CX6B1_BOVIN
ID CX6B1_BOVIN Reviewed; 86 AA.
AC P00429; Q54A32;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Cytochrome c oxidase subunit 6B1;
DE AltName: Full=Cytochrome c oxidase polypeptide VII;
DE AltName: Full=Cytochrome c oxidase subunit AED;
DE AltName: Full=Cytochrome c oxidase subunit VIb isoform 1;
DE Short=COX VIb-1;
GN Name=COX6B1; Synonyms=COX6B;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=2548168; DOI=10.1093/nar/17.14.5845;
RA Lightowlers R.N., Capaldi R.A.;
RT "Nucleotide sequence of the cDNA encoding subunit AED (VIB) of beef heart
RT cytochrome c oxidase.";
RL Nucleic Acids Res. 17:5845-5845(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-86.
RX PubMed=229067; DOI=10.1515/bchm2.1979.360.2.1641;
RA Steffens G.C.M., Steffens G.J., Buse G.;
RT "Studies on cytochrome c oxidase, VIII. The amino acid sequence of
RT polypeptide VII.";
RL Hoppe-Seyler's Z. Physiol. Chem. 360:1641-1650(1979).
RN [4]
RP PROTEIN SEQUENCE OF 2-86, AND ACETYLATION AT ALA-2.
RX PubMed=6262305; DOI=10.1016/s0021-9258(19)69329-4;
RA Tanaka M., Yasunobu K.T., Wei Y.-H., King T.E.;
RT "The complete amino acid sequence of bovine heart cytochrome oxidase
RT subunit VI.";
RL J. Biol. Chem. 256:4832-4837(1981).
RN [5]
RP PROTEIN SEQUENCE OF 45-67.
RC TISSUE=Liver;
RX PubMed=2844245; DOI=10.1021/bi00413a048;
RA Yanamura W., Zhang Y.-Z., Takamiya S., Capaldi R.A.;
RT "Tissue-specific differences between heart and liver cytochrome c
RT oxidase.";
RL Biochemistry 27:4909-4914(1988).
RN [6]
RP SUBUNIT.
RX PubMed=26698328; DOI=10.1074/jbc.m115.680553;
RA Shinzawa-Itoh K., Shimomura H., Yanagisawa S., Shimada S., Takahashi R.,
RA Oosaki M., Ogura T., Tsukihara T.;
RT "Purification of active respiratory supercomplex from bovine heart
RT mitochondria enables functional studies.";
RL J. Biol. Chem. 291:4178-4184(2016).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND DISULFIDE BONDS.
RX PubMed=8638158; DOI=10.1126/science.272.5265.1136;
RA Tsukihara T., Aoyama H., Yamashita E., Tomizaki T., Yamaguchi H.,
RA Shinzawa-Itoh K., Nakashima R., Yaono R., Yoshikawa S.;
RT "The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8
RT A.";
RL Science 272:1136-1144(1996).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RC TISSUE=Heart;
RX PubMed=10089392; DOI=10.1107/s0907444998006362;
RA Tomizaki T., Yamashita E., Yamaguchi H., Aoyama H., Tsukihara T.,
RA Shinzawa-Itoh K., Nakashima R., Yaono R., Yoshikawa S.;
RT "Structure analysis of bovine heart cytochrome c oxidase at 2.8 A
RT resolution.";
RL Acta Crystallogr. D 55:31-45(1999).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RC TISSUE=Heart;
RX PubMed=10771420; DOI=10.1107/s0907444900002213;
RA Fei M.J., Yamashita E., Inoue N., Yao M., Yamaguchi H., Tsukihara T.,
RA Shinzawa-Itoh K., Nakashima R., Yoshikawa S.;
RT "X-ray structure of azide-bound fully oxidized cytochrome c oxidase from
RT bovine heart at 2.9 A resolution.";
RL Acta Crystallogr. D 56:529-535(2000).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), AND DISULFIDE BONDS.
RX PubMed=20385840; DOI=10.1073/pnas.0910410107;
RA Muramoto K., Ohta K., Shinzawa-Itoh K., Kanda K., Taniguchi M.,
RA Nabekura H., Yamashita E., Tsukihara T., Yoshikawa S.;
RT "Bovine cytochrome c oxidase structures enable O2 reduction with
RT minimization of reactive oxygens and provide a proton-pumping gate.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:7740-7745(2010).
