ID   CX6B1_MOUSE             Reviewed;          86 AA.
AC   P56391; Q545A3;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 164.
DE   RecName: Full=Cytochrome c oxidase subunit 6B1;
DE   AltName: Full=Cytochrome c oxidase subunit VIb isoform 1;
DE            Short=COX VIb-1;
GN   Name=Cox6b1; Synonyms=Cox6b;
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=Kidney, and 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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; 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 29-39; 48-58 AND 63-86, 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,
RC   Pancreas, 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   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-62, AND IDENTIFICATION BY MASS
RP   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: Component of the cytochrome c oxidase, the last enzyme in the
CC       mitochondrial electron transport chain which drives oxidative
CC       phosphorylation. The respiratory chain contains 3 multisubunit
CC       complexes succinate dehydrogenase (complex II, CII), ubiquinol-
CC       cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III,
CC       CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to
CC       transfer electrons derived from NADH and succinate to molecular oxygen,
CC       creating an electrochemical gradient over the inner membrane that
CC       drives transmembrane transport and the ATP synthase. Cytochrome c
CC       oxidase is the component of the respiratory chain that catalyzes the
CC       reduction of oxygen to water. Electrons originating from reduced
CC       cytochrome c in the intermembrane space (IMS) are transferred via the
CC       dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1
CC       to the active site in subunit 1, a binuclear center (BNC) formed by
CC       heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2
CC       water molecules using 4 electrons from cytochrome c in the IMS and 4
CC       protons from the mitochondrial matrix. {ECO:0000250|UniProtKB:Q01519}.
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000250|UniProtKB:Q01519}.
CC   -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a
CC       multisubunit enzyme composed of 14 subunits. The complex is composed of
CC       a catalytic core of 3 subunits MT-CO1, MT-CO2 and MT-CO3, encoded in
CC       the mitochondrial DNA, and 11 supernumerary subunits COX4I, COX5A,
CC       COX5B, COX6A, COX6B, COX6C, COX7A, COX7B, COX7C, COX8 and NDUFA4, which
CC       are encoded in the nuclear genome. The complex exists as a monomer or a
CC       dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC       membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and
CC       ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex
CC       III, CIII), resulting in different assemblies (supercomplex
CC       SCI(1)III(2)IV(1) and megacomplex MCI(2)III(2)IV(2)).
CC       {ECO:0000250|UniProtKB:P00429}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P00429}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P00429}; Intermembrane side
CC       {ECO:0000250|UniProtKB:P00429}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 6B family.
CC       {ECO:0000305}.
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DR   EMBL; AK007996; BAB25398.1; -; mRNA.
DR   EMBL; AK012686; BAB28411.1; -; mRNA.
DR   EMBL; AK018721; BAB31367.1; -; mRNA.
DR   EMBL; BC024343; AAH24343.1; -; mRNA.
DR   CCDS; CCDS39887.1; -.
DR   RefSeq; NP_079904.1; NM_025628.2.
DR   PDB; 7O37; EM; 3.20 A; h=2-86.
DR   PDB; 7O3C; EM; 3.30 A; h=2-86.
DR   PDB; 7O3E; EM; 3.60 A; h=2-86.
DR   PDBsum; 7O37; -.
DR   PDBsum; 7O3C; -.
DR   PDBsum; 7O3E; -.
DR   AlphaFoldDB; P56391; -.
DR   EMDB; EMD-12702; -.
DR   EMDB; EMD-12703; -.
DR   EMDB; EMD-12705; -.
DR   SMR; P56391; -.
DR   BioGRID; 225497; 65.
DR   CORUM; P56391; -.
DR   IntAct; P56391; 3.
DR   MINT; P56391; -.
DR   STRING; 10090.ENSMUSP00000075150; -.
DR   GlyGen; P56391; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; P56391; -.
DR   PhosphoSitePlus; P56391; -.
DR   SwissPalm; P56391; -.
DR   EPD; P56391; -.
DR   jPOST; P56391; -.
DR   MaxQB; P56391; -.
DR   PaxDb; 10090-ENSMUSP00000075150; -.
DR   PeptideAtlas; P56391; -.
DR   ProteomicsDB; 284070; -.
