The NDUFB10 gene is located on the p arm of chromosome 16 in position 13.3 and is 2,459 base pairs long.[9][10]
Structureedit
The NDUFB10 protein weighs 21 kDa and is composed of 172 amino acids.[9][10] NDUFB10 is a subunit of the enzyme NADH dehydrogenase (ubiquinone), the largest of the respiratory complexes. The structure is L-shaped with a long, hydrophobictransmembrane domain and a hydrophilic domain for the peripheral arm that includes all the known redox centers and the NADH binding site.[8] It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two-domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH dehydrogenase (ubiquinone) complex at the inner mitochondrial membrane.[7]
Functionedit
The protein encoded by this gene is an accessory subunit of the multisubunit NADH:ubiquinone oxidoreductase (complex I) that is not directly involved in catalysis. Mammalian complex I is composed of 45 different subunits. It locates at the mitochondrial inner membrane. This protein complex has NADH dehydrogenase activity and oxidoreductase activity. It transfers electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. Alternative splicing occurs at this locus and two transcript variants encoding distinct isoforms have been identified.[7] Initially, NADH binds to Complex I and transfers two electrons to the isoalloxazine ring of the flavin mononucleotide (FMN) prosthetic arm to form FMNH2. The electrons are transferred through a series of iron-sulfur (Fe-S) clusters in the prosthetic arm and finally to coenzyme Q10 (CoQ), which is reduced to ubiquinol (CoQH2). The flow of electrons changes the redox state of the protein, resulting in a conformational change and pK shift of the ionizable side chain, which pumps four hydrogen ions out of the mitochondrial matrix.[8]
Referencesedit
^ abcGRCh38: Ensembl release 89: ENSG00000140990 - Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000040048 - Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Emahazion T, Beskow A, Gyllensten U, Brookes AJ (Nov 1998). "Intron based radiation hybrid mapping of 15 complex I genes of the human electron transport chain". Cytogenetics and Cell Genetics. 82 (1–2): 115–9. doi:10.1159/000015082. PMID 9763677. S2CID 46818955.
^Loeffen JL, Triepels RH, van den Heuvel LP, Schuelke M, Buskens CA, Smeets RJ, Trijbels JM, Smeitink JA (Dec 1998). "cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase: human complex I cDNA characterization completed". Biochemical and Biophysical Research Communications. 253 (2): 415–22. doi:10.1006/bbrc.1998.9786. PMID 9878551.
^ abcVoet D, Voet JG, Pratt CW (2013). "Chapter 18". Fundamentals of biochemistry: life at the molecular level (4th ed.). Hoboken, NJ: Wiley. pp. 581–620. ISBN978-0-470-54784-7.
^ abZong NC, Li H, Li H, Lam MP, Jimenez RC, Kim CS, Deng N, Kim AK, Choi JH, Zelaya I, Liem D, Meyer D, Odeberg J, Fang C, Lu HJ, Xu T, Weiss J, Duan H, Uhlen M, Yates JR, Apweiler R, Ge J, Hermjakob H, Ping P (Oct 2013). "Integration of cardiac proteome biology and medicine by a specialized knowledgebase". Circulation Research. 113 (9): 1043–53. doi:10.1161/CIRCRESAHA.113.301151. PMC4076475. PMID 23965338.
Sheffler DJ, Kroeze WK, Garcia BG, Deutch AY, Hufeisen SJ, Leahy P, Brüning JC, Roth BL (Mar 2006). "p90 ribosomal S6 kinase 2 exerts a tonic brake on G protein-coupled receptor signaling". Proceedings of the National Academy of Sciences of the United States of America. 103 (12): 4717–22. Bibcode:2006PNAS..103.4717S. doi:10.1073/pnas.0600585103. PMC1450237. PMID 16537434.
Suzuki Y, Yamashita R, Shirota M, Sakakibara Y, Chiba J, Mizushima-Sugano J, Nakai K, Sugano S (Sep 2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions". Genome Research. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC515316. PMID 15342556.
