NDUBB_MOUSE
ID NDUBB_MOUSE Reviewed; 151 AA.
AC O09111;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial;
DE AltName: Full=Complex I-ESSS;
DE Short=CI-ESSS;
DE AltName: Full=NADH-ubiquinone oxidoreductase ESSS subunit;
DE AltName: Full=Neuronal protein 15.6;
DE Short=Np15.6;
DE Short=p15.6;
DE Flags: Precursor;
GN Name=Ndufb11; Synonyms=Np15;
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 [MRNA] OF 2-151.
RA Rogister B., Mazy-Servais C., Leprince P., Schilz F., Moonen G.;
RT "Molecular cloning of mouse NP15.6 a novel neuronal protein whose
RT expression is developmentally regulated.";
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Small intestine;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 PROTEIN SEQUENCE OF 46-86 AND 128-144, 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
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:Q9NX14}.
CC -!- SUBUNIT: Complex I is composed of 45 different subunits. Interacts with
CC BCAP31. {ECO:0000250|UniProtKB:Q9NX14}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q9NX14}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9NX14}. Note=The interaction with BCAP31
CC mediates mitochondria localization. {ECO:0000250|UniProtKB:Q9NX14}.
CC -!- SIMILARITY: Belongs to the complex I NDUFB11 subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH27265.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC25760.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA69961.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Y08702; CAA69961.1; ALT_INIT; mRNA.
DR EMBL; AK028121; BAC25760.1; ALT_INIT; mRNA.
DR EMBL; BC027265; AAH27265.1; ALT_INIT; mRNA.
DR CCDS; CCDS53012.1; -.
DR RefSeq; NP_062308.2; NM_019435.4.
DR RefSeq; XP_006527617.1; XM_006527554.1.
DR PDB; 6G2J; EM; 3.30 A; g=1-151.
DR PDB; 6G72; EM; 3.90 A; g=1-151.
DR PDB; 6ZR2; EM; 3.10 A; g=1-151.
DR PDB; 6ZTQ; EM; 3.00 A; g=1-151.
DR PDB; 7AK5; EM; 3.17 A; g=1-151.
DR PDB; 7AK6; EM; 3.82 A; g=1-151.
DR PDB; 7B93; EM; 3.04 A; g=1-151.
DR PDB; 7PSA; EM; 3.40 A; g=1-151.
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; O09111; -.
DR SMR; O09111; -.
DR BioGRID; 222383; 5.
DR ComplexPortal; CPX-266; Mitochondrial respiratory chain complex I.
DR CORUM; O09111; -.
DR IntAct; O09111; 3.
DR STRING; 10090.ENSMUSP00000112320; -.
DR iPTMnet; O09111; -.
DR PhosphoSitePlus; O09111; -.
DR EPD; O09111; -.
DR jPOST; O09111; -.
DR MaxQB; O09111; -.
DR PaxDb; O09111; -.
DR PeptideAtlas; O09111; -.
DR PRIDE; O09111; -.
DR ProteomicsDB; 293643; -.
DR TopDownProteomics; O09111; -.
DR DNASU; 104130; -.
DR Ensembl; ENSMUST00000116621; ENSMUSP00000112320; ENSMUSG00000031059.
DR GeneID; 104130; -.
DR KEGG; mmu:104130; -.
DR UCSC; uc009ste.2; mouse.
DR CTD; 54539; -.
DR MGI; MGI:1349919; Ndufb11.
DR VEuPathDB; HostDB:ENSMUSG00000031059; -.
DR eggNOG; KOG4808; Eukaryota.
DR GeneTree; ENSGT00390000003022; -.
DR HOGENOM; CLU_109862_0_0_1; -.
DR InParanoid; O09111; -.
DR OMA; CAQSHFR; -.
DR OrthoDB; 1609364at2759; -.
DR PhylomeDB; O09111; -.
DR TreeFam; TF314671; -.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR Reactome; R-MMU-6799198; Complex I biogenesis.
DR BioGRID-ORCS; 104130; 25 hits in 70 CRISPR screens.
DR ChiTaRS; Ndufb11; mouse.
DR PRO; PR:O09111; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; O09111; protein.
DR Bgee; ENSMUSG00000031059; Expressed in temporalis muscle and 263 other tissues.
DR Genevisible; O09111; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO: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: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; IPR019329; NADH_UbQ_OxRdtase_ESSS_su.
DR PANTHER; PTHR13327; PTHR13327; 1.
DR Pfam; PF10183; ESSS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Respiratory chain; Transit peptide; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 30..151
FT /note="NADH dehydrogenase [ubiquinone] 1 beta subcomplex
FT subunit 11, mitochondrial"
FT /id="PRO_0000020058"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 40..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT TURN 64..67
FT /evidence="ECO:0007829|PDB:7B93"
FT HELIX 78..92
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 96..105
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:7B93"
FT HELIX 114..129
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:6ZTQ"
SQ SEQUENCE 151 AA; 17444 MW; ABF2C84E326F23A6 CRC64;
MAARLLSLYG RCLSAAGAMR GLPAARVRWE SSRAVIAPSG VEKKRQREPT MQWQEDPEPE
DENVYAKNPD FHGYDSDPVV DVWNMRAVFF FGFSIVLVFG TTFVAYVPDY RMQEWARREA
ERLVKYREVN GLPIMESNYF DPSKIQLPED D