RN [11]
RP STRUCTURE BY ELECTRON MICROSCOPY (9.10 ANGSTROMS).
RX PubMed=27830641; DOI=10.7554/elife.21290;
RA Sousa J.S., Mills D.J., Vonck J., Kuehlbrandt W.;
RT "Functional asymmetry and electron flow in the bovine respirasome.";
RL Elife 5:0-0(2016).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS), AND DISULFIDE BONDS.
RX PubMed=27605664; DOI=10.1074/jbc.m115.711770;
RA Yano N., Muramoto K., Shimada A., Takemura S., Baba J., Fujisawa H.,
RA Mochizuki M., Shinzawa-Itoh K., Yamashita E., Tsukihara T., Yoshikawa S.;
RT "The Mg2+-containing water cluster of mammalian cytochrome c oxidase
RT collects four pumping proton equivalents in each catalytic cycle.";
RL J. Biol. Chem. 291:23882-23894(2016).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), AND DISULFIDE BONDS.
RX PubMed=31533957; DOI=10.1073/pnas.1907183116;
RA Shinzawa-Itoh K., Sugimura T., Misaki T., Tadehara Y., Yamamoto S.,
RA Hanada M., Yano N., Nakagawa T., Uene S., Yamada T., Aoyama H.,
RA Yamashita E., Tsukihara T., Yoshikawa S., Muramoto K.;
RT "Monomeric structure of an active form of bovine cytochrome c oxidase.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:19945-19951(2019).
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 COX4I1 (or
CC COX4I2), COX5A, COX5B, COX6A2 (or COX6A1), COX6B1 (or COX6B2), COX6C,
CC COX7A1 (or COX7A2), COX7B, COX7C, COX8B and NDUFA4, which are encoded
CC in the nuclear genome (PubMed:8638158). The complex exists as a monomer
CC or a 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)) (PubMed:26698328,
CC PubMed:27830641). {ECO:0000269|PubMed:26698328,
CC ECO:0000269|PubMed:27830641, ECO:0000269|PubMed:8638158}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}; Peripheral
CC membrane protein {ECO:0000269|PubMed:27605664,
CC ECO:0000269|PubMed:31533957}; Intermembrane side
CC {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 6B family.
CC {ECO:0000305}.
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DR EMBL; X15112; CAA33211.1; -; mRNA.
DR EMBL; BC102366; AAI02367.1; -; mRNA.
DR PIR; S05432; OGBO7.
DR RefSeq; NP_788848.1; NM_176675.3.
DR PDB; 1OCC; X-ray; 2.80 A; H/U=2-86.
DR PDB; 1OCO; X-ray; 2.80 A; H/U=2-86.
DR PDB; 1OCR; X-ray; 2.35 A; H/U=2-86.
DR PDB; 1OCZ; X-ray; 2.90 A; H/U=2-86.
DR PDB; 1V54; X-ray; 1.80 A; H/U=2-86.
DR PDB; 1V55; X-ray; 1.90 A; H/U=2-86.
DR PDB; 2DYR; X-ray; 1.80 A; H/U=2-86.
DR PDB; 2DYS; X-ray; 2.20 A; H/U=2-86.
DR PDB; 2EIJ; X-ray; 1.90 A; H/U=2-86.
DR PDB; 2EIK; X-ray; 2.10 A; H/U=2-86.
DR PDB; 2EIL; X-ray; 2.10 A; H/U=2-86.
DR PDB; 2EIM; X-ray; 2.60 A; H/U=2-86.
DR PDB; 2EIN; X-ray; 2.70 A; H/U=2-86.
DR PDB; 2OCC; X-ray; 2.30 A; H/U=2-86.
DR PDB; 2Y69; X-ray; 1.95 A; H/U=1-86.
DR PDB; 2YBB; EM; 19.00 A; S=2-86.
DR PDB; 2ZXW; X-ray; 2.50 A; H/U=2-86.
DR PDB; 3ABK; X-ray; 2.00 A; H/U=2-86.
DR PDB; 3ABL; X-ray; 2.10 A; H/U=2-86.
DR PDB; 3ABM; X-ray; 1.95 A; H/U=2-86.
DR PDB; 3AG1; X-ray; 2.20 A; H/U=2-86.
DR PDB; 3AG2; X-ray; 1.80 A; H/U=2-86.
DR PDB; 3AG3; X-ray; 1.80 A; H/U=2-86.
DR PDB; 3AG4; X-ray; 2.05 A; H/U=2-86.
