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NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial (EC 1.6.5.3) (EC 1.6.99.3) (Complex I-75kD) (CI-75kD)

 NDUS1_HUMAN             Reviewed;         727 AA.
P28331; B4DIN9; B4DJA0; B4DPG1; B4DUC1; E7ENF3; Q53TR8; Q8N1C4;
Q8TCC9;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
07-MAR-2006, sequence version 3.
27-SEP-2017, entry version 192.
RecName: Full=NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial;
EC=1.6.5.3;
EC=1.6.99.3;
AltName: Full=Complex I-75kD;
Short=CI-75kD;
Flags: Precursor;
Name=NDUFS1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT PHE-649.
PubMed=1935949; DOI=10.1111/j.1432-1033.1991.tb16313.x;
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 MRNA] (ISOFORMS 1; 3; 4 AND 5).
TISSUE=Hippocampus, Kidney, and Substantia nigra;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton 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] (ISOFORM 1), AND VARIANT
GLN-241.
TISSUE=Brain, and Liver;
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]
PROTEIN SEQUENCE OF 185-200; 247-266; 277-289; 312-325; 361-382;
451-467; 471-499; 519-538; 544-557 AND 625-655, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[7]
IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX, AND
IDENTIFICATION BY MASS SPECTROMETRY.
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).
[8]
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).
[9]
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).
[10]
CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER THR-23, AND
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).
[11]
VARIANTS MT-C1D TRP-241 AND GLY-252.
PubMed=11349233; DOI=10.1086/320603;
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).
[12]
VARIANT GLY-253.
PubMed=22499341; DOI=10.1136/jmedgenet-2012-100836;
Shamseldin H.E., Alshammari M., Al-Sheddi T., Salih M.A.,
Alkhalidi H., Kentab A., Repetto G.M., Hashem M., Alkuraya F.S.;
"Genomic analysis of mitochondrial diseases in a consanguineous
population reveals novel candidate disease genes.";
J. Med. Genet. 49:234-241(2012).
-!- 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. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: NADH + ubiquinone + 5 H(+)(In) = NAD(+) +
ubiquinol + 4 H(+)(Out).
-!- CATALYTIC ACTIVITY: NADH + acceptor = NAD(+) + reduced acceptor.
-!- COFACTOR:
Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
Evidence={ECO:0000250};
Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000250};
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000250};
Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000250};
-!- SUBUNIT: Complex I is composed of 45 different subunits.
{ECO:0000269|PubMed:12611891}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=P28331-1; Sequence=Displayed;
Name=2;
IsoId=P28331-2; Sequence=VSP_042682;
Note=No experimental confirmation available.;
Name=3;
IsoId=P28331-3; Sequence=VSP_043728, VSP_043729;
Note=No experimental confirmation available.;
Name=4;
IsoId=P28331-4; Sequence=VSP_043727;
Note=No experimental confirmation available.;
Name=5;
IsoId=P28331-5; Sequence=VSP_045864;
Note=No experimental confirmation available.;
-!- 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:11349233}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
{ECO:0000305}.
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EMBL; X61100; CAA43412.1; -; mRNA.
EMBL; AK295705; BAG58551.1; -; mRNA.
EMBL; AK295987; BAG58762.1; -; mRNA.
EMBL; AK298320; BAG60573.1; -; mRNA.
EMBL; AK300585; BAG62283.1; -; mRNA.
EMBL; AC007383; AAY15061.1; -; Genomic_DNA.
EMBL; CH471063; EAW70379.1; -; Genomic_DNA.
EMBL; BC022368; AAH22368.1; -; mRNA.
EMBL; BC030833; AAH30833.1; -; mRNA.
CCDS; CCDS2366.1; -. [P28331-1]
CCDS; CCDS56162.1; -. [P28331-4]
CCDS; CCDS56163.1; -. [P28331-3]
CCDS; CCDS56164.1; -. [P28331-5]
CCDS; CCDS56165.1; -. [P28331-2]
PIR; S17854; S17854.
RefSeq; NP_001186910.1; NM_001199981.1. [P28331-5]
RefSeq; NP_001186911.1; NM_001199982.1. [P28331-3]
RefSeq; NP_001186912.1; NM_001199983.1. [P28331-4]
RefSeq; NP_001186913.1; NM_001199984.1. [P28331-2]
RefSeq; NP_004997.4; NM_005006.6. [P28331-1]
UniGene; Hs.471207; -.
UniGene; Hs.598436; -.
ProteinModelPortal; P28331; -.
SMR; P28331; -.
BioGrid; 110799; 93.
CORUM; P28331; -.
IntAct; P28331; 52.
MINT; MINT-3011123; -.
STRING; 9606.ENSP00000392709; -.
ChEMBL; CHEMBL2363065; -.
DrugBank; DB00157; NADH.
iPTMnet; P28331; -.
PhosphoSitePlus; P28331; -.
SwissPalm; P28331; -.
BioMuta; NDUFS1; -.
DMDM; 92090799; -.
REPRODUCTION-2DPAGE; IPI00604664; -.
REPRODUCTION-2DPAGE; P28331; -.
