ID   NDUB7_HUMAN             Reviewed;         137 AA.
AC   P17568; Q6ICN9; Q9UI16;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   28-JAN-2026, entry version 209.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7;
DE   AltName: Full=Cell adhesion protein SQM1;
DE   AltName: Full=Complex I-B18;
DE            Short=CI-B18;
DE   AltName: Full=NADH-ubiquinone oxidoreductase B18 subunit;
GN   Name=NDUFB7;
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=2302251; DOI=10.1016/0006-291x(90)90908-6;
RA   Wong Y.-C., Tsao S.-W., Kakefuda M., Bernal S.D.;
RT   "cDNA cloning of a novel cell adhesion protein expressed in human squamous
RT   carcinoma cells.";
RL   Biochem. Biophys. Res. Commun. 166:984-992(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10830904; DOI=10.1007/s004390000278;
RA   Triepels R., Smeitink J., Loeffen J., Smeets R., Trijbels F.,
RA   van den Heuvel L.;
RT   "Characterization of the human complex I NDUFB7 and 17.2-kDa cDNAs and
RT   mutational analysis of 19 genes of the HP fraction in complex I-deficient-
RT   patients.";
RL   Hum. Genet. 106:385-391(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Hypothalamus;
RX   PubMed=10931946; DOI=10.1073/pnas.160270997;
RA   Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA   Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA   Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA   Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA   Chen M.-D., Chen J.-L.;
RT   "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT   and full-length cDNA cloning.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
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   [7]
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   [8]
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   [9]
RP   SUBCELLULAR LOCATION, DOMAIN, AND MOTIF.
RX   PubMed=21310150; DOI=10.1016/j.febslet.2011.01.046;
RA   Szklarczyk R., Wanschers B.F., Nabuurs S.B., Nouws J., Nijtmans L.G.,
RA   Huynen M.A.;
RT   "NDUFB7 and NDUFA8 are located at the intermembrane surface of complex I.";
RL   FEBS Lett. 585:737-743(2011).
RN   [10]
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   [11]
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).
RN   [12]
RP   INVOLVEMENT IN MC1DN39, AND FUNCTION.
RX   PubMed=33502047; DOI=10.1002/humu.24173;
RA   Correia S.P., Moedas M.F., Naess K., Bruhn H., Maffezzini C.,
RA   Calvo-Garrido J., Lesko N., Wibom R., Schober F.A., Jemt A.,
RA   Stranneheim H., Freyer C., Wedell A., Wredenberg A.;
RT   "Severe congenital lactic acidosis and hypertrophic cardiomyopathy caused
RT   by an intronic variant in NDUFB7.";
RL   Hum. Mutat. 42:378-384(2021).
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       ECO:0000269|PubMed:33502047}.
CC   -!- SUBUNIT: Complex I is composed of 45 different subunits.
CC       {ECO:0000269|PubMed:12611891, ECO:0000269|PubMed:27626371}.
CC   -!- INTERACTION:
CC       P17568; Q5U5Z8-3: AGBL2; NbExp=3; IntAct=EBI-1246238, EBI-12226473;
CC       P17568; Q9NX04: AIRIM; NbExp=3; IntAct=EBI-1246238, EBI-8643161;
CC       P17568; Q8N2N9-4: ANKRD36B; NbExp=3; IntAct=EBI-1246238, EBI-12170453;
CC       P17568; Q7Z3C6-3: ATG9A; NbExp=3; IntAct=EBI-1246238, EBI-12006308;
CC       P17568; Q8N4L8: CCDC24; NbExp=3; IntAct=EBI-1246238, EBI-1104933;
CC       P17568; P24863: CCNC; NbExp=3; IntAct=EBI-1246238, EBI-395261;
CC       P17568; Q96GN5: CDCA7L; NbExp=3; IntAct=EBI-1246238, EBI-5278764;
CC       P17568; P55273: CDKN2D; NbExp=3; IntAct=EBI-1246238, EBI-745859;
CC       P17568; Q9UKJ5: CHIC2; NbExp=3; IntAct=EBI-1246238, EBI-741528;
CC       P17568; Q9BW66: CINP; NbExp=3; IntAct=EBI-1246238, EBI-739784;
CC       P17568; P51800-3: CLCNKA; NbExp=3; IntAct=EBI-1246238, EBI-11980535;
CC       P17568; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-1246238, EBI-11962928;
CC       P17568; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-1246238, EBI-744099;
CC       P17568; Q96MY7: FAM161B; NbExp=3; IntAct=EBI-1246238, EBI-7225287;
CC       P17568; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-1246238, EBI-6658203;
