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NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial (EC 1.6.5.3) (EC 1.6.99.3) (Complex I-49kD) (CI-49kD) (NADH-ubiquinone oxidoreductase 49 kDa subunit)

 NDUS2_HUMAN             Reviewed;         463 AA.
O75306; D3DVG7; J3KPM7; Q5VTW0; Q969P3; Q9UEV3;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
16-APR-2002, sequence version 2.
22-NOV-2017, entry version 181.
RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial;
EC=1.6.5.3;
EC=1.6.99.3;
AltName: Full=Complex I-49kD;
Short=CI-49kD;
AltName: Full=NADH-ubiquinone oxidoreductase 49 kDa subunit;
Flags: Precursor;
Name=NDUFS2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9647766; DOI=10.1006/bbrc.1998.8882;
Loeffen J., van den Heuvel L., Smeets R., Triepels R., Sengers R.,
Trijbels F., Smeitink J.;
"cDNA sequence and chromosomal localization of the remaining three
human nuclear encoded iron sulphur protein (IP) subunits of complex I:
the human IP fraction is completed.";
Biochem. Biophys. Res. Commun. 247:751-758(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
PubMed=9585441; DOI=10.1007/s003359900803;
Procaccio V., de Sury R., Martinez P., Depetris D., Rabilloud T.,
Soularue P., Lunardi J., Issartel J.-P.;
"Mapping to 1q23 of the human gene (NDUFS2) encoding the 49-kDa
subunit of the mitochondrial respiratory complex I and immunodetection
of the mature protein in mitochondria.";
Mamm. Genome 9:482-484(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle, and Placenta;
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).
[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]
INTERACTION WITH NDUFAF3.
PubMed=19463981; DOI=10.1016/j.ajhg.2009.04.020;
Saada A., Vogel R.O., Hoefs S.J., van den Brand M.A., Wessels H.J.,
Willems P.H., Venselaar H., Shaag A., Barghuti F., Reish O.,
Shohat M., Huynen M.A., Smeitink J.A.M., van den Heuvel L.P.,
Nijtmans L.G.;
"Mutations in NDUFAF3 (C3ORF60), encoding an NDUFAF4 (C6ORF66)-
interacting complex I assembly protein, cause fatal neonatal
mitochondrial disease.";
Am. J. Hum. Genet. 84:718-727(2009).
[9]
INTERACTION WITH NDUFAF7.
PubMed=20406883; DOI=10.1242/jcs.066076;
Carilla-Latorre S., Gallardo M.E., Annesley S.J., Calvo-Garrido J.,
Grana O., Accari S.L., Smith P.K., Valencia A., Garesse R.,
Fisher P.R., Escalante R.;
"MidA is a putative methyltransferase that is required for
mitochondrial complex I function.";
J. Cell Sci. 123:1674-1683(2010).
[10]
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).
[11]
METHYLATION AT ARG-118, AND INTERACTION WITH NDUFAF7.
PubMed=24089531; DOI=10.1074/jbc.M113.518803;
Rhein V.F., Carroll J., Ding S., Fearnley I.M., Walker J.E.;
"NDUFAF7 methylates arginine 85 in the NDUFS2 subunit of human complex
I.";
J. Biol. Chem. 288:33016-33026(2013).
[12]
METHYLATION AT ARG-118.
PubMed=24838397; DOI=10.1093/hmg/ddu239;
Zurita Rendon O., Silva Neiva L., Sasarman F., Shoubridge E.A.;
"The arginine methyltransferase NDUFAF7 is essential for complex I
assembly and early vertebrate embryogenesis.";
Hum. Mol. Genet. 23:5159-5170(2014).
[13]
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).
[14]
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).
[15]
VARIANTS MT-C1D GLN-228; GLN-229 AND PRO-413.
PubMed=11220739;
DOI=10.1002/1531-8249(20010201)49:2<195::AID-ANA39>3.0.CO;2-M;
Loeffen J., Elpeleg O., Smeitink J., Smeets R.,
Stoeckler-Ipsiroglu S., Mandel H., Sengers R., Trijbels F.,
van den Heuvel L.;
"Mutations in the complex I NDUFS2 gene of patients with
cardiomyopathy and encephalomyopathy.";
Ann. Neurol. 49:195-201(2001).
[16]
VARIANT VAL-224.