UCD-2DPAGE; P28331; -.
EPD; P28331; -.
MaxQB; P28331; -.
PaxDb; P28331; -.
PeptideAtlas; P28331; -.
PRIDE; P28331; -.
Ensembl; ENST00000233190; ENSP00000233190; ENSG00000023228. [P28331-1]
Ensembl; ENST00000423725; ENSP00000397760; ENSG00000023228. [P28331-4]
Ensembl; ENST00000432169; ENSP00000409689; ENSG00000023228. [P28331-3]
Ensembl; ENST00000440274; ENSP00000409766; ENSG00000023228. [P28331-5]
Ensembl; ENST00000449699; ENSP00000399912; ENSG00000023228. [P28331-1]
Ensembl; ENST00000455934; ENSP00000392709; ENSG00000023228. [P28331-2]
Ensembl; ENST00000635748; ENSP00000489640; ENSG00000283447. [P28331-1]
Ensembl; ENST00000636505; ENSP00000490898; ENSG00000283447. [P28331-1]
Ensembl; ENST00000637298; ENSP00000490583; ENSG00000283447. [P28331-4]
Ensembl; ENST00000637631; ENSP00000489705; ENSG00000283447. [P28331-3]
Ensembl; ENST00000637733; ENSP00000490092; ENSG00000283447. [P28331-2]
Ensembl; ENST00000637990; ENSP00000490766; ENSG00000283447. [P28331-5]
GeneID; 4719; -.
KEGG; hsa:4719; -.
UCSC; uc002vbe.4; human. [P28331-1]
CTD; 4719; -.
DisGeNET; 4719; -.
EuPathDB; HostDB:ENSG00000023228.13; -.
GeneCards; NDUFS1; -.
HGNC; HGNC:7707; NDUFS1.
HPA; CAB070844; -.
HPA; HPA064605; -.
MalaCards; NDUFS1; -.
MIM; 157655; gene.
MIM; 252010; phenotype.
neXtProt; NX_P28331; -.
OpenTargets; ENSG00000023228; -.
Orphanet; 2609; Isolated NADH-CoQ reductase deficiency.
Orphanet; 255241; Leigh syndrome with leukodystrophy.
PharmGKB; PA31518; -.
eggNOG; KOG2282; Eukaryota.
eggNOG; COG1034; LUCA.
GeneTree; ENSGT00390000018768; -.
HOGENOM; HOG000031442; -.
HOVERGEN; HBG003482; -.
InParanoid; P28331; -.
KO; K03934; -.
OMA; PQASCAM; -.
OrthoDB; EOG091G02C2; -.
PhylomeDB; P28331; -.
TreeFam; TF105756; -.
Reactome; R-HSA-611105; Respiratory electron transport.
Reactome; R-HSA-6799198; Complex I biogenesis.
ChiTaRS; NDUFS1; human.
GeneWiki; NDUFS1; -.
GenomeRNAi; 4719; -.
PMAP-CutDB; P28331; -.
PRO; PR:P28331; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000023228; -.
CleanEx; HS_NDUFS1; -.
ExpressionAtlas; P28331; baseline and differential.
Genevisible; P28331; HS.
GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0009055; F:electron carrier activity; NAS:UniProtKB.
GO; GO:0051536; F:iron-sulfur cluster binding; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; NAS:UniProtKB.
GO; GO:0008637; P:apoptotic mitochondrial changes; IDA:UniProtKB.
GO; GO:0046034; P:ATP metabolic process; 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; TAS:Reactome.
GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:UniProtKB.
GO; GO:0051881; P:regulation of mitochondrial membrane potential; IMP:UniProtKB.
CDD; cd00207; fer2; 1.
Gene3D; 3.10.20.30; -; 1.
InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
InterPro; IPR012675; Beta-grasp_dom.
InterPro; IPR006656; Mopterin_OxRdtase.
InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS.
InterPro; IPR010228; NADH_UbQ_OxRdtase_Gsu.
InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
InterPro; IPR015405; NuoG_C.
Pfam; PF00384; Molybdopterin; 1.
Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
Pfam; PF09326; NADH_dhqG_C; 1.
SMART; SM00929; NADH-G_4Fe-4S_3; 1.
SUPFAM; SSF54292; SSF54292; 1.
TIGRFAMs; TIGR01973; NuoG; 1.
PROSITE; PS51085; 2FE2S_FER_2; 1.
PROSITE; PS51839; 4FE4S_HC3; 1.
PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
PROSITE; PS00641; COMPLEX1_75K_1; 1.
PROSITE; PS00642; COMPLEX1_75K_2; 1.
PROSITE; PS00643; COMPLEX1_75K_3; 1.
1: Evidence at protein level;
2Fe-2S; 4Fe-4S; Acetylation; Alternative splicing; Complete proteome;
Direct protein sequencing; Disease mutation; Electron transport; Iron;
Iron-sulfur; Membrane; Metal-binding; Mitochondrion;
Mitochondrion inner membrane; NAD; Oxidoreductase; Polymorphism;
Primary mitochondrial disease; Reference proteome; Respiratory chain;
Transit peptide; Transport; Ubiquinone.
