NDUS5_HUMAN
ID NDUS5_HUMAN Reviewed; 106 AA.
AC O43920;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 5;
DE AltName: Full=Complex I-15 kDa;
DE Short=CI-15 kDa;
DE AltName: Full=NADH-ubiquinone oxidoreductase 15 kDa subunit;
GN Name=NDUFS5;
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 [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=9653160; DOI=10.1073/pnas.95.14.8175;
RA Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H.,
RA He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H.,
RA Wang Y.-X., Chen S.-J., Chen Z.;
RT "Identification of genes expressed in human CD34(+) hematopoietic
RT stem/progenitor cells by expressed sequence tags and efficient full-length
RT cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10070614; DOI=10.1023/a:1005434912463;
RA Loeffen J., Smeets R., Smeitink J., Triepels R., Sengers R., Trijbels F.,
RA van den Heuvel L.;
RT "The human NADH:ubiquinone oxidoreductase NDUFS5 (15 kDa) subunit: cDNA
RT cloning, chromosomal localization, tissue distribution and the absence of
RT mutations in isolated complex I-deficient patients.";
RL J. Inherit. Metab. Dis. 22:19-28(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
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 [9]
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 [10]
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 [11]
RP VARIANT SER-96.
RX PubMed=20818383; DOI=10.1038/ng.659;
RA Calvo S.E., Tucker E.J., Compton A.G., Kirby D.M., Crawford G., Burtt N.P.,
RA Rivas M., Guiducci C., Bruno D.L., Goldberger O.A., Redman M.C.,
RA Wiltshire E., Wilson C.J., Altshuler D., Gabriel S.B., Daly M.J.,
RA Thorburn D.R., Mootha V.K.;
RT "High-throughput, pooled sequencing identifies mutations in NUBPL and
RT FOXRED1 in human complex I deficiency.";
RL Nat. Genet. 42:851-858(2010).
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: Mammalian complex I is composed of 45 different subunits. This
CC is a component of the iron-sulfur (IP) fragment of the enzyme.
CC {ECO:0000269|PubMed:12611891, ECO:0000269|PubMed:27626371}.
CC -!- INTERACTION:
CC O43920; Q9NP61: ARFGAP3; NbExp=3; IntAct=EBI-1246091, EBI-2875816;
CC O43920; P42858: HTT; NbExp=7; IntAct=EBI-1246091, EBI-466029;
CC O43920; Q2NKQ1-4: SGSM1; NbExp=3; IntAct=EBI-1246091, EBI-10182463;
CC O43920; Q496A3: SPATS1; NbExp=3; IntAct=EBI-1246091, EBI-3923692;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:12611891}; Peripheral membrane protein
CC {ECO:0000305}. Mitochondrion intermembrane space {ECO:0000305}.
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 -!- SIMILARITY: Belongs to the complex I NDUFS5 subunit family.
CC {ECO:0000305}.
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DR EMBL; AF047434; AAC39878.1; -; mRNA.
DR EMBL; AF020352; AAB87866.1; -; mRNA.
DR EMBL; BC001884; AAH01884.1; -; mRNA.
DR CCDS; CCDS434.1; -.
DR RefSeq; NP_001171908.1; NM_001184979.1.
DR RefSeq; NP_004543.1; NM_004552.2.
DR PDB; 5XTC; EM; 3.70 A; h=2-105.
DR PDB; 5XTD; EM; 3.70 A; h=2-105.
DR PDB; 5XTH; EM; 3.90 A; h=2-105.
DR PDB; 5XTI; EM; 17.40 A; Bh/h=2-105.
DR PDBsum; 5XTC; -.
DR PDBsum; 5XTD; -.
DR PDBsum; 5XTH; -.
DR PDBsum; 5XTI; -.
DR AlphaFoldDB; O43920; -.
DR SMR; O43920; -.
DR BioGRID; 110804; 149.
DR ComplexPortal; CPX-577; Mitochondrial respiratory chain complex I.
DR CORUM; O43920; -.
DR IntAct; O43920; 71.
DR MINT; O43920; -.