PubMed=21057504; DOI=10.1038/ng.706;
Haack T.B., Danhauser K., Haberberger B., Hoser J., Strecker V.,
Boehm D., Uziel G., Lamantea E., Invernizzi F., Poulton J.,
Rolinski B., Iuso A., Biskup S., Schmidt T., Mewes H.W., Wittig I.,
Meitinger T., Zeviani M., Prokisch H.;
"Exome sequencing identifies ACAD9 mutations as a cause of complex I
deficiency.";
Nat. Genet. 42:1131-1134(2010).
-!- 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 (PubMed:12611891). {ECO:0000269|PubMed:12611891}.
-!- CATALYTIC ACTIVITY: NADH + ubiquinone + 5 H(+)(In) = NAD(+) +
ubiquinol + 4 H(+)(Out).
-!- CATALYTIC ACTIVITY: NADH + acceptor = NAD(+) + reduced acceptor.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Note=Binds 1 [4Fe-4S] cluster.;
-!- SUBUNIT: Complex I is composed of 45 different subunits. Component
of the iron-sulfur (IP) fragment of the enzyme (PubMed:12611891).
Interacts with NDUFAF3 (PubMed:19463981). Interacts with NDUFAF7
(PubMed:20406883, PubMed:24089531). {ECO:0000269|PubMed:12611891,
ECO:0000269|PubMed:19463981, ECO:0000269|PubMed:20406883,
ECO:0000269|PubMed:24089531}.
-!- INTERACTION:
O75489:NDUFS3; NbExp=6; IntAct=EBI-1224806, EBI-1224896;
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000269|PubMed:12611891, ECO:0000269|PubMed:9585441};
Peripheral membrane protein {ECO:0000269|PubMed:12611891}; Matrix
side {ECO:0000269|PubMed:12611891}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O75306-1; Sequence=Displayed;
Name=2;
IsoId=O75306-2; Sequence=VSP_046466;
Note=No experimental confirmation available.;
-!- PTM: Dimethylation at Arg-118 by NDUFAF7 takes place after NDUFS2
assembles into the complex I, leading to stabilize the early
intermediate complex (PubMed:24089531, PubMed:24838397).
{ECO:0000269|PubMed:24089531, ECO:0000269|PubMed:24838397}.
-!- 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:11220739}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
{ECO:0000305}.
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EMBL; AF050640; AAC27453.1; -; mRNA.
EMBL; AF013160; AAC34362.1; -; mRNA.
EMBL; AK314807; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AL590714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471121; EAW52625.1; -; Genomic_DNA.
EMBL; CH471121; EAW52626.1; -; Genomic_DNA.
EMBL; BC000170; AAH00170.1; -; mRNA.
EMBL; BC001456; AAH01456.1; -; mRNA.
EMBL; BC008868; AAH08868.1; -; mRNA.
CCDS; CCDS1224.1; -. [O75306-1]
CCDS; CCDS53404.1; -. [O75306-2]
PIR; JE0193; JE0193.
RefSeq; NP_001159631.1; NM_001166159.1. [O75306-2]
RefSeq; NP_004541.1; NM_004550.4. [O75306-1]
RefSeq; XP_005245265.1; XM_005245208.2. [O75306-1]
RefSeq; XP_016856846.1; XM_017001357.1. [O75306-1]
UniGene; Hs.173611; -.
PDB; 5XTB; EM; 3.40 A; Q=79-463.
PDB; 5XTC; EM; 3.70 A; Q=34-79.
PDB; 5XTD; EM; 3.70 A; Q=34-463.
PDB; 5XTH; EM; 3.90 A; Q=34-463.
PDB; 5XTI; EM; 17.40 A; BQ/Q=34-463.
PDBsum; 5XTB; -.
PDBsum; 5XTC; -.
PDBsum; 5XTD; -.
PDBsum; 5XTH; -.
PDBsum; 5XTI; -.
ProteinModelPortal; O75306; -.
SMR; O75306; -.
BioGrid; 110800; 65.
CORUM; O75306; -.
IntAct; O75306; 37.
STRING; 9606.ENSP00000356972; -.
ChEMBL; CHEMBL2363065; -.
DrugBank; DB00997; Doxorubicin.
DrugBank; DB00157; NADH.
iPTMnet; O75306; -.
PhosphoSitePlus; O75306; -.
SwissPalm; O75306; -.
BioMuta; NDUFS2; -.
EPD; O75306; -.
MaxQB; O75306; -.
PaxDb; O75306; -.
PeptideAtlas; O75306; -.
PRIDE; O75306; -.
