NDUAB_HUMAN
ID NDUAB_HUMAN Reviewed; 141 AA.
AC Q86Y39; C9JT23; Q6ZS66;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11;
DE AltName: Full=Complex I-B14.7;
DE Short=CI-B14.7;
DE AltName: Full=NADH-ubiquinone oxidoreductase subunit B14.7;
GN Name=NDUFA11;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS
RP SPECTROMETRY, AND IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE
RP COMPLEX.
RC TISSUE=Heart;
RX PubMed=12611891; DOI=10.1074/jbc.c300064200;
RA Murray J., Zhang B., Taylor S.W., Oglesbee D., Fahy E., Marusich M.F.,
RA Ghosh S.S., Capaldi R.A.;
RT "The subunit composition of the human NADH dehydrogenase obtained by rapid
RT one-step immunopurification.";
RL J. Biol. Chem. 278:13619-13622(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 2-7.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [6]
RP INVOLVEMENT IN MC1DN14.
RX PubMed=18306244; DOI=10.1002/ana.21332;
RA Berger I., Hershkovitz E., Shaag A., Edvardson S., Saada A., Elpeleg O.;
RT "Mitochondrial complex I deficiency caused by a deleterious NDUFA11
RT mutation.";
RL Ann. Neurol. 63:405-408(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [9]
RP FUNCTION, AND IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX.
RX PubMed=27626371; DOI=10.1038/nature19754;
RA Stroud D.A., Surgenor E.E., Formosa L.E., Reljic B., Frazier A.E.,
RA Dibley M.G., Osellame L.D., Stait T., Beilharz T.H., Thorburn D.R.,
RA Salim A., Ryan M.T.;
RT "Accessory subunits are integral for assembly and function of human
RT mitochondrial complex I.";
RL Nature 538:123-126(2016).
CC -!- FUNCTION: Accessory subunit of the mitochondrial membrane respiratory
CC chain NADH dehydrogenase (Complex I), that is believed not to be
CC involved in catalysis. Complex I functions in the transfer of electrons
CC from NADH to the respiratory chain. The immediate electron acceptor for
CC the enzyme is believed to be ubiquinone. {ECO:0000269|PubMed:27626371}.
CC -!- SUBUNIT: Complex I is composed of 45 different subunits.
CC {ECO:0000269|PubMed:12611891, ECO:0000269|PubMed:27626371}.
CC -!- INTERACTION:
CC Q86Y39; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-1246415, EBI-16439278;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:12611891}; Multi-pass membrane protein
CC {ECO:0000255}; Matrix side {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86Y39-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86Y39-2; Sequence=VSP_033813;
CC -!- DISEASE: Mitochondrial complex I deficiency, nuclear type 14 (MC1DN14)
CC [MIM:618236]: A form of mitochondrial complex I deficiency, the most
CC common biochemical signature of mitochondrial disorders, a group of
CC highly heterogeneous conditions characterized by defective oxidative
CC phosphorylation, which collectively affects 1 in 5-10000 live births.
CC Clinical disorders have variable severity, ranging from lethal neonatal
CC disease to adult-onset neurodegenerative disorders. Phenotypes include
CC macrocephaly with progressive leukodystrophy, non-specific
CC encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh
CC syndrome, Leber hereditary optic neuropathy, and some forms of
CC Parkinson disease. MC1DN14 transmission pattern is consistent with
CC autosomal recessive inheritance. {ECO:0000269|PubMed:18306244}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the complex I NDUFA11 subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC87088.1; Type=Miscellaneous discrepancy; Note=Erroneous CDS prediction.; Evidence={ECO:0000305};
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DR EMBL; AJ539081; CAD62165.1; -; mRNA.
DR EMBL; AK127692; BAC87088.1; ALT_SEQ; mRNA.
DR EMBL; AC024592; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104532; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069045; AAH69045.1; -; mRNA.
DR CCDS; CCDS12155.1; -. [Q86Y39-1]
DR CCDS; CCDS54203.1; -. [Q86Y39-2]
DR RefSeq; NP_001180304.1; NM_001193375.1. [Q86Y39-2]
DR RefSeq; NP_783313.1; NM_175614.4. [Q86Y39-1]
DR PDB; 5XTC; EM; 3.70 A; V=2-141.
DR PDB; 5XTD; EM; 3.70 A; V=2-141.
DR PDB; 5XTH; EM; 3.90 A; V=2-141.
DR PDB; 5XTI; EM; 17.40 A; BV/V=2-141.
DR PDBsum; 5XTC; -.
DR PDBsum; 5XTD; -.
DR PDBsum; 5XTH; -.
DR PDBsum; 5XTI; -.
DR AlphaFoldDB; Q86Y39; -.
DR SMR; Q86Y39; -.
DR BioGRID; 125981; 62.
DR ComplexPortal; CPX-577; Mitochondrial respiratory chain complex I.
DR CORUM; Q86Y39; -.
DR IntAct; Q86Y39; 43.
DR MINT; Q86Y39; -.
DR STRING; 9606.ENSP00000389160; -.
DR BindingDB; Q86Y39; -.
DR ChEMBL; CHEMBL2363065; -.