CC       P17568; P55040: GEM; NbExp=3; IntAct=EBI-1246238, EBI-744104;
CC       P17568; Q9NWQ4-1: GPATCH2L; NbExp=3; IntAct=EBI-1246238, EBI-11959863;
CC       P17568; P13807: GYS1; NbExp=3; IntAct=EBI-1246238, EBI-740553;
CC       P17568; P60014: KRTAP10-10; NbExp=3; IntAct=EBI-1246238, EBI-11955579;
CC       P17568; P25791-3: LMO2; NbExp=3; IntAct=EBI-1246238, EBI-11959475;
CC       P17568; Q96A72: MAGOHB; NbExp=3; IntAct=EBI-1246238, EBI-746778;
CC       P17568; O14770-4: MEIS2; NbExp=3; IntAct=EBI-1246238, EBI-8025850;
CC       P17568; Q13064: MKRN3; NbExp=3; IntAct=EBI-1246238, EBI-2340269;
CC       P17568; Q15653: NFKBIB; NbExp=3; IntAct=EBI-1246238, EBI-352889;
CC       P17568; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-1246238, EBI-10271199;
CC       P17568; Q9P2K3-2: RCOR3; NbExp=3; IntAct=EBI-1246238, EBI-1504830;
CC       P17568; Q6P9E2: RECK; NbExp=3; IntAct=EBI-1246238, EBI-10253121;
CC       P17568; Q0D2K3: RIPPLY1; NbExp=3; IntAct=EBI-1246238, EBI-10226430;
CC       P17568; Q5TAB7: RIPPLY2; NbExp=3; IntAct=EBI-1246238, EBI-10246897;
CC       P17568; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-1246238, EBI-748391;
CC       P17568; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-1246238, EBI-5235340;
CC       P17568; Q7Z698: SPRED2; NbExp=3; IntAct=EBI-1246238, EBI-7082156;
CC       P17568; Q9BX79-6: STRA6; NbExp=3; IntAct=EBI-1246238, EBI-12140683;
CC       P17568; Q01664: TFAP4; NbExp=3; IntAct=EBI-1246238, EBI-2514218;
CC       P17568; Q08117-2: TLE5; NbExp=3; IntAct=EBI-1246238, EBI-11741437;
CC       P17568; Q9Y6T4: WUGSC:H_DJ0726N20.gs.b; NbExp=3; IntAct=EBI-1246238, EBI-12369705;
CC       P17568; Q9Y3S2: ZNF330; NbExp=3; IntAct=EBI-1246238, EBI-373456;
CC       P17568; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-1246238, EBI-740727;
CC       P17568; Q8TBZ8: ZNF564; NbExp=3; IntAct=EBI-1246238, EBI-10273713;
CC       P17568; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-1246238, EBI-6427977;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:21310150}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:21310150}. Mitochondrion intermembrane space
CC       {ECO:0000269|PubMed:21310150}.
CC   -!- DOMAIN: Contains two C-X9-C motifs that are predicted to form a helix-
CC       coil-helix structure, permitting the formation of intramolecular
CC       disulfide bonds. {ECO:0000269|PubMed:21310150}.
CC   -!- DISEASE: Mitochondrial complex I deficiency, nuclear type 39 (MC1DN39)
CC       [MIM:620135]: 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. MC1DN39 is an autosomal recessive form characterized
CC       by intrauterine growth retardation, anemia, and postpartum hypertrophic
CC       cardiomyopathy, lactic acidosis, encephalopathy, and a severe complex I
CC       defect with a fatal outcome. {ECO:0000269|PubMed:33502047}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the complex I NDUFB7 subunit family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA35675.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; M33374; AAA35675.1; ALT_FRAME; mRNA.
DR   EMBL; AF217091; AAF91223.1; -; mRNA.
DR   EMBL; AF112200; AAF17188.1; -; mRNA.
DR   EMBL; CR450354; CAG29350.1; -; mRNA.
DR   EMBL; CH471106; EAW84436.1; -; Genomic_DNA.
DR   EMBL; BC002595; AAH02595.1; -; mRNA.
DR   CCDS; CCDS12314.1; -.
DR   PIR; A34653; A34653.
DR   RefSeq; NP_004137.2; NM_004146.5.
DR   PDB; 5XTC; EM; 3.70 A; v=3-124.
DR   PDB; 5XTD; EM; 3.70 A; v=1-137.
DR   PDB; 5XTH; EM; 3.90 A; v=3-124.
DR   PDB; 5XTI; EM; 17.40 A; Bv/v=3-124.
DR   PDB; 9CWT; EM; 3.44 A; v=1-137.
DR   PDBsum; 5XTC; -.
DR   PDBsum; 5XTD; -.
DR   PDBsum; 5XTH; -.
DR   PDBsum; 5XTI; -.
DR   PDBsum; 9CWT; -.
DR   AlphaFoldDB; P17568; -.
DR   EMDB; EMD-45974; -.
DR   SMR; P17568; -.
DR   BioGRID; 110793; 115.
DR   ComplexPortal; CPX-577; Mitochondrial respiratory chain complex I.
DR   CORUM; P17568; -.
DR   FunCoup; P17568; 1894.
DR   IntAct; P17568; 91.
DR   MINT; P17568; -.
DR   STRING; 9606.ENSP00000215565; -.
DR   BindingDB; P17568; -.
DR   ChEMBL; CHEMBL2363065; -.
