NDUB3_MOUSE
ID NDUB3_MOUSE Reviewed; 104 AA.
AC Q9CQZ6; Q3UUR9;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3;
DE AltName: Full=Complex I-B12;
DE Short=CI-B12;
DE AltName: Full=NADH-ubiquinone oxidoreductase B12 subunit;
GN Name=Ndufb3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Pancreas, Thymus, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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 [3]
RP PROTEIN SEQUENCE OF 20-26 AND 30-40, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-29 AND LYS-40, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-29 AND LYS-40, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
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.
CC {ECO:0000250|UniProtKB:O43676}.
CC -!- SUBUNIT: Complex I is composed of 45 different subunits.
CC {ECO:0000250|UniProtKB:O43676}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:O43676}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:O43676}; Matrix side
CC {ECO:0000250|UniProtKB:O43676}.
CC -!- PTM: Methylation at His residues by METTL9 enhances complex I-mediated
CC mitochondrial respiration. {ECO:0000250|UniProtKB:O43676}.
CC -!- SIMILARITY: Belongs to the complex I NDUFB3 subunit family.
CC {ECO:0000305}.
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DR EMBL; AK007930; BAB25357.1; -; mRNA.
DR EMBL; AK009008; BAB26021.1; -; mRNA.
DR EMBL; AK012320; BAB28160.1; -; mRNA.
DR EMBL; AK138123; BAE23555.1; -; mRNA.
DR EMBL; BC036989; AAH36989.1; -; mRNA.
DR CCDS; CCDS14977.1; -.
DR RefSeq; NP_079873.1; NM_025597.3.
DR PDB; 6G2J; EM; 3.30 A; k=1-104.
DR PDB; 6G72; EM; 3.90 A; k=1-104.
DR PDB; 6ZR2; EM; 3.10 A; k=1-104.
DR PDB; 6ZTQ; EM; 3.00 A; k=1-104.
DR PDB; 7AK5; EM; 3.17 A; k=1-104.
DR PDB; 7AK6; EM; 3.82 A; k=1-104.
DR PDB; 7B93; EM; 3.04 A; k=1-104.
DR PDB; 7PSA; EM; 3.40 A; k=1-104.
DR PDBsum; 6G2J; -.
DR PDBsum; 6G72; -.
DR PDBsum; 6ZR2; -.
DR PDBsum; 6ZTQ; -.
DR PDBsum; 7AK5; -.
DR PDBsum; 7AK6; -.
DR PDBsum; 7B93; -.
DR PDBsum; 7PSA; -.
DR AlphaFoldDB; Q9CQZ6; -.
DR SMR; Q9CQZ6; -.
DR BioGRID; 211516; 15.
DR ComplexPortal; CPX-266; Mitochondrial respiratory chain complex I.
DR CORUM; Q9CQZ6; -.
DR IntAct; Q9CQZ6; 4.
DR STRING; 10090.ENSMUSP00000027193; -.
DR iPTMnet; Q9CQZ6; -.
DR PhosphoSitePlus; Q9CQZ6; -.
DR EPD; Q9CQZ6; -.
DR jPOST; Q9CQZ6; -.
DR MaxQB; Q9CQZ6; -.
DR PaxDb; Q9CQZ6; -.
DR PeptideAtlas; Q9CQZ6; -.
DR PRIDE; Q9CQZ6; -.
DR ProteomicsDB; 252798; -.
DR TopDownProteomics; Q9CQZ6; -.
DR Antibodypedia; 34135; 136 antibodies from 26 providers.
DR DNASU; 66495; -.
DR Ensembl; ENSMUST00000027193; ENSMUSP00000027193; ENSMUSG00000026032.
DR GeneID; 66495; -.
DR KEGG; mmu:66495; -.
DR UCSC; uc007bck.1; mouse.
DR CTD; 4709; -.
DR MGI; MGI:1913745; Ndufb3.
DR VEuPathDB; HostDB:ENSMUSG00000026032; -.
DR eggNOG; KOG4631; Eukaryota.
DR GeneTree; ENSGT00390000010316; -.
DR HOGENOM; CLU_160226_1_0_1; -.
DR InParanoid; Q9CQZ6; -.
DR OMA; EAWRYEP; -.
DR OrthoDB; 1568057at2759; -.
DR PhylomeDB; Q9CQZ6; -.
DR TreeFam; TF319656; -.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR Reactome; R-MMU-6799198; Complex I biogenesis.
DR BioGRID-ORCS; 66495; 18 hits in 74 CRISPR screens.
DR ChiTaRS; Ndufb3; mouse.
DR PRO; PR:Q9CQZ6; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9CQZ6; protein.
DR Bgee; ENSMUSG00000026032; Expressed in facial nucleus and 267 other tissues.
DR Genevisible; Q9CQZ6; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0009060; P:aerobic respiration; IC:ComplexPortal.
DR GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IC:ComplexPortal.
DR InterPro; IPR012576; NDUFB3.
DR PANTHER; PTHR15082; PTHR15082; 1.
DR Pfam; PF08122; NDUF_B12; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Electron transport;
KW Membrane; Methylation; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Respiratory chain; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q02365"
FT CHAIN 2..104
FT /note="NADH dehydrogenase [ubiquinone] 1 beta subcomplex
FT subunit 3"
FT /id="PRO_0000118798"
FT TRANSMEM 72..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q02365"
FT MOD_RES 11
FT /note="Pros-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:O43676"
FT MOD_RES 13
FT /note="Pros-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:O43676"
FT MOD_RES 15
FT /note="Pros-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:O43676"
FT MOD_RES 29
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 29
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 40
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 40
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:7B93"
FT HELIX 35..44
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 54..59
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 69..73
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 77..92
FT /evidence="ECO:0007829|PDB:6ZTQ"
SQ SEQUENCE 104 AA; 11692 MW; 3D6BEE7E6C37ABD2 CRC64;
MAAGHGHEHG HEHGHGHGKM ELPDYRQWKI EGTPLETVQK KLAARGLRDP WARNEAWRYM
GGFAGNITFP SVILKGFKWG FAAFVVALGA EYFLDSQNGD KKHH