TopDownProteomics; O75306-1; -. [O75306-1]
DNASU; 4720; -.
Ensembl; ENST00000367993; ENSP00000356972; ENSG00000158864. [O75306-1]
Ensembl; ENST00000392179; ENSP00000376018; ENSG00000158864. [O75306-2]
GeneID; 4720; -.
KEGG; hsa:4720; -.
UCSC; uc001fyv.4; human. [O75306-1]
CTD; 4720; -.
DisGeNET; 4720; -.
EuPathDB; HostDB:ENSG00000158864.12; -.
GeneCards; NDUFS2; -.
HGNC; HGNC:7708; NDUFS2.
HPA; HPA055140; -.
HPA; HPA061953; -.
MalaCards; NDUFS2; -.
MIM; 252010; phenotype.
MIM; 602985; gene.
neXtProt; NX_O75306; -.
OpenTargets; ENSG00000158864; -.
Orphanet; 2609; Isolated NADH-CoQ reductase deficiency.
PharmGKB; PA31519; -.
eggNOG; KOG2870; Eukaryota.
eggNOG; COG0649; LUCA.
GeneTree; ENSGT00390000009529; -.
HOGENOM; HOG000228264; -.
HOVERGEN; HBG000760; -.
InParanoid; O75306; -.
KO; K03935; -.
OMA; KKIAWPA; -.
OrthoDB; EOG091G0WWQ; -.
PhylomeDB; O75306; -.
TreeFam; TF300370; -.
Reactome; R-HSA-611105; Respiratory electron transport.
Reactome; R-HSA-6799198; Complex I biogenesis.
ChiTaRS; NDUFS2; human.
GeneWiki; NDUFS2; -.
GenomeRNAi; 4720; -.
PRO; PR:O75306; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000158864; -.
CleanEx; HS_NDUFS2; -.
Genevisible; O75306; HS.
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:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0009055; F:electron carrier activity; NAS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0051287; F:NAD binding; IEA:InterPro.
GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; NAS:UniProtKB.
GO; GO:0048038; F:quinone binding; IEA:InterPro.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; IMP:CAFA.
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:0006979; P:response to oxidative stress; IDA:UniProtKB.
Gene3D; 1.10.645.10; -; 2.
HAMAP; MF_01358; NDH1_NuoD; 1.
InterPro; IPR001135; NADH_Q_OxRdtase_suD.
InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS.
InterPro; IPR022885; NDH1_su_D/H.
InterPro; IPR029014; NiFe_Hase-like.
Pfam; PF00346; Complex1_49kDa; 1.
SUPFAM; SSF56762; SSF56762; 1.
TIGRFAMs; TIGR01962; NuoD; 1.
PROSITE; PS00535; COMPLEX1_49K; 1.
1: Evidence at protein level;
3D-structure; 4Fe-4S; Acetylation; Alternative splicing;
Complete proteome; Disease mutation; Electron transport; Iron;
Iron-sulfur; Membrane; Metal-binding; Methylation; Mitochondrion;
Mitochondrion inner membrane; NAD; Oxidoreductase; Polymorphism;
Primary mitochondrial disease; Reference proteome; Respiratory chain;
Transit peptide; Transport; Ubiquinone.
TRANSIT 1 33 Mitochondrion. {ECO:0000250}.
CHAIN 34 463 NADH dehydrogenase [ubiquinone] iron-
sulfur protein 2, mitochondrial.
/FTId=PRO_0000019981.
METAL 326 326 Iron-sulfur (4Fe-4S). {ECO:0000255}.
METAL 332 332 Iron-sulfur (4Fe-4S). {ECO:0000255}.
METAL 347 347 Iron-sulfur (4Fe-4S). {ECO:0000255}.
MOD_RES 62 62 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q91WD5}.
MOD_RES 118 118 Symmetric dimethylarginine.
{ECO:0000269|PubMed:24089531,
ECO:0000269|PubMed:24838397}.
VAR_SEQ 454 463 QDIVFGEVDR -> RPIV (in isoform 2).
{ECO:0000305}.
/FTId=VSP_046466.
VARIANT 20 20 P -> T (in dbSNP:rs11538340).
/FTId=VAR_034150.
VARIANT 224 224 A -> V. {ECO:0000269|PubMed:21057504}.
/FTId=VAR_071891.
VARIANT 228 228 R -> Q (in MT-C1D; dbSNP:rs121434427).
{ECO:0000269|PubMed:11220739}.