DR PDB; 3ASN; X-ray; 3.00 A; H/U=2-86.
DR PDB; 3ASO; X-ray; 2.30 A; H/U=2-86.
DR PDB; 3WG7; X-ray; 1.90 A; H/U=2-86.
DR PDB; 3X2Q; X-ray; 2.00 A; H/U=2-86.
DR PDB; 5B1A; X-ray; 1.50 A; H/U=2-86.
DR PDB; 5B1B; X-ray; 1.60 A; H/U=2-86.
DR PDB; 5B3S; X-ray; 1.68 A; H/U=2-86.
DR PDB; 5GPN; EM; 5.40 A; 5=2-86.
DR PDB; 5IY5; X-ray; 2.00 A; H/U=8-86.
DR PDB; 5LUF; EM; 9.10 A; 5=2-86.
DR PDB; 5W97; X-ray; 2.30 A; H/h=2-86.
DR PDB; 5WAU; X-ray; 1.95 A; H/h=2-86.
DR PDB; 5X19; X-ray; 2.20 A; H/U=2-86.
DR PDB; 5X1B; X-ray; 2.40 A; H/U=2-86.
DR PDB; 5X1F; X-ray; 2.20 A; H/U=2-86.
DR PDB; 5XDQ; X-ray; 1.77 A; H/U=2-86.
DR PDB; 5XDX; X-ray; 1.99 A; H/U=2-86.
DR PDB; 5XTH; EM; 3.90 A; 4=12-86.
DR PDB; 5XTI; EM; 17.40 A; 4/B4=12-86.
DR PDB; 5Z84; X-ray; 1.85 A; H/U=2-86.
DR PDB; 5Z85; X-ray; 1.85 A; H/U=2-86.
DR PDB; 5Z86; X-ray; 1.85 A; H/U=2-86.
DR PDB; 5ZCO; X-ray; 1.90 A; H/U=2-86.
DR PDB; 5ZCP; X-ray; 1.65 A; H/U=2-86.
DR PDB; 5ZCQ; X-ray; 1.65 A; H/U=2-86.
DR PDB; 6J8M; X-ray; 1.90 A; H/U=2-86.
DR PDB; 6JUW; X-ray; 1.80 A; H/U=8-86.
DR PDB; 6JY3; X-ray; 1.85 A; H=2-86.
DR PDB; 6JY4; X-ray; 1.95 A; H=2-86.
DR PDB; 6NKN; X-ray; 2.50 A; H/U=2-86.
DR PDB; 6NMF; X-ray; 2.80 A; H/U=2-86.
DR PDB; 6NMP; X-ray; 2.90 A; H/U=2-86.
DR PDB; 7COH; X-ray; 1.30 A; H/U=2-86.
DR PDB; 7CP5; X-ray; 1.76 A; H/U=8-86.
DR PDB; 7D5W; X-ray; 1.84 A; H/U=8-86.
DR PDB; 7D5X; X-ray; 1.74 A; H/U=8-86.
DR PDB; 7EV7; X-ray; 1.70 A; H/U=2-86.
DR PDB; 7THU; X-ray; 1.93 A; HHH/UUU=2-86.
DR PDB; 7TIE; X-ray; 1.90 A; HHH/UUU=2-86.
DR PDB; 7TIH; X-ray; 2.35 A; HHH/UUU=2-86.
DR PDB; 7TII; X-ray; 2.45 A; HHH/UUU=2-86.
DR PDBsum; 1OCC; -.
DR PDBsum; 1OCO; -.
DR PDBsum; 1OCR; -.
DR PDBsum; 1OCZ; -.
DR PDBsum; 1V54; -.
DR PDBsum; 1V55; -.
DR PDBsum; 2DYR; -.
DR PDBsum; 2DYS; -.
DR PDBsum; 2EIJ; -.
DR PDBsum; 2EIK; -.
DR PDBsum; 2EIL; -.
DR PDBsum; 2EIM; -.
DR PDBsum; 2EIN; -.
DR PDBsum; 2OCC; -.
DR PDBsum; 2Y69; -.
DR PDBsum; 2YBB; -.
DR PDBsum; 2ZXW; -.
DR PDBsum; 3ABK; -.
DR PDBsum; 3ABL; -.
DR PDBsum; 3ABM; -.
DR PDBsum; 3AG1; -.
DR PDBsum; 3AG2; -.
DR PDBsum; 3AG3; -.