Yano M, Terada K, Mori M (Oct 2003). "AIP is a mitochondrial import mediator that binds to both import receptor Tom20 and preproteins". The Journal of Cell Biology. 163 (1): 45–56. doi:10.1083/jcb.200305051. PMC2173431. PMID 14557246.
Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR (Feb 2001). "Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16". Human Molecular Genetics. 10 (4): 339–52. doi:10.1093/hmg/10.4.339. PMID 11157797.
Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z (Oct 2000). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells". Genome Research. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC310934. PMID 11042152.
ndufb10, nadh, dehydrogenase, ubiquinone, beta, subcomplex, subunit, enzyme, that, humans, encoded, gene, nadh, dehydrogenase, ubiquinone, beta, subcomplex, subunit, accessory, subunit, nadh, dehydrogenase, ubiquinone, complex, located, mitochondrial, inner, m. NADH dehydrogenase ubiquinone 1 beta subcomplex subunit 10 is an enzyme that in humans is encoded by the NDUFB10 gene 5 6 7 NADH dehydrogenase ubiquinone 1 beta subcomplex subunit 10 is an accessory subunit of the NADH dehydrogenase ubiquinone complex located in the mitochondrial inner membrane It is also known as Complex I and is the largest of the five complexes of the electron transport chain 8 NDUFB10IdentifiersAliasesNDUFB10 PDSW NADH ubiquinone oxidoreductase subunit B10 MC1DN35External IDsOMIM 603843 MGI 1915592 HomoloGene 3343 GeneCards NDUFB10Gene location Human Chr Chromosome 16 human 1 Band16p13 3Start1 959 538 bp 1 End1 961 975 bp 1 Gene location Mouse Chr Chromosome 17 mouse 2 Band17 17 A3 3Start24 941 034 bp 2 End24 943 452 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed intibialis anterior musclequadriceps femoris musclevastus lateralis musclegastrocnemius muscleright ventriclebody of tonguedeltoid muscleparotid glandbody of stomachBrodmann area 9Top expressed ininterventricular septummyocardium of ventricleintercostal musclethoracic diaphragmplantaris muscleextraocular musclesoleus muscledigastric musclemedial vestibular nucleusquadriceps femoris muscleMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionprotein binding NADH dehydrogenase ubiquinone activityCellular componentmitochondrial respiratory chain complex I mitochondrion respirasome mitochondrial inner membrane membraneBiological processmitochondrial electron transport NADH to ubiquinone mitochondrial respiratory chain complex I assemblySources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez471668342EnsemblENSG00000140990ENSMUSG00000040048UniProtO96000Q9DCS9RefSeq mRNA NM 004548NM 026684RefSeq protein NP 004539NP 080960Location UCSC Chr 16 1 96 1 96 MbChr 17 24 94 24 94 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse Contents 1 Gene 2 Structure 3 Function 4 References 5 Further readingGene editThe NDUFB10 gene is located on the p arm of chromosome 16 in position 13 3 and is 2 459 base pairs long 9 10 Structure editThe NDUFB10 protein weighs 21 kDa and is composed of 172 amino acids 9 10 NDUFB10 is a subunit of the enzyme NADH dehydrogenase ubiquinone the largest of the respiratory complexes The structure is L shaped with a long hydrophobic transmembrane domain and a hydrophilic domain for the peripheral arm that includes all the known redox centers and the NADH binding site 8 It has been noted that the N terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C terminal hydrophilic domain interacting with globular subunits of Complex I The highly conserved two domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH dehydrogenase ubiquinone complex at the inner mitochondrial membrane 7 Function editThe protein encoded by this gene is an accessory subunit of the multisubunit NADH ubiquinone oxidoreductase complex I that is not directly involved in catalysis Mammalian complex I is composed of 45 different subunits It locates at the mitochondrial inner membrane This protein complex has NADH