NDUS3_DROME
ID NDUS3_DROME Reviewed; 265 AA.
AC Q9VZU4;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial {ECO:0000305};
DE EC=7.1.1.2 {ECO:0000250|UniProtKB:Q56219};
DE AltName: Full=NADH dehydrogenase (Ubiquinone) 30 kDa subunit {ECO:0000312|EMBL:AAF47723.1};
DE Flags: Precursor;
GN Name=ND-30 {ECO:0000312|FlyBase:FBgn0266582};
GN Synonyms=NDUFS3 {ECO:0000303|PubMed:23509070,
GN ECO:0000312|FlyBase:FBgn0266582};
GN ORFNames=CG12079 {ECO:0000312|FlyBase:FBgn0266582};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAM49901.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM49901.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAM49901.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000312|EMBL:AAR96134.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAR96134.1};
RA Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J.,
RA Park S., Wan K., Yu C., Rubin G.M., Celniker S.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP INTERACTION WITH SICILY, AND SUBCELLULAR LOCATION.
RX PubMed=23509070; DOI=10.1083/jcb.201208033;
RA Zhang K., Li Z., Jaiswal M., Bayat V., Xiong B., Sandoval H., Charng W.L.,
RA David G., Haueter C., Yamamoto S., Graham B.H., Bellen H.J.;
RT "The C8ORF38 homologue Sicily is a cytosolic chaperone for a mitochondrial
RT complex I subunit.";
RL J. Cell Biol. 200:807-820(2013).
RN [6]
RP TRANSLATION TERMINATION IMPAIRMENT.
RX PubMed=31378462; DOI=10.1016/j.molcel.2019.06.031;
RA Wu Z., Tantray I., Lim J., Chen S., Li Y., Davis Z., Sitron C., Dong J.,
RA Gispert S., Auburger G., Brandman O., Bi X., Snyder M., Lu B.;
RT "MISTERMINATE Mechanistically Links Mitochondrial Dysfunction with
RT Proteostasis Failure.";
RL Mol. Cell 75:835-848.e8(2019).
CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC NADH dehydrogenase (Complex I) that is believed to belong to the
CC minimal assembly required for catalysis. Complex I functions in the
CC transfer of electrons from NADH to the respiratory chain. The immediate
CC electron acceptor for the enzyme is believed to be ubiquinone.
CC {ECO:0000250|UniProtKB:O75489, ECO:0000250|UniProtKB:Q56219}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) +
CC NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2;
CC Evidence={ECO:0000250|UniProtKB:Q56219};
CC -!- SUBUNIT: Part of the mitochondrial membrane respiratory chain NADH
CC dehydrogenase (Complex I) (By similarity). Interacts with sicily;
CC interaction is stronger with unprocessed sicily protein
CC (PubMed:23509070). {ECO:0000250|UniProtKB:O75489,
CC ECO:0000269|PubMed:23509070}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:23509070}.
CC -!- MISCELLANEOUS: Upon mitochondrial dysfunction, the translation of the
CC mRNA occurring on the mitochondrial surface is impaired and amino acids
CC non-coded by the RNA template are added to the C-terminal of the
CC protein. The C-terminal extended proteins aggregates in the cytosol and
CC are toxic. The phenomenon is called mitochondrial-stress induced
CC translational termination impairment and protein carboxyl terminal
CC extension (MISTERMINATE). {ECO:0000269|PubMed:31378462}.
CC -!- SIMILARITY: Belongs to the complex I 30 kDa subunit family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014296; AAF47723.1; -; Genomic_DNA.
DR EMBL; AY118532; AAM49901.1; -; mRNA.
DR EMBL; BT011342; AAR96134.1; -; mRNA.
DR RefSeq; NP_647775.1; NM_139518.3.
DR AlphaFoldDB; Q9VZU4; -.
DR SMR; Q9VZU4; -.
DR IntAct; Q9VZU4; 1.
DR STRING; 7227.FBpp0072975; -.
DR PaxDb; Q9VZU4; -.
DR PRIDE; Q9VZU4; -.
DR DNASU; 38378; -.
DR EnsemblMetazoa; FBtr0073113; FBpp0072975; FBgn0266582.
DR GeneID; 38378; -.
DR KEGG; dme:Dmel_CG12079; -.
DR UCSC; CG12079-RA; d. melanogaster.
DR CTD; 38378; -.
DR FlyBase; FBgn0266582; ND-30.
DR VEuPathDB; VectorBase:FBgn0266582; -.
DR eggNOG; KOG1713; Eukaryota.
DR GeneTree; ENSGT00390000017480; -.
DR HOGENOM; CLU_042628_0_1_1; -.
DR InParanoid; Q9VZU4; -.
DR OMA; PCRKNRF; -.
DR OrthoDB; 1276923at2759; -.
DR PhylomeDB; Q9VZU4; -.
DR Reactome; R-DME-611105; Respiratory electron transport.
DR Reactome; R-DME-6799198; Complex I biogenesis.
DR SignaLink; Q9VZU4; -.
DR BioGRID-ORCS; 38378; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 38378; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0266582; Expressed in mouthpart and 44 other tissues.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS:FlyBase.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:FlyBase.
DR Gene3D; 3.30.460.80; -; 1.
DR HAMAP; MF_01357; NDH1_NuoC; 1.
DR InterPro; IPR010218; NADH_DH_suC.
DR InterPro; IPR037232; NADH_quin_OxRdtase_su_C/D-like.
DR InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su.
DR InterPro; IPR020396; NADH_UbQ_OxRdtase_CS.
DR Pfam; PF00329; Complex1_30kDa; 1.
DR SUPFAM; SSF143243; SSF143243; 1.
DR TIGRFAMs; TIGR01961; NuoC_fam; 1.
DR PROSITE; PS00542; COMPLEX1_30K; 1.
PE 1: Evidence at protein level;
KW Electron transport; Mitochondrion; NAD; Oxidoreductase; Reference proteome;
KW Respiratory chain; Transit peptide; Translocase; Transport; Ubiquinone.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 34..265
FT /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT 3, mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000451151"
SQ SEQUENCE 265 AA; 29971 MW; B924B9335BDAC881 CRC64;
MAALIRNLGA RAAVAALSAK HVVPAAGSTA LRMASTTPVE PKKADKPTVR QPDAVARSHL
SDFGRYVAEC LPKYVQKVQL TAGDELEVLI APEGVVPVLQ FLKDHHQAQF TNLVDIAGVD
VPCRKNRFEV VYNLLSLRYN SRIRVKTYTD ELTPLDSACE VHKAANWYER EIWDMYGVFF
ANHPDLRRIL TDYGFEGHPQ RRDFPLSGYV ELRYDDEKKR VVCEPLELAQ EFRKFDLSAP
WEQFPNFRNA NPPAEVVPPQ APAKK