TRANSIT 1 23 Mitochondrion.
{ECO:0000244|PubMed:25944712}.
CHAIN 24 727 NADH-ubiquinone oxidoreductase 75 kDa
subunit, mitochondrial.
/FTId=PRO_0000019968.
DOMAIN 30 108 2Fe-2S ferredoxin-type.
{ECO:0000255|PROSITE-ProRule:PRU00465}.
DOMAIN 108 147 4Fe-4S His(Cys)3-ligated-type.
{ECO:0000255|PROSITE-ProRule:PRU01184}.
DOMAIN 245 301 4Fe-4S Mo/W bis-MGD-type.
{ECO:0000255|PROSITE-ProRule:PRU01004}.
METAL 64 64 Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
METAL 75 75 Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
METAL 78 78 Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
METAL 92 92 Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
METAL 124 124 Iron-sulfur 2 (4Fe-4S); via tele
nitrogen. {ECO:0000255|PROSITE-
ProRule:PRU01184}.
METAL 128 128 Iron-sulfur 2 (4Fe-4S).
{ECO:0000255|PROSITE-ProRule:PRU01184}.
METAL 131 131 Iron-sulfur 2 (4Fe-4S).
{ECO:0000255|PROSITE-ProRule:PRU01184}.
METAL 137 137 Iron-sulfur 2 (4Fe-4S).
{ECO:0000255|PROSITE-ProRule:PRU01184}.
METAL 176 176 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
METAL 179 179 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
METAL 182 182 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
METAL 226 226 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
MOD_RES 84 84 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q91VD9}.
MOD_RES 467 467 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q91VD9}.
MOD_RES 499 499 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q91VD9}.
MOD_RES 709 709 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q91VD9}.
VAR_SEQ 1 57 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043727.
VAR_SEQ 1 2 ML -> MW (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043728.
VAR_SEQ 1 1 M -> MRIRGSSGTLSRINM (in isoform 2).
{ECO:0000305}.
/FTId=VSP_042682.
VAR_SEQ 3 113 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043729.
VAR_SEQ 52 87 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045864.
VARIANT 241 241 R -> Q (in dbSNP:rs17856901).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_025511.
VARIANT 241 241 R -> W (in MT-C1D; dbSNP:rs199422225).
{ECO:0000269|PubMed:11349233}.
/FTId=VAR_019532.
VARIANT 252 252 D -> G (in MT-C1D; dbSNP:rs199422224).
{ECO:0000269|PubMed:11349233}.
/FTId=VAR_019533.
VARIANT 253 253 V -> G (in dbSNP:rs786205666).
{ECO:0000269|PubMed:22499341}.
/FTId=VAR_069506.
VARIANT 649 649 V -> F (in dbSNP:rs1044049).
{ECO:0000269|PubMed:1935949}.
/FTId=VAR_018463.
CONFLICT 8 8 K -> R (in Ref. 1; CAA43412).
{ECO:0000305}.
CONFLICT 417 417 R -> W (in Ref. 1; CAA43412).
{ECO:0000305}.
CONFLICT 572 572 H -> L (in Ref. 2; BAG58551).
{ECO:0000305}.
CONFLICT 691 691 I -> L (in Ref. 1; CAA43412).
{ECO:0000305}.
SEQUENCE 727 AA; 79468 MW; 9C35F4B8294771FB CRC64;
MLRIPVRKAL VGLSKSPKGC VRTTATAASN LIEVFVDGQS VMVEPGTTVL QACEKVGMQI
PRFCYHERLS VAGNCRMCLV EIEKAPKVVA ACAMPVMKGW NILTNSEKSK KAREGVMEFL
LANHPLDCPI CDQGGECDLQ DQSMMFGNDR SRFLEGKRAV EDKNIGPLVK TIMTRCIQCT
RCIRFASEIA GVDDLGTTGR GNDMQVGTYI EKMFMSELSG NIIDICPVGA LTSKPYAFTA
RPWETRKTES IDVMDAVGSN IVVSTRTGEV MRILPRMHED INEEWISDKT RFAYDGLKRQ
RLTEPMVRNE KGLLTYTSWE DALSRVAGML QSFQGKDVAA IAGGLVDAEA LVALKDLLNR
VDSDTLCTEE VFPTAGAGTD LRSNYLLNTT IAGVEEADVV LLVGTNPRFE APLFNARIRK
SWLHNDLKVA LIGSPVDLTY TYDHLGDSPK ILQDIASGSH PFSQVLKEAK KPMVVLGSSA
LQRNDGAAIL AAVSSIAQKI RMTSGVTGDW KVMNILHRIA SQVAALDLGY KPGVEAIRKN
PPKVLFLLGA DGGCITRQDL PKDCFIIYQG HHGDVGAPIA DVILPGAAYT EKSATYVNTE
GRAQQTKVAV TPPGLAREDW KIIRALSEIA GMTLPYDTLD QVRNRLEEVS PNLVRYDDIE
GANYFQQANE LSKLVNQQLL ADPLVPPQLT IKDFYMTDSI SRASQTMAKC VKAVTEGAQA
VEEPSIC


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