NDUA7_HUMAN
ID NDUA7_HUMAN Reviewed; 113 AA.
AC O95182;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7;
DE AltName: Full=Complex I-B14.5a;
DE Short=CI-B14.5a;
DE AltName: Full=NADH-ubiquinone oxidoreductase subunit B14.5a;
GN Name=NDUFA7;
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=Lung;
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, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-96, AND IDENTIFICATION BY
RP 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 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 O95182; P25800: LMO1; NbExp=3; IntAct=EBI-721471, EBI-8639312;
CC O95182; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-721471, EBI-10244780;
CC O95182; P49638: TTPA; NbExp=3; IntAct=EBI-721471, EBI-10210710;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:12611891}; Peripheral membrane protein
CC {ECO:0000305}; Matrix side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the complex I NDUFA7 subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC99399.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF050637; AAD05427.1; -; mRNA.
DR EMBL; AF054178; AAC99399.1; ALT_INIT; mRNA.
DR EMBL; BC003102; AAH03102.1; -; mRNA.
DR CCDS; CCDS42492.1; -.
DR PIR; JE0380; JE0380.
DR RefSeq; NP_004992.2; NM_005001.4.
DR PDB; 5XTB; EM; 3.40 A; I=4-113.
DR PDB; 5XTD; EM; 3.70 A; I=4-113.
DR PDB; 5XTH; EM; 3.90 A; I=4-113.
DR PDB; 5XTI; EM; 17.40 A; BI/I=4-113.
DR PDBsum; 5XTB; -.
DR PDBsum; 5XTD; -.
DR PDBsum; 5XTH; -.
DR PDBsum; 5XTI; -.
DR AlphaFoldDB; O95182; -.
DR SMR; O95182; -.
DR BioGRID; 110781; 209.
DR ComplexPortal; CPX-577; Mitochondrial respiratory chain complex I.
DR CORUM; O95182; -.
DR IntAct; O95182; 49.
DR MINT; O95182; -.
DR STRING; 9606.ENSP00000301457; -.
DR BindingDB; O95182; -.
DR ChEMBL; CHEMBL2363065; -.
DR DrugBank; DB00157; NADH.
DR DrugCentral; O95182; -.
DR iPTMnet; O95182; -.
DR PhosphoSitePlus; O95182; -.
DR BioMuta; NDUFA7; -.
DR EPD; O95182; -.
DR jPOST; O95182; -.
DR MassIVE; O95182; -.
DR MaxQB; O95182; -.
DR PaxDb; O95182; -.
DR PeptideAtlas; O95182; -.
DR PRIDE; O95182; -.
DR ProteomicsDB; 50692; -.
DR TopDownProteomics; O95182; -.
DR Antibodypedia; 70788; 295 antibodies from 27 providers.
DR DNASU; 4701; -.
DR Ensembl; ENST00000301457.3; ENSP00000301457.1; ENSG00000267855.6.
DR Ensembl; ENST00000593729.5; ENSP00000470962.1; ENSG00000267855.6.
DR GeneID; 4701; -.
DR KEGG; hsa:4701; -.
DR MANE-Select; ENST00000301457.3; ENSP00000301457.1; NM_005001.5; NP_004992.2.
DR UCSC; uc002mjm.3; human.
DR CTD; 4701; -.
DR DisGeNET; 4701; -.
DR GeneCards; NDUFA7; -.
DR HGNC; HGNC:7691; NDUFA7.
DR HPA; ENSG00000267855; Tissue enhanced (skeletal muscle, tongue).
DR MIM; 602139; gene.
DR neXtProt; NX_O95182; -.
DR OpenTargets; ENSG00000267855; -.
DR PharmGKB; PA31497; -.
DR VEuPathDB; HostDB:ENSG00000267855; -.
DR eggNOG; KOG4630; Eukaryota.
DR GeneTree; ENSGT00390000006553; -.
DR HOGENOM; CLU_149566_0_0_1; -.
DR InParanoid; O95182; -.
DR OMA; NWASGQN; -.
DR OrthoDB; 1465659at2759; -.
DR PhylomeDB; O95182; -.
DR TreeFam; TF319126; -.
DR BioCyc; MetaCyc:HS09632-MON; -.
DR PathwayCommons; O95182; -.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR Reactome; R-HSA-6799198; Complex I biogenesis.
DR SignaLink; O95182; -.
DR SIGNOR; O95182; -.
DR BioGRID-ORCS; 4701; 14 hits in 1080 CRISPR screens.
DR ChiTaRS; NDUFA7; human.
DR GenomeRNAi; 4701; -.
DR Pharos; O95182; Tclin.
DR PRO; PR:O95182; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O95182; protein.
DR Bgee; ENSG00000267855; Expressed in hindlimb stylopod muscle and 96 other tissues.
DR ExpressionAtlas; O95182; baseline and differential.
DR Genevisible; O95182; 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:0005761; C:mitochondrial ribosome; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; NAS:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; ISS:UniProtKB.
DR GO; GO:0009060; P:aerobic respiration; IC:ComplexPortal.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IBA:GO_Central.
DR GO; GO:0032543; P:mitochondrial translation; ISS:UniProtKB.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IC:ComplexPortal.
DR InterPro; IPR009947; NDUA7.
DR PANTHER; PTHR12485; PTHR12485; 1.
DR Pfam; PF07347; CI-B14_5a; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Electron transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Phosphoprotein; Reference proteome;
KW Respiratory chain; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q05752"
FT CHAIN 2..113
FT /note="NADH dehydrogenase [ubiquinone] 1 alpha subcomplex
FT subunit 7"
FT /id="PRO_0000118834"
FT REGION 32..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q05752"
FT MOD_RES 40
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1P6"
FT MOD_RES 96
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VARIANT 66
FT /note="P -> A (in dbSNP:rs2288415)"
FT /id="VAR_050589"
FT HELIX 6..16
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:5XTB"
SQ SEQUENCE 113 AA; 12551 MW; 0B6BF051809B5E9E CRC64;
MASATRLIQR LRNWASGHDL QGKLQLRYQE ISKRTQPPPK LPVGPSHKLS NNYYCTRDGR
RESVPPSIIM SSQKALVSGK PAESSAVAAT EKKAVTPAPP IKRWELSSDQ PYL