DR   Pumba; P56391; -.
DR   TopDownProteomics; P56391; -.
DR   Antibodypedia; 1083; 341 antibodies from 32 providers.
DR   DNASU; 110323; -.
DR   Ensembl; ENSMUST00000075738.6; ENSMUSP00000075150.5; ENSMUSG00000036751.8.
DR   GeneID; 110323; -.
DR   KEGG; mmu:110323; -.
DR   UCSC; uc009gfl.1; mouse.
DR   AGR; MGI:107460; -.
DR   CTD; 1340; -.
DR   MGI; MGI:107460; Cox6b1.
DR   VEuPathDB; HostDB:ENSMUSG00000036751; -.
DR   eggNOG; KOG3057; Eukaryota.
DR   GeneTree; ENSGT00940000156204; -.
DR   HOGENOM; CLU_133964_3_1_1; -.
DR   InParanoid; P56391; -.
DR   OMA; CPNEWIA; -.
DR   OrthoDB; 555936at2759; -.
DR   PhylomeDB; P56391; -.
DR   TreeFam; TF105065; -.
DR   Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
DR   Reactome; R-MMU-611105; Respiratory electron transport.
DR   Reactome; R-MMU-9707564; Cytoprotection by HMOX1.
DR   UniPathway; UPA00705; -.
DR   BioGRID-ORCS; 110323; 19 hits in 76 CRISPR screens.
DR   ChiTaRS; Cox6b1; mouse.
DR   PRO; PR:P56391; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P56391; Protein.
DR   Bgee; ENSMUSG00000036751; Expressed in motor neuron and 251 other cell types or tissues.
DR   ExpressionAtlas; P56391; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR   GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR   GO; GO:0005751; C:mitochondrial respiratory chain complex IV; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0045277; C:respiratory chain complex IV; IBA:GO_Central.
DR   GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR   CDD; cd00926; Cyt_c_Oxidase_VIb; 1.
DR   Gene3D; 1.10.10.140; Cytochrome c oxidase, subunit VIb; 1.
DR   InterPro; IPR048280; COX6B-like.
DR   InterPro; IPR003213; Cyt_c_oxidase_su6B.
DR   InterPro; IPR036549; Cyt_c_oxidase_su6B_sf.
DR   PANTHER; PTHR11387; CYTOCHROME C OXIDASE SUBUNIT 6B; 1.
DR   PANTHER; PTHR11387:SF16; CYTOCHROME C OXIDASE SUBUNIT 6B1; 1.
DR   Pfam; PF02297; COX6B; 1.
DR   PIRSF; PIRSF000278; Cyt_c_oxidase_6B; 1.
DR   SUPFAM; SSF47694; Cytochrome c oxidase subunit h; 1.
DR   PROSITE; PS51808; CHCH; 1.
DR   Genevisible; P56391; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Direct protein sequencing; Disulfide bond;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P00429"
FT   CHAIN           2..86
FT                   /note="Cytochrome c oxidase subunit 6B1"
FT                   /id="PRO_0000194915"
FT   DOMAIN          27..73
FT                   /note="CHCH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           30..40
FT                   /note="Cx9C motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           54..65
FT                   /note="Cx10C motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P00429"
FT   MOD_RES         62
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   DISULFID        30..65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        40..54
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   STRAND          19..21
FT                   /evidence="ECO:0007829|PDB:7O37"
FT   STRAND          23..25
FT                   /evidence="ECO:0007829|PDB:7O37"
FT   HELIX           27..47
FT                   /evidence="ECO:0007829|PDB:7O37"
FT   HELIX           52..54
FT                   /evidence="ECO:0007829|PDB:7O37"
FT   HELIX           55..64
FT                   /evidence="ECO:0007829|PDB:7O37"
FT   HELIX           67..79
FT                   /evidence="ECO:0007829|PDB:7O37"
SQ   SEQUENCE   86 AA;  10071 MW;  A2E96D96CC37509A CRC64;
     MAEDIKTKIK NYKTAPFDSR FPNQNQTKNC WQNYLDFHRC EKAMTAKGGD VSVCEWYRRV
     YKSLCPVSWV SAWDDRIAEG TFPGKI
//