DR PDBsum; 3AG4; -.
DR PDBsum; 3ASN; -.
DR PDBsum; 3ASO; -.
DR PDBsum; 3WG7; -.
DR PDBsum; 3X2Q; -.
DR PDBsum; 5B1A; -.
DR PDBsum; 5B1B; -.
DR PDBsum; 5B3S; -.
DR PDBsum; 5GPN; -.
DR PDBsum; 5IY5; -.
DR PDBsum; 5LUF; -.
DR PDBsum; 5W97; -.
DR PDBsum; 5WAU; -.
DR PDBsum; 5X19; -.
DR PDBsum; 5X1B; -.
DR PDBsum; 5X1F; -.
DR PDBsum; 5XDQ; -.
DR PDBsum; 5XDX; -.
DR PDBsum; 5XTH; -.
DR PDBsum; 5XTI; -.
DR PDBsum; 5Z84; -.
DR PDBsum; 5Z85; -.
DR PDBsum; 5Z86; -.
DR PDBsum; 5ZCO; -.
DR PDBsum; 5ZCP; -.
DR PDBsum; 5ZCQ; -.
DR PDBsum; 6J8M; -.
DR PDBsum; 6JUW; -.
DR PDBsum; 6JY3; -.
DR PDBsum; 6JY4; -.
DR PDBsum; 6NKN; -.
DR PDBsum; 6NMF; -.
DR PDBsum; 6NMP; -.
DR PDBsum; 7COH; -.
DR PDBsum; 7CP5; -.
DR PDBsum; 7D5W; -.
DR PDBsum; 7D5X; -.
DR PDBsum; 7EV7; -.
DR PDBsum; 7THU; -.
DR PDBsum; 7TIE; -.
DR PDBsum; 7TIH; -.
DR PDBsum; 7TII; -.
DR AlphaFoldDB; P00429; -.
DR SMR; P00429; -.
DR CORUM; P00429; -.
DR DIP; DIP-38988N; -.
DR IntAct; P00429; 3.
DR iPTMnet; P00429; -.
DR PaxDb; P00429; -.
DR PeptideAtlas; P00429; -.
DR PRIDE; P00429; -.
DR GeneID; 100270792; -.
DR KEGG; bta:100270792; -.
DR CTD; 1340; -.
DR eggNOG; KOG3057; Eukaryota.
DR InParanoid; P00429; -.
DR OrthoDB; 1586678at2759; -.
DR BRENDA; 7.1.1.9; 908.
DR UniPathway; UPA00705; -.
DR EvolutionaryTrace; P00429; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:AgBase.
DR GO; GO:0005739; C:mitochondrion; ISS:AgBase.
DR GO; GO:0045277; C:respiratory chain complex IV; IDA:UniProtKB.
DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR CDD; cd00926; Cyt_c_Oxidase_VIb; 1.
DR Gene3D; 1.10.10.140; -; 1.
DR InterPro; IPR003213; Cyt_c_oxidase_su6B.
DR InterPro; IPR036549; Cyt_c_oxidase_su6B_sf.
DR PANTHER; PTHR11387; PTHR11387; 1.
DR Pfam; PF02297; COX6B; 1.
DR PIRSF; PIRSF000278; Cyt_c_oxidase_6B; 1.
DR SUPFAM; SSF47694; SSF47694; 1.
DR PROSITE; PS51808; CHCH; 1.
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:0000269|PubMed:229067,
FT ECO:0000269|PubMed:6262305"
FT CHAIN 2..86
FT /note="Cytochrome c oxidase subunit 6B1"
FT /id="PRO_0000194911"
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:0000269|PubMed:6262305"
FT MOD_RES 62
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P56391"
FT DISULFID 30..65
FT /evidence="ECO:0000269|PubMed:20385840,
FT ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957,
FT ECO:0000269|PubMed:8638158"
FT DISULFID 40..54
FT /evidence="ECO:0000269|PubMed:20385840,
FT ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957,
FT ECO:0000269|PubMed:8638158"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 27..46
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 55..64
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 67..79
FT /evidence="ECO:0007829|PDB:7COH"
SQ SEQUENCE 86 AA; 10156 MW; A8933C01C71ACB8B CRC64;
MAEDIQAKIK NYQTAPFDSR FPNQNQTRNC WQNYLDFHRC EKAMTAKGGD VSVCEWYRRV
YKSLCPISWV STWDDRRAEG TFPGKI