DR   DrugBank; DB00157; NADH.
DR   DrugCentral; P17568; -.
DR   GlyGen; P17568; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P17568; -.
DR   PhosphoSitePlus; P17568; -.
DR   BioMuta; NDUFB7; -.
DR   DMDM; 12644140; -.
DR   jPOST; P17568; -.
DR   MassIVE; P17568; -.
DR   PaxDb; 9606-ENSP00000215565; -.
DR   PeptideAtlas; P17568; -.
DR   ProteomicsDB; 53493; -.
DR   Pumba; P17568; -.
DR   Antibodypedia; 1259; 151 antibodies from 30 providers.
DR   DNASU; 4713; -.
DR   Ensembl; ENST00000215565.3; ENSP00000215565.1; ENSG00000099795.8.
DR   GeneID; 4713; -.
DR   KEGG; hsa:4713; -.
DR   MANE-Select; ENST00000215565.3; ENSP00000215565.1; NM_004146.6; NP_004137.2.
DR   UCSC; uc002mzg.4; human.
DR   AGR; HGNC:7702; -.
DR   ClinPGx; PA31513; -.
DR   CTD; 4713; -.
DR   DisGeNET; 4713; -.
DR   GeneCards; NDUFB7; -.
DR   HGNC; HGNC:7702; NDUFB7.
DR   HPA; ENSG00000099795; Low tissue specificity.
DR   MalaCards; NDUFB7; -.
DR   MIM; 603842; gene.
DR   MIM; 620135; phenotype.
DR   OpenTargets; ENSG00000099795; -.
DR   VEuPathDB; HostDB:ENSG00000099795; -.
DR   eggNOG; KOG3468; Eukaryota.
DR   GeneTree; ENSGT00390000018759; -.
DR   HOGENOM; CLU_154847_1_0_1; -.
DR   InParanoid; P17568; -.
DR   OMA; FVYQCAH; -.
DR   OrthoDB; 268414at2759; -.
DR   PAN-GO; P17568; 1 GO annotation based on evolutionary models.
DR   PhylomeDB; P17568; -.
DR   BioCyc; MetaCyc:HS01908-MONOMER; -.
DR   PathwayCommons; P17568; -.
DR   Reactome; R-HSA-611105; Respiratory electron transport.
DR   Reactome; R-HSA-6799198; Complex I biogenesis.
DR   SignaLink; P17568; -.
DR   SIGNOR; P17568; -.
DR   Agora; ENSG00000099795; -.
DR   BioGRID-ORCS; 4713; 347 hits in 1160 CRISPR screens.
DR   CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities.
DR   ChiTaRS; NDUFB7; human.
DR   GeneWiki; NDUFB7; -.
DR   GenomeRNAi; 4713; -.
DR   Pharos; P17568; Tclin.
DR   PRO; PR:P17568; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; P17568; protein.
DR   Bgee; ENSG00000099795; Expressed in apex of heart and 201 other cell types or tissues.
DR   ExpressionAtlas; P17568; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; HDA:UniProtKB.
DR   GO; GO:0045271; C:respiratory chain complex I; IDA:UniProtKB.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IMP:UniProtKB.
DR   GO; GO:0009060; P:aerobic respiration; NAS:ComplexPortal.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; NAS:UniProtKB.
DR   GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; NAS:ComplexPortal.
DR   InterPro; IPR008698; NDUB7.
DR   PANTHER; PTHR20900:SF0; NADH DEHYDROGENASE [UBIQUINONE] 1 BETA SUBCOMPLEX SUBUNIT 7; 1.
DR   PANTHER; PTHR20900; NADH:UBIQUINONE OXIDOREDUCTASE B18-LIKE SUBUNIT; 1.
DR   Pfam; PF05676; NDUF_B7; 1.
DR   PROSITE; PS51808; CHCH; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Electron transport; Lipoprotein; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Myristate; Phosphoprotein;
KW   Primary mitochondrial disease; Proteomics identification;
KW   Reference proteome; Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..137
FT                   /note="NADH dehydrogenase [ubiquinone] 1 beta subcomplex
FT                   subunit 7"
FT                   /id="PRO_0000118811"
FT   DOMAIN          56..98
FT                   /note="CHCH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   REGION          113..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           59..69
FT                   /note="Cx9C motif 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           80..90
FT                   /note="Cx9C motif 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOD_RES         73
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CR61"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        59..90
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        69..80
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   VARIANT         106
FT                   /note="R -> G (in dbSNP:rs3752220)"
FT                   /id="VAR_050591"
SQ   SEQUENCE   137 AA;  16402 MW;  2743716544288776 CRC64;
     MGAHLVRRYL GDASVEPDPL QMPTFPPDYG FPERKEREMV ATQQEMMDAQ LRLQLRDYCA
     HHLIRLLKCK RDSFPNFLAC KQERHDWDYC EHRDYVMRMK EFERERRLLQ RKKRREKKAA
     ELAKGQGPGE VDPKVAL
//