bladder;
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).
[3]
INVOLVEMENT IN LS.
PubMed=12616398; DOI=10.1007/s00439-002-0884-2;
Benit P., Steffann J., Lebon S., Chretien D., Kadhom N., de Lonlay P.,
Goldenberg A., Dumez Y., Dommergues M., Rustin P., Munnich A.,
Roetig A.;
"Genotyping microsatellite DNA markers at putative disease loci in
inbred/multiplex families with respiratory chain complex I deficiency
allows rapid identification of a novel nonsense mutation (IVS1nt -1)
in the NDUFS4 gene in Leigh syndrome.";
Hum. Genet. 112:563-566(2003).
[4]
IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX,
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR
LOCATION.
PubMed=12611891; DOI=10.1074/jbc.C300064200;
Murray J., Zhang B., Taylor S.W., Oglesbee D., Fahy E., Marusich M.F.,
Ghosh S.S., Capaldi R.A.;
"The subunit composition of the human NADH dehydrogenase obtained by
rapid one-step immunopurification.";
J. Biol. Chem. 278:13619-13622(2003).
[5]
INVOLVEMENT IN LS.
PubMed=19107570; DOI=10.1007/s10545-008-1049-9;
Anderson S.L., Chung W.K., Frezzo J., Papp J.C., Ekstein J.,
DiMauro S., Rubin B.Y.;
"A novel mutation in NDUFS4 causes Leigh syndrome in an Ashkenazi
Jewish family.";
J. Inherit. Metab. Dis. 31:S461-S467(2008).
[6]
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).
[7]
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).
[8]
IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX.
PubMed=27626371; DOI=10.1038/nature19754;
Stroud D.A., Surgenor E.E., Formosa L.E., Reljic B., Frazier A.E.,
Dibley M.G., Osellame L.D., Stait T., Beilharz T.H., Thorburn D.R.,
Salim A., Ryan M.T.;
"Accessory subunits are integral for assembly and function of human
mitochondrial complex I.";
Nature 538:123-126(2016).
[9]
VARIANT MT-C1D 97-TRP--LYS-175 DEL, AND VARIANT LS 106-ARG--LYS-175
DEL.
PubMed=10944442; DOI=10.1006/bbrc.2000.3257;
Budde S.M., van den Heuvel L.P., Janssen A.J., Smeets R.J.,
Buskens C.A., DeMeirleir L., Van Coster R., Baethmann M., Voit T.,
Trijbels J.M., Smeitink J.A.;
"Combined enzymatic complex I and III deficiency associated with
mutations in the nuclear encoded NDUFS4 gene.";
Biochem. Biophys. Res. Commun. 275:63-68(2000).
[10]
VARIANT MT-C1D 15-TRP--LYS-175 DEL.
PubMed=11181577;
Petruzzella V., Vergari R., Puzziferri I., Boffoli D., Lamantea E.,
Zeviani M., Papa S.;
"A nonsense mutation in the NDUFS4 gene encoding the 18 kDa (AQDQ)
subunit of complex I abolishes assembly and activity of the complex in
a patient with Leigh-like syndrome.";
Hum. Mol. Genet. 10:529-535(2001).
[11]
VARIANT LS HIS-119.
PubMed=19364667; DOI=10.1016/j.ymgme.2009.03.002;
Leshinsky-Silver E., Lebre A.S., Minai L., Saada A., Steffann J.,
Cohen S., Roetig A., Munnich A., Lev D., Lerman-Sagie T.;
"NDUFS4 mutations cause Leigh syndrome with predominant brainstem
involvement.";
Mol. Genet. Metab. 97:185-189(2009).
-!- FUNCTION: Accessory subunit of the mitochondrial membrane
respiratory chain NADH dehydrogenase (Complex I), that is believed
not to be involved in 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. {ECO:0000269|PubMed:12611891,
ECO:0000269|PubMed:9463323}.
-!- SUBUNIT: Mammalian complex I is composed of 45 different subunits.
This is a component of the iron-sulfur (IP) fragment of the
enzyme. {ECO:0000269|PubMed:12611891,
ECO:0000269|PubMed:27626371}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000269|PubMed:12611891}; Peripheral membrane protein
{ECO:0000269|PubMed:12611891}; Matrix side
{ECO:0000269|PubMed:12611891}.
-!- DISEASE: Mitochondrial complex I deficiency (MT-C1D) [MIM:252010]:
A disorder of the mitochondrial respiratory chain that causes a
wide range of clinical manifestations from lethal neonatal disease
to adult-onset neurodegenerative disorders. Phenotypes include
macrocephaly with progressive leukodystrophy, non-specific
encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh
syndrome, Leber hereditary optic neuropathy, and some forms of
Parkinson disease. {ECO:0000269|PubMed:10944442,
ECO:0000269|PubMed:11181577, ECO:0000269|PubMed:9463323}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Leigh syndrome (LS) [MIM:256000]: An early-onset
progressive neurodegenerative disorder characterized by the
presence of focal, bilateral lesions in one or more areas of the
central nervous system including the brainstem, thalamus, basal
ganglia, cerebellum and spinal cord. Clinical features depend on
which areas of the central nervous system are involved and include
subacute onset of psychomotor retardation, hypotonia, ataxia,
weakness, vision loss, eye movement abnormalities, seizures, and
dysphagia. {ECO:0000269|PubMed:10944442,
ECO:0000269|PubMed:12616398, ECO:0000269|PubMed:19107570,
ECO:0000269|PubMed:19364667}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the complex I NDUFS4 subunit family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF020351; AAB87865.1; -; mRNA.