/FTId=VAR_019535.
VARIANT 229 229 P -> A (in dbSNP:rs16827493).
/FTId=VAR_034151.
VARIANT 229 229 P -> Q (in MT-C1D; dbSNP:rs121434428).
{ECO:0000269|PubMed:11220739}.
/FTId=VAR_019536.
VARIANT 352 352 P -> A (in dbSNP:rs11576415).
/FTId=VAR_034152.
VARIANT 413 413 S -> P (in MT-C1D; dbSNP:rs121434429).
{ECO:0000269|PubMed:11220739}.
/FTId=VAR_019537.
CONFLICT 24 24 V -> G (in Ref. 2; AAC34362).
{ECO:0000305}.
STRAND 80 82 {ECO:0000244|PDB:5XTB}.
STRAND 86 88 {ECO:0000244|PDB:5XTB}.
TURN 89 94 {ECO:0000244|PDB:5XTB}.
STRAND 96 105 {ECO:0000244|PDB:5XTB}.
STRAND 107 112 {ECO:0000244|PDB:5XTB}.
HELIX 120 125 {ECO:0000244|PDB:5XTB}.
HELIX 129 132 {ECO:0000244|PDB:5XTB}.
HELIX 134 137 {ECO:0000244|PDB:5XTB}.
STRAND 140 142 {ECO:0000244|PDB:5XTB}.
HELIX 145 158 {ECO:0000244|PDB:5XTB}.
HELIX 165 193 {ECO:0000244|PDB:5XTB}.
HELIX 198 218 {ECO:0000244|PDB:5XTB}.
STRAND 219 223 {ECO:0000244|PDB:5XTB}.
STRAND 231 234 {ECO:0000244|PDB:5XTB}.
HELIX 240 249 {ECO:0000244|PDB:5XTB}.
HELIX 251 259 {ECO:0000244|PDB:5XTB}.
TURN 260 264 {ECO:0000244|PDB:5XTB}.
HELIX 266 272 {ECO:0000244|PDB:5XTB}.
HELIX 280 286 {ECO:0000244|PDB:5XTB}.
HELIX 291 294 {ECO:0000244|PDB:5XTB}.
TURN 295 297 {ECO:0000244|PDB:5XTB}.
HELIX 310 312 {ECO:0000244|PDB:5XTB}.
STRAND 318 320 {ECO:0000244|PDB:5XTB}.
HELIX 326 349 {ECO:0000244|PDB:5XTB}.
TURN 361 363 {ECO:0000244|PDB:5XTB}.
HELIX 368 371 {ECO:0000244|PDB:5XTB}.
HELIX 375 384 {ECO:0000244|PDB:5XTB}.
TURN 385 387 {ECO:0000244|PDB:5XTB}.
STRAND 393 402 {ECO:0000244|PDB:5XTB}.
STRAND 405 413 {ECO:0000244|PDB:5XTB}.
STRAND 415 423 {ECO:0000244|PDB:5XTB}.
HELIX 427 439 {ECO:0000244|PDB:5XTB}.
HELIX 444 453 {ECO:0000244|PDB:5XTB}.
HELIX 458 461 {ECO:0000244|PDB:5XTB}.
SEQUENCE 463 AA; 52546 MW; A2BF56F008B6312C CRC64;
MAALRALCGF RGVAAQVLRP GAGVRLPIQP SRGVRQWQPD VEWAQQFGGA VMYPSKETAH
WKPPPWNDVD PPKDTIVKNI TLNFGPQHPA AHGVLRLVME LSGEMVRKCD PHIGLLHRGT
EKLIEYKTYL QALPYFDRLD YVSMMCNEQA YSLAVEKLLN IRPPPRAQWI RVLFGEITRL
LNHIMAVTTH ALDLGAMTPF FWLFEEREKM FEFYERVSGA RMHAAYIRPG GVHQDLPLGL
MDDIYQFSKN FSLRLDELEE LLTNNRIWRN RTIDIGVVTA EEALNYGFSG VMLRGSGIQW
DLRKTQPYDV YDQVEFDVPV GSRGDCYDRY LCRVEEMRQS LRIIAQCLNK MPPGEIKVDD
AKVSPPKRAE MKTSMESLIH HFKLYTEGYQ VPPGATYTAI EAPKGEFGVY LVSDGSSRPY
RCKIKAPGFA HLAGLDKMSK GHMLADVVAI IGTQDIVFGE VDR


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