COX8B_BOVIN
ID COX8B_BOVIN Reviewed; 70 AA.
AC P10175; Q2KI98;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Cytochrome c oxidase subunit 8B, mitochondrial;
DE AltName: Full=Cytochrome c oxidase polypeptide VIII-heart;
DE AltName: Full=Cytochrome c oxidase subunit 8-1;
DE AltName: Full=Cytochrome c oxidase subunit 8H;
DE AltName: Full=IX;
DE AltName: Full=VIIIb;
DE Flags: Precursor;
GN Name=COX8B; Synonyms=COX8H;
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=1689292; DOI=10.1016/s0021-9258(19)39854-0;
RA Lightowlers R.N., Ewart G.D., Aggeler R.J., Zhang Y.-Z., Calavetta L.,
RA Capaldi R.A.;
RT "Isolation and characterization of the cDNAs encoding two isoforms of
RT subunit CIX of bovine cytochrome c oxidase.";
RL J. Biol. Chem. 265:2677-2681(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7766994; DOI=10.1007/bf00303255;
RA Lomax M.I., Riggs P.K., Womack J.E.;
RT "Structure and chromosomal location of the bovine gene for the heart muscle
RT isoform of cytochrome c oxidase subunit VIII.";
RL Mamm. Genome 6:118-122(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Rumen;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 25-70.
RC TISSUE=Heart;
RX PubMed=6327490; DOI=10.1515/bchm2.1984.365.1.313;
RA Meinecke L., Steffens G.J., Buse G.;
RT "Studies on cytochrome c oxidase, X. Isolation and amino-acid sequence of
RT polypeptide VIIIb.";
RL Hoppe-Seyler's Z. Physiol. Chem. 365:313-320(1984).
RN [5]
RP PROTEIN SEQUENCE OF 25-30.
RC TISSUE=Heart;
RX PubMed=2176624; DOI=10.1016/0014-5793(90)80817-3;
RA Anthony G., Stroh A., Lottspeich F., Kadenbach B.;
RT "Different isozymes of cytochrome c oxidase are expressed in bovine smooth
RT muscle and skeletal or heart muscle.";
RL FEBS Lett. 277:97-100(1990).
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) OF 25-70.
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) OF 25-70.
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) OF 25-70.
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).
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).
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).
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:0000269|PubMed:27605664}.
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000305|PubMed:27605664}.
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}; Single-pass
CC membrane protein {ECO:0000269|PubMed:27605664,
CC ECO:0000269|PubMed:31533957}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase VIII family.
CC {ECO:0000305}.
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DR EMBL; J05202; AAA30466.1; -; mRNA.
DR EMBL; U15540; AAA80279.1; -; Genomic_DNA.
DR EMBL; BC112717; AAI12718.1; -; mRNA.
DR PIR; A35537; OSBO8.
DR RefSeq; NP_001107989.1; NM_001114517.2.
DR PDB; 1OCC; X-ray; 2.80 A; M/Z=25-70.
DR PDB; 1OCO; X-ray; 2.80 A; M/Z=25-70.
DR PDB; 1OCR; X-ray; 2.35 A; M/Z=25-70.
DR PDB; 1OCZ; X-ray; 2.90 A; M/Z=25-70.
DR PDB; 1V54; X-ray; 1.80 A; M/Z=25-70.
DR PDB; 1V55; X-ray; 1.90 A; M/Z=25-70.
DR PDB; 2DYR; X-ray; 1.80 A; M/Z=25-70.
DR PDB; 2DYS; X-ray; 2.20 A; M/Z=25-70.
DR PDB; 2EIJ; X-ray; 1.90 A; M/Z=25-70.
DR PDB; 2EIK; X-ray; 2.10 A; M/Z=25-70.
DR PDB; 2EIL; X-ray; 2.10 A; M/Z=25-70.
DR PDB; 2EIM; X-ray; 2.60 A; M/Z=25-70.
DR PDB; 2EIN; X-ray; 2.70 A; M/Z=25-70.
DR PDB; 2OCC; X-ray; 2.30 A; M/Z=25-70.
DR PDB; 2Y69; X-ray; 1.95 A; M/Z=1-70.
DR PDB; 2YBB; EM; 19.00 A; X=25-70.
DR PDB; 2ZXW; X-ray; 2.50 A; M/Z=25-70.
DR PDB; 3ABK; X-ray; 2.00 A; M/Z=25-70.
DR PDB; 3ABL; X-ray; 2.10 A; M/Z=25-70.
DR PDB; 3ABM; X-ray; 1.95 A; M/Z=25-70.
DR PDB; 3AG1; X-ray; 2.20 A; M/Z=25-70.
DR PDB; 3AG2; X-ray; 1.80 A; M/Z=25-70.
DR PDB; 3AG3; X-ray; 1.80 A; M/Z=25-70.
DR PDB; 3AG4; X-ray; 2.05 A; M/Z=25-70.
DR PDB; 3ASN; X-ray; 3.00 A; M/Z=25-70.
DR PDB; 3ASO; X-ray; 2.30 A; M/Z=25-70.
DR PDB; 3WG7; X-ray; 1.90 A; M/Z=25-70.
DR PDB; 3X2Q; X-ray; 2.00 A; M/Z=25-70.
DR PDB; 5B1A; X-ray; 1.50 A; M/Z=25-70.
