NDUA3_HUMAN
ID NDUA3_HUMAN Reviewed; 84 AA.
AC O95167;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3;
DE AltName: Full=Complex I-B9;
DE Short=CI-B9;
DE AltName: Full=NADH-ubiquinone oxidoreductase B9 subunit;
GN Name=NDUFA3;
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].
RX PubMed=9878551; DOI=10.1006/bbrc.1998.9786;
RA Loeffen J.L.C.M., Triepels R.H., van den Heuvel L.P., Schuelke M.,
RA Buskens C.A.F., Smeets R.J.P., Trijbels J.M.F., Smeitink J.A.M.;
RT "cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase:
RT human complex I cDNA characterization completed.";
RL Biochem. Biophys. Res. Commun. 253:415-422(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas, and Prostate;
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 [4]
RP IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
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 [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [7]
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 [8]
RP VARIANT [LARGE SCALE ANALYSIS] ASP-62.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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 O95167; Q9BUF7-2: CRB3; NbExp=3; IntAct=EBI-1246131, EBI-17233035;
CC O95167; Q15125: EBP; NbExp=3; IntAct=EBI-1246131, EBI-3915253;
CC O95167; Q9UKR5: ERG28; NbExp=3; IntAct=EBI-1246131, EBI-711490;
CC O95167; Q6ZVE7: GOLT1A; NbExp=3; IntAct=EBI-1246131, EBI-17231387;
CC O95167; O95214: LEPROTL1; NbExp=3; IntAct=EBI-1246131, EBI-750776;
CC O95167; Q8N4V1: MMGT1; NbExp=3; IntAct=EBI-1246131, EBI-6163737;
CC O95167; P15941-11: MUC1; NbExp=3; IntAct=EBI-1246131, EBI-17263240;
CC O95167; Q9UHI5: SLC7A8; NbExp=3; IntAct=EBI-1246131, EBI-13292283;
CC O95167; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-1246131, EBI-12947623;
CC O95167; Q96DZ7: TM4SF19; NbExp=3; IntAct=EBI-1246131, EBI-6448756;
CC O95167; Q96IK0: TMEM101; NbExp=3; IntAct=EBI-1246131, EBI-3922699;
CC O95167; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-1246131, EBI-8638294;
CC O95167; Q6UW68: TMEM205; NbExp=3; IntAct=EBI-1246131, EBI-6269551;
CC O95167; Q9NWH2: TMEM242; NbExp=3; IntAct=EBI-1246131, EBI-10315004;
CC O95167; Q9Y320: TMX2; NbExp=3; IntAct=EBI-1246131, EBI-6447886;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:12611891}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the complex I NDUFA3 subunit family.
CC {ECO:0000305}.
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DR EMBL; AF044955; AAD05420.1; -; mRNA.
DR EMBL; AF070653; AAD20959.1; -; mRNA.
DR EMBL; BC022369; AAH22369.1; -; mRNA.
DR EMBL; BC061644; AAH61644.1; -; mRNA.
DR CCDS; CCDS12877.1; -.
DR PIR; JE0379; JE0379.
DR RefSeq; NP_004533.1; NM_004542.3.
DR RefSeq; XP_016882322.1; XM_017026833.1.
DR PDB; 5XTC; EM; 3.70 A; U=2-84.
DR PDB; 5XTD; EM; 3.70 A; U=2-84.
DR PDB; 5XTH; EM; 3.90 A; U=2-84.
DR PDB; 5XTI; EM; 17.40 A; BU/U=2-84.
DR PDBsum; 5XTC; -.
DR PDBsum; 5XTD; -.
DR PDBsum; 5XTH; -.
DR PDBsum; 5XTI; -.
DR AlphaFoldDB; O95167; -.
DR SMR; O95167; -.
DR BioGRID; 110776; 69.
DR ComplexPortal; CPX-577; Mitochondrial respiratory chain complex I.
DR CORUM; O95167; -.
DR IntAct; O95167; 32.
DR MINT; O95167; -.
DR STRING; 9606.ENSP00000418438; -.
DR BindingDB; O95167; -.
DR ChEMBL; CHEMBL2363065; -.
DR DrugBank; DB00157; NADH.
DR DrugCentral; O95167; -.
DR iPTMnet; O95167; -.
DR PhosphoSitePlus; O95167; -.
DR BioMuta; NDUFA3; -.
DR EPD; O95167; -.
DR jPOST; O95167; -.