DR STRING; 9606.ENSP00000362060; -.
DR BindingDB; O43920; -.
DR ChEMBL; CHEMBL2363065; -.
DR DrugBank; DB00157; NADH.
DR DrugCentral; O43920; -.
DR iPTMnet; O43920; -.
DR PhosphoSitePlus; O43920; -.
DR BioMuta; NDUFS5; -.
DR EPD; O43920; -.
DR jPOST; O43920; -.
DR MassIVE; O43920; -.
DR PaxDb; O43920; -.
DR PeptideAtlas; O43920; -.
DR PRIDE; O43920; -.
DR ProteomicsDB; 49237; -.
DR TopDownProteomics; O43920; -.
DR Antibodypedia; 31851; 230 antibodies from 30 providers.
DR DNASU; 4725; -.
DR Ensembl; ENST00000372967.3; ENSP00000362058.3; ENSG00000168653.11.
DR Ensembl; ENST00000372969.8; ENSP00000362060.3; ENSG00000168653.11.
DR GeneID; 4725; -.
DR KEGG; hsa:4725; -.
DR MANE-Select; ENST00000372969.8; ENSP00000362060.3; NM_004552.3; NP_004543.1.
DR CTD; 4725; -.
DR DisGeNET; 4725; -.
DR GeneCards; NDUFS5; -.
DR HGNC; HGNC:7712; NDUFS5.
DR HPA; ENSG00000168653; Low tissue specificity.
DR MIM; 603847; gene.
DR neXtProt; NX_O43920; -.
DR OpenTargets; ENSG00000168653; -.
DR PharmGKB; PA31522; -.
DR VEuPathDB; HostDB:ENSG00000168653; -.
DR eggNOG; KOG4110; Eukaryota.
DR GeneTree; ENSGT00390000002919; -.
DR HOGENOM; CLU_176387_0_0_1; -.
DR InParanoid; O43920; -.
DR OMA; CAHGIGQ; -.
DR OrthoDB; 1549192at2759; -.
DR PhylomeDB; O43920; -.
DR TreeFam; TF332111; -.
DR BioCyc; MetaCyc:ENSG00000168653-MON; -.
DR PathwayCommons; O43920; -.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR Reactome; R-HSA-6799198; Complex I biogenesis.
DR SignaLink; O43920; -.
DR SIGNOR; O43920; -.
DR BioGRID-ORCS; 4725; 504 hits in 1057 CRISPR screens.
DR ChiTaRS; NDUFS5; human.
DR GeneWiki; NDUFS5; -.
DR GenomeRNAi; 4725; -.
DR Pharos; O43920; Tclin.
DR PRO; PR:O43920; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O43920; protein.
DR Bgee; ENSG00000168653; Expressed in apex of heart and 206 other tissues.
DR ExpressionAtlas; O43920; baseline and differential.
DR Genevisible; O43920; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA: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; IPR019342; NADH_UbQ_OxRdtase_FeS-su5.
DR PANTHER; PTHR15224; PTHR15224; 1.
DR Pfam; PF10200; Ndufs5; 1.
DR PROSITE; PS51808; CHCH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Electron transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Respiratory chain;
KW Transport.
FT CHAIN 1..106
FT /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT 5"
FT /id="PRO_0000118786"
FT DOMAIN 30..74
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT REGION 84..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 33..43
FT /note="Cx9C motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 56..66
FT /note="Cx9C motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 33..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 43..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT VARIANT 96
FT /note="P -> S (detected in a patient with mitochondrial
FT complex I deficiency; uncertain pathological significance;
FT dbSNP:rs201212110)"
FT /evidence="ECO:0000269|PubMed:20818383"
FT /id="VAR_064569"
SQ SEQUENCE 106 AA; 12518 MW; 3D55402837DD99EE CRC64;
MPFLDIQKRF GLNIDRWLTI QSGEQPYKMA GRCHAFEKEW IECAHGIGYT RAEKECKIEY
DDFVECLLRQ KTMRRAGTIR KQRDKLIKEG KYTPPPHHIG KGEPRP