dehydrogenase activity and oxidoreductase activity It transfers electrons from NADH to the respiratory chain The immediate electron acceptor for the enzyme is believed to be ubiquinone Alternative splicing occurs at this locus and two transcript variants encoding distinct isoforms have been identified 7 Initially NADH binds to Complex I and transfers two electrons to the isoalloxazine ring of the flavin mononucleotide FMN prosthetic arm to form FMNH2 The electrons are transferred through a series of iron sulfur Fe S clusters in the prosthetic arm and finally to coenzyme Q10 CoQ which is reduced to ubiquinol CoQH2 The flow of electrons changes the redox state of the protein resulting in a conformational change and pK shift of the ionizable side chain which pumps four hydrogen ions out of the mitochondrial matrix 8 References edit a b c GRCh38 Ensembl release 89 ENSG00000140990 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000040048 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Emahazion T Beskow A Gyllensten U Brookes AJ Nov 1998 Intron based radiation hybrid mapping of 15 complex I genes of the human electron transport chain Cytogenetics and Cell Genetics 82 1 2 115 9 doi 10 1159 000015082 PMID 9763677 S2CID 46818955 Loeffen JL Triepels RH van den Heuvel LP Schuelke M Buskens CA Smeets RJ Trijbels JM Smeitink JA Dec 1998 cDNA of eight nuclear encoded subunits of NADH ubiquinone oxidoreductase human complex I cDNA characterization completed Biochemical and Biophysical Research Communications 253 2 415 22 doi 10 1006 bbrc 1998 9786 PMID 9878551 a b c Entrez Gene NDUFB10 NADH dehydrogenase ubiquinone 1 beta subcomplex 10 22kDa a b c Voet D Voet JG Pratt CW 2013 Chapter 18 Fundamentals of biochemistry life at the molecular level 4th ed Hoboken NJ Wiley pp 581 620 ISBN 978 0 470 54784 7 a b Zong NC Li H Li H Lam MP Jimenez RC Kim CS Deng N Kim AK Choi JH Zelaya I Liem D Meyer D Odeberg J Fang C Lu HJ Xu T Weiss J Duan H Uhlen M Yates JR Apweiler R Ge J Hermjakob H Ping P Oct 2013 Integration of cardiac proteome biology and medicine by a specialized knowledgebase Circulation Research 113 9 1043 53 doi 10 1161 CIRCRESAHA 113 301151 PMC 4076475 PMID 23965338 a b NADH dehydrogenase ubiquinone 1 beta subcomplex subunit 10 Cardiac Organellar Protein Atlas Knowledgebase COPaKB Further reading editSheffler DJ Kroeze WK Garcia BG Deutch AY Hufeisen SJ Leahy P Bruning JC Roth BL Mar 2006 p90 ribosomal S6 kinase 2 exerts a tonic brake on G protein coupled receptor signaling Proceedings of the National Academy of Sciences of the United States of America 103 12 4717 22 Bibcode 2006PNAS 103 4717S doi 10 1073 pnas 0600585103 PMC 1450237 PMID 16537434 Suzuki Y Yamashita R Shirota M Sakakibara Y Chiba J Mizushima Sugano J Nakai K Sugano S Sep 2004 Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions Genome Research 14 9 1711 8 doi 10 1101 gr 2435604 PMC 515316 PMID 15342556 Yano M Terada K Mori M Oct 2003 AIP is a mitochondrial import mediator that binds to both import receptor Tom20 and preproteins The Journal of Cell Biology 163 1 45 56 doi 10 1083 jcb 200305051 PMC 2173431 PMID 14557246 Daniels RJ Peden JF Lloyd C Horsley SW Clark K Tufarelli C Kearney L Buckle VJ Doggett NA Flint J Higgs DR Feb 2001 Sequence structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16 Human Molecular Genetics 10 4 339 52 doi 10 1093 hmg 10 4 339 PMID 11157797 Zhang QH Ye M Wu XY Ren SX Zhao M Zhao CJ Fu G Shen Y Fan HY Lu G Zhong M Xu XR Han ZG Zhang JW Tao J Huang QH Zhou J Hu GX Gu J Chen SJ Chen Z Oct 2000 Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34 hematopoietic stem progenitor cells Genome Research 10 10 1546 60 doi 10 1101 gr 140200 PMC 310934 PMID 11042152 This article incorporates text from the United States National Library of Medicine which is in the public domain Retrieved from https en wikipedia org w index php title NDUFB10 amp oldid 1118753868, wikipedia, wiki, book, books, library,