EMBL; BC005270; AAH05270.1; -; mRNA.
CCDS; CCDS3960.1; -.
RefSeq; NP_002486.1; NM_002495.3.
UniGene; Hs.528222; -.
ProteinModelPortal; O43181; -.
SMR; O43181; -.
BioGrid; 110803; 83.
CORUM; O43181; -.
IntAct; O43181; 26.
STRING; 9606.ENSP00000296684; -.
ChEMBL; CHEMBL2363065; -.
DrugBank; DB00157; NADH.
iPTMnet; O43181; -.
PhosphoSitePlus; O43181; -.
BioMuta; NDUFS4; -.
UCD-2DPAGE; O43181; -.
EPD; O43181; -.
MaxQB; O43181; -.
PaxDb; O43181; -.
PeptideAtlas; O43181; -.
PRIDE; O43181; -.
TopDownProteomics; O43181; -.
DNASU; 4724; -.
Ensembl; ENST00000296684; ENSP00000296684; ENSG00000164258.
GeneID; 4724; -.
KEGG; hsa:4724; -.
UCSC; uc003jpe.3; human.
CTD; 4724; -.
DisGeNET; 4724; -.
EuPathDB; HostDB:ENSG00000164258.11; -.
GeneCards; NDUFS4; -.
HGNC; HGNC:7711; NDUFS4.
HPA; HPA003884; -.
MalaCards; NDUFS4; -.
MIM; 252010; phenotype.
MIM; 256000; phenotype.
MIM; 602694; gene.
neXtProt; NX_O43181; -.
OpenTargets; ENSG00000164258; -.
Orphanet; 2609; Isolated NADH-CoQ reductase deficiency.
Orphanet; 255241; Leigh syndrome with leukodystrophy.
PharmGKB; PA31521; -.
eggNOG; KOG3389; Eukaryota.
eggNOG; ENOG4111TR4; LUCA.
GeneTree; ENSGT00390000013835; -.
HOGENOM; HOG000140414; -.
HOVERGEN; HBG003007; -.
InParanoid; O43181; -.
KO; K03937; -.
OMA; PLKHIRT; -.
OrthoDB; EOG091G0LT1; -.
PhylomeDB; O43181; -.
TreeFam; TF105619; -.
Reactome; R-HSA-611105; Respiratory electron transport.
Reactome; R-HSA-6799198; Complex I biogenesis.
ChiTaRS; NDUFS4; human.
GeneWiki; NDUFS4; -.
GenomeRNAi; 4724; -.
PRO; PR:O43181; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000164258; -.
CleanEx; HS_NDUFS4; -.
ExpressionAtlas; O43181; baseline and differential.
Genevisible; O43181; HS.
GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IMP:UniProtKB.
GO; GO:0007420; P:brain development; IMP:UniProtKB.
GO; GO:0019933; P:cAMP-mediated signaling; IMP:UniProtKB.
GO; GO:0045333; P:cellular respiration; IMP:UniProtKB.
GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; TAS:Reactome.
GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IMP:UniProtKB.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:UniProtKB.
GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:UniProtKB.
GO; GO:0001932; P:regulation of protein phosphorylation; IMP:MGI.
GO; GO:0051591; P:response to cAMP; IMP:UniProtKB.
InterPro; IPR006885; NADH_UbQ_FeS_4_mit.
PANTHER; PTHR12219; PTHR12219; 1.
Pfam; PF04800; ETC_C1_NDUFA4; 1.
1: Evidence at protein level;
Complete proteome; Disease mutation; Electron transport;
Leigh syndrome; Membrane; Mitochondrion; Mitochondrion inner membrane;
Polymorphism; Primary mitochondrial disease; Reference proteome;
Respiratory chain; Transit peptide; Transport.
TRANSIT 1 42 Mitochondrion. {ECO:0000250}.
CHAIN 43 175 NADH dehydrogenase [ubiquinone] iron-
sulfur protein 4, mitochondrial.
/FTId=PRO_0000020038.
VARIANT 15 175 Missing (in MT-C1D).
{ECO:0000269|PubMed:11181577}.
/FTId=VAR_078943.
VARIANT 97 175 Missing (in MT-C1D).
{ECO:0000269|PubMed:10944442}.
/FTId=VAR_078944.
VARIANT 106 175 Missing (in LS).
{ECO:0000269|PubMed:10944442}.
/FTId=VAR_078945.
VARIANT 119 119 D -> H (in LS; dbSNP:rs747359752).
{ECO:0000269|PubMed:19364667}.
/FTId=VAR_078946.
VARIANT 174 174 T -> P (in dbSNP:rs1044692).
/FTId=VAR_012037.
CONFLICT 39 39 T -> S (in Ref. 2; AAH05270).
{ECO:0000305}.
SEQUENCE 175 AA; 20108 MW; DE5B51DBDD76231E CRC64;
MAAVSMSVVL RQTLWRRRAV AVAALSVSRV PTRSLRTSTW RLAQDQTQDT QLITVDEKLD
ITTLTGVPEE HIKTRKVRIF VPARNNMQSG VNNTKKWKME FDTRERWENP LMGWASTADP
LSNMVLTFST KEDAVSFAEK NGWSYDIEER KVPKPKSKSY GANFSWNKRT RVSTK


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