DR PDB; 5B1B; X-ray; 1.60 A; M/Z=25-70.
DR PDB; 5B3S; X-ray; 1.68 A; M/Z=25-70.
DR PDB; 5GPN; EM; 5.40 A; s=25-70.
DR PDB; 5IY5; X-ray; 2.00 A; M/Z=25-67.
DR PDB; 5LUF; EM; 9.10 A; 0=25-70.
DR PDB; 5W97; X-ray; 2.30 A; M/m=25-70.
DR PDB; 5WAU; X-ray; 1.95 A; M/m=25-70.
DR PDB; 5X19; X-ray; 2.20 A; M/Z=25-70.
DR PDB; 5X1B; X-ray; 2.40 A; M/Z=25-70.
DR PDB; 5X1F; X-ray; 2.20 A; M/Z=25-70.
DR PDB; 5XDQ; X-ray; 1.77 A; M/Z=25-70.
DR PDB; 5XDX; X-ray; 1.99 A; M/Z=25-70.
DR PDB; 5XTH; EM; 3.90 A; 9=25-67.
DR PDB; 5XTI; EM; 17.40 A; 9/B9=25-67.
DR PDB; 5Z84; X-ray; 1.85 A; M/Z=25-70.
DR PDB; 5Z85; X-ray; 1.85 A; M/Z=25-70.
DR PDB; 5Z86; X-ray; 1.85 A; M/Z=25-70.
DR PDB; 5ZCO; X-ray; 1.90 A; M/Z=25-70.
DR PDB; 5ZCP; X-ray; 1.65 A; M/Z=25-70.
DR PDB; 5ZCQ; X-ray; 1.65 A; M/Z=25-70.
DR PDB; 6J8M; X-ray; 1.90 A; M/Z=25-70.
DR PDB; 6JUW; X-ray; 1.80 A; M/Z=25-67.
DR PDB; 6JY3; X-ray; 1.85 A; M=25-70.
DR PDB; 6JY4; X-ray; 1.95 A; M=25-70.
DR PDB; 6NKN; X-ray; 2.50 A; M/Z=25-70.
DR PDB; 6NMF; X-ray; 2.80 A; M/Z=25-70.
DR PDB; 6NMP; X-ray; 2.90 A; M/Z=25-70.
DR PDB; 7COH; X-ray; 1.30 A; M/Z=25-70.
DR PDB; 7CP5; X-ray; 1.76 A; M/Z=25-67.
DR PDB; 7D5W; X-ray; 1.84 A; M/Z=25-67.
DR PDB; 7D5X; X-ray; 1.74 A; M/Z=25-67.
DR PDB; 7EV7; X-ray; 1.70 A; M/Z=25-70.
DR PDB; 7THU; X-ray; 1.93 A; MMM/ZZZ=25-70.
DR PDB; 7TIE; X-ray; 1.90 A; MMM/ZZZ=25-70.
DR PDB; 7TIH; X-ray; 2.35 A; MMM/ZZZ=25-70.
DR PDB; 7TII; X-ray; 2.45 A; MMM/ZZZ=25-70.
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; P10175; -.
DR SMR; P10175; -.
DR CORUM; P10175; -.
DR DIP; DIP-60941N; -.
DR IntAct; P10175; 1.
DR STRING; 9913.ENSBTAP00000002651; -.
DR PaxDb; P10175; -.
DR GeneID; 615757; -.
DR KEGG; bta:615757; -.
DR CTD; 12869; -.
DR eggNOG; ENOG502SB3F; Eukaryota.
DR HOGENOM; CLU_203368_0_0_1; -.
DR InParanoid; P10175; -.
DR OrthoDB; 1632471at2759; -.
DR TreeFam; TF105070; -.
DR BRENDA; 7.1.1.9; 908.
DR UniPathway; UPA00705; -.
DR EvolutionaryTrace; P10175; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IEA:InterPro.
DR GO; GO:0045277; C:respiratory chain complex IV; IDA:UniProtKB.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IEA:InterPro.
DR DisProt; DP00780; -.
DR Gene3D; 4.10.81.10; -; 1.
DR InterPro; IPR003205; Cyt_c_oxidase_su8.
DR InterPro; IPR036548; Cyt_c_oxidase_su8_sf.
DR PANTHER; PTHR16717; PTHR16717; 1.
DR Pfam; PF02285; COX8; 1.
DR SUPFAM; SSF81431; SSF81431; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2176624,
FT ECO:0000269|PubMed:6327490"
FT CHAIN 25..70
FT /note="Cytochrome c oxidase subunit 8B, mitochondrial"
FT /id="PRO_0000006176"
FT TOPO_DOM 25..35
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TRANSMEM 36..59
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TOPO_DOM 60..70
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:27605664"
FT CONFLICT 19
FT /note="A -> V (in Ref. 1; AAA30466)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="K -> R (in Ref. 1; AAA30466)"
FT /evidence="ECO:0000305"
FT HELIX 36..59
FT /evidence="ECO:0007829|PDB:7COH"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:7COH"
SQ SEQUENCE 70 AA; 7639 MW; 17BE70ADEC45FDD8 CRC64;
MLRLAPTVRL LQAPLRGWAV PKAHITAKPA KTPTSPKEQA IGLSVTFLSF LLPAGWVLYH
LDNYKKSSAA