DR MassIVE; O95167; -.
DR PaxDb; O95167; -.
DR PeptideAtlas; O95167; -.
DR PRIDE; O95167; -.
DR ProteomicsDB; 50680; -.
DR TopDownProteomics; O95167; -.
DR Antibodypedia; 32779; 141 antibodies from 21 providers.
DR DNASU; 4696; -.
DR Ensembl; ENST00000419113.5; ENSP00000398290.1; ENSG00000170906.16.
DR Ensembl; ENST00000485876.6; ENSP00000418438.1; ENSG00000170906.16.
DR Ensembl; ENST00000610406.1; ENSP00000478119.1; ENSG00000275724.1.
DR Ensembl; ENST00000612327.1; ENSP00000480437.1; ENSG00000276220.1.
DR Ensembl; ENST00000613276.1; ENSP00000477919.1; ENSG00000273642.1.
DR Ensembl; ENST00000617282.1; ENSP00000482015.1; ENSG00000278365.1.
DR Ensembl; ENST00000618338.1; ENSP00000481545.1; ENSG00000274359.1.
DR Ensembl; ENST00000619253.1; ENSP00000483934.1; ENSG00000275605.1.
DR Ensembl; ENST00000619966.1; ENSP00000484436.1; ENSG00000276766.1.
DR Ensembl; ENST00000620289.4; ENSP00000477783.1; ENSG00000276061.4.
DR Ensembl; ENST00000621307.1; ENSP00000483002.1; ENSG00000277722.1.
DR Ensembl; ENST00000622523.4; ENSP00000483683.1; ENSG00000276061.4.
DR GeneID; 4696; -.
DR KEGG; hsa:4696; -.
DR MANE-Select; ENST00000485876.6; ENSP00000418438.1; NM_004542.4; NP_004533.1.
DR CTD; 4696; -.
DR DisGeNET; 4696; -.
DR GeneCards; NDUFA3; -.
DR HGNC; HGNC:7686; NDUFA3.
DR HPA; ENSG00000170906; Tissue enhanced (heart muscle, skeletal muscle).
DR MIM; 603832; gene.
DR neXtProt; NX_O95167; -.
DR OpenTargets; ENSG00000170906; -.
DR PharmGKB; PA31492; -.
DR VEuPathDB; HostDB:ENSG00000170906; -.
DR eggNOG; ENOG502S4RS; Eukaryota.
DR GeneTree; ENSGT00390000004322; -.
DR HOGENOM; CLU_171491_0_0_1; -.
DR InParanoid; O95167; -.
DR OMA; PDIPAHP; -.
DR OrthoDB; 1577370at2759; -.
DR PhylomeDB; O95167; -.
DR TreeFam; TF333021; -.
DR BioCyc; MetaCyc:HS10204-MON; -.
DR PathwayCommons; O95167; -.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR Reactome; R-HSA-6799198; Complex I biogenesis.
DR SignaLink; O95167; -.
DR SIGNOR; O95167; -.
DR BioGRID-ORCS; 4696; 112 hits in 1075 CRISPR screens.
DR ChiTaRS; NDUFA3; human.
DR GenomeRNAi; 4696; -.
DR Pharos; O95167; Tclin.
DR PRO; PR:O95167; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O95167; protein.
DR Bgee; ENSG00000170906; Expressed in primary visual cortex and 94 other tissues.
DR ExpressionAtlas; O95167; baseline and differential.
DR Genevisible; O95167; 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; HDA:UniProtKB.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; NAS:UniProtKB.
DR GO; GO:0009060; P:aerobic respiration; IC:ComplexPortal.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; NAS:UniProtKB.
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; IPR026626; NDUFA3.
DR PANTHER; PTHR15221; PTHR15221; 1.
DR Pfam; PF14987; NADHdh_A3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Electron transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Respiratory chain;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q02371"
FT CHAIN 2..84
FT /note="NADH dehydrogenase [ubiquinone] 1 alpha subcomplex
FT subunit 3"
FT /id="PRO_0000118793"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 56..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q02371"
FT VARIANT 62
FT /note="N -> D (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036175"
SQ SEQUENCE 84 AA; 9279 MW; 38B27A96D7A05D31 CRC64;
MAARVGAFLK NAWDKEPVLV VSFVVGGLAV ILPPLSPYFK YSVMINKATP YNYPVPVRDD
GNMPDVPSHP QDPQGPSLEW LKKL