DR DrugBank; DB00157; NADH.
DR DrugCentral; Q86Y39; -.
DR GlyGen; Q86Y39; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q86Y39; -.
DR PhosphoSitePlus; Q86Y39; -.
DR SwissPalm; Q86Y39; -.
DR BioMuta; NDUFA11; -.
DR DMDM; 52000823; -.
DR EPD; Q86Y39; -.
DR jPOST; Q86Y39; -.
DR MassIVE; Q86Y39; -.
DR MaxQB; Q86Y39; -.
DR PaxDb; Q86Y39; -.
DR PeptideAtlas; Q86Y39; -.
DR PRIDE; Q86Y39; -.
DR ProteomicsDB; 11546; -.
DR ProteomicsDB; 70371; -. [Q86Y39-1]
DR ProteomicsDB; 70372; -. [Q86Y39-2]
DR TopDownProteomics; Q86Y39-1; -. [Q86Y39-1]
DR Antibodypedia; 52912; 83 antibodies from 24 providers.
DR DNASU; 126328; -.
DR Ensembl; ENST00000308961.5; ENSP00000311740.4; ENSG00000174886.14. [Q86Y39-1]
DR Ensembl; ENST00000418389.6; ENSP00000389160.1; ENSG00000174886.14. [Q86Y39-2]
DR GeneID; 126328; -.
DR KEGG; hsa:126328; -.
DR MANE-Select; ENST00000308961.5; ENSP00000311740.4; NM_175614.5; NP_783313.1.
DR UCSC; uc002mdp.3; human. [Q86Y39-1]
DR CTD; 126328; -.
DR DisGeNET; 126328; -.
DR GeneCards; NDUFA11; -.
DR HGNC; HGNC:20371; NDUFA11.
DR HPA; ENSG00000174886; Low tissue specificity.
DR MalaCards; NDUFA11; -.
DR MIM; 612638; gene.
DR MIM; 618236; phenotype.
DR neXtProt; NX_Q86Y39; -.
DR OpenTargets; ENSG00000174886; -.
DR Orphanet; 2609; Isolated complex I deficiency.
DR PharmGKB; PA134914606; -.
DR VEuPathDB; HostDB:ENSG00000174886; -.
DR eggNOG; ENOG502S6F6; Eukaryota.
DR GeneTree; ENSGT00390000012434; -.
DR HOGENOM; CLU_1214425_0_0_1; -.
DR InParanoid; Q86Y39; -.
DR OMA; QKTWITT; -.
DR OrthoDB; 1456214at2759; -.
DR PhylomeDB; Q86Y39; -.
DR TreeFam; TF314729; -.
DR BioCyc; MetaCyc:HS16402-MON; -.
DR PathwayCommons; Q86Y39; -.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR Reactome; R-HSA-6799198; Complex I biogenesis.
DR SignaLink; Q86Y39; -.
DR SIGNOR; Q86Y39; -.
DR BioGRID-ORCS; 126328; 373 hits in 1064 CRISPR screens.
DR ChiTaRS; NDUFA11; human.
DR GenomeRNAi; 126328; -.
DR Pharos; Q86Y39; Tclin.
DR PRO; PR:Q86Y39; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q86Y39; protein.
DR Bgee; ENSG00000174886; Expressed in pancreatic ductal cell and 181 other tissues.
DR ExpressionAtlas; Q86Y39; baseline and differential.
DR Genevisible; Q86Y39; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0009060; P:aerobic respiration; IC:ComplexPortal.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IMP:UniProtKB.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IC:ComplexPortal.
DR InterPro; IPR039205; NDUFA11.
DR PANTHER; PTHR21382; PTHR21382; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Primary mitochondrial disease; Reference proteome; Respiratory chain;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8HXG6,
FT ECO:0000269|PubMed:12665801"
FT CHAIN 2..141
FT /note="NADH dehydrogenase [ubiquinone] 1 alpha subcomplex
FT subunit 11"
FT /id="PRO_0000118841"
FT TRANSMEM 21..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8HXG6"
FT VAR_SEQ 105..141
FT /note="THNYGIGAAACVYFGIAASLVKMGRLEGWEVFAKPKV -> KTGSHCVVQAG
FT LKLLASSSPHTSASQSAGIIGMSHCVQRFWVPSSSACLEVLSGESTDVHACSSTRGACN
FT SSGSRPLPELGARASGSLRKGGHTHPAPRGAGALTPVQALIESLLNTLGSNPRT (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_033813"
FT CONFLICT Q86Y39-2:160
FT /note="S -> G (in Ref. 2; BAC87088)"
FT /evidence="ECO:0000305"
FT CONFLICT Q86Y39-2:221
FT /note="T -> A (in Ref. 2; BAC87088)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 141 AA; 14852 MW; 379D58482D7E8BDB CRC64;
MAPKVFRQYW DIPDGTDCHR KAYSTTSIAS VAGLTAAAYR VTLNPPGTFL EGVAKVGQYT
FTAAAVGAVF GLTTCISAHV REKPDDPLNY FLGGCAGGLT LGARTHNYGI GAAACVYFGI
AASLVKMGRL EGWEVFAKPK V
