CX6A2_BOVIN
ID CX6A2_BOVIN Reviewed; 97 AA.
AC P07471; Q3SZ61;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Cytochrome c oxidase subunit 6A2, mitochondrial;
DE AltName: Full=Cytochrome c oxidase polypeptide VIa-heart;
DE Short=COXVIAH;
DE AltName: Full=Cytochrome c oxidase polypeptide VIb;
DE Flags: Precursor;
GN Name=COX6A2; Synonyms=COX6A;
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=1647214; DOI=10.1016/0167-4781(91)90022-e;
RA Smith E.O., Bement D.M., Grossman L.I., Lomax M.I.;
RT "The cDNA for the heart/muscle isoform of bovine cytochrome c oxidase
RT subunit VIa encodes a presequence.";
RL Biochim. Biophys. Acta 1089:266-268(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7687470; DOI=10.1016/0167-4781(93)90092-r;
RA Smith E.O., Lomax M.I.;
RT "Structural organization of the bovine gene for the heart/muscle isoform of
RT cytochrome c oxidase subunit VIa.";
RL Biochim. Biophys. Acta 1174:63-71(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 13-96.
RC TISSUE=Heart;
RX PubMed=2994692; DOI=10.1515/bchm3.1985.366.2.687;
RA Meinecke L., Buse G.;
RT "Studies on cytochrome c oxidase, XII. Isolation and primary structure of
RT polypeptide VIb from bovine heart.";
RL Biol. Chem. Hoppe-Seyler 366:687-694(1985).
RN [5]
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 [6]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
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 [7]
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 [8]
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 [9]
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 [10]
RP STRUCTURE BY ELECTRON MICROSCOPY (9.10 ANGSTROMS) OF 13-96.
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 [11]
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 [12]
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 unsing 4 electrons from cytochrome c in the IMS and 4
CC protons from the mitochondrial matrix. Plays a role in the assembly and
CC stabilization of complex IV (By similarity).
CC {ECO:0000250|UniProtKB:P32799, ECO:0000250|UniProtKB:P43023}.
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000250|UniProtKB:P32799}.
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 -!- TISSUE SPECIFICITY: Heart/muscle specific isoform.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 6A family.
CC {ECO:0000305}.
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DR EMBL; X56857; CAA40183.1; -; mRNA.
DR EMBL; S64127; AAB27605.1; -; Genomic_DNA.
DR EMBL; BC103117; AAI03118.1; -; mRNA.
DR PIR; S35702; OGBO6.
DR RefSeq; NP_776947.1; NM_174522.3.
DR PDB; 1OCC; X-ray; 2.80 A; G/T=13-96.
DR PDB; 1OCO; X-ray; 2.80 A; G/T=13-96.
DR PDB; 1OCR; X-ray; 2.35 A; G/T=13-96.
DR PDB; 1OCZ; X-ray; 2.90 A; G/T=13-96.
DR PDB; 1V54; X-ray; 1.80 A; G/T=13-97.
DR PDB; 1V55; X-ray; 1.90 A; G/T=13-97.
DR PDB; 2DYR; X-ray; 1.80 A; G/T=13-97.
DR PDB; 2DYS; X-ray; 2.20 A; G/T=13-97.
DR PDB; 2EIJ; X-ray; 1.90 A; G/T=13-97.
DR PDB; 2EIK; X-ray; 2.10 A; G/T=13-97.
DR PDB; 2EIL; X-ray; 2.10 A; G/T=13-97.
DR PDB; 2EIM; X-ray; 2.60 A; G/T=13-97.
DR PDB; 2EIN; X-ray; 2.70 A; G/T=13-97.
DR PDB; 2OCC; X-ray; 2.30 A; G/T=13-96.
DR PDB; 2Y69; X-ray; 1.95 A; G/T=1-97.
DR PDB; 2YBB; EM; 19.00 A; R=13-96.
DR PDB; 2ZXW; X-ray; 2.50 A; G/T=13-97.
DR PDB; 3ABK; X-ray; 2.00 A; G/T=13-97.
DR PDB; 3ABL; X-ray; 2.10 A; G/T=13-97.
DR PDB; 3ABM; X-ray; 1.95 A; G/T=13-97.
DR PDB; 3AG1; X-ray; 2.20 A; G/T=13-97.
DR PDB; 3AG2; X-ray; 1.80 A; G/T=13-97.
DR PDB; 3AG3; X-ray; 1.80 A; G/T=13-97.
DR PDB; 3AG4; X-ray; 2.05 A; G/T=13-97.
DR PDB; 3ASN; X-ray; 3.00 A; G/T=13-97.
DR PDB; 3ASO; X-ray; 2.30 A; G/T=13-97.
DR PDB; 3WG7; X-ray; 1.90 A; G/T=13-97.
DR PDB; 3X2Q; X-ray; 2.00 A; G/T=13-97.
DR PDB; 5B1A; X-ray; 1.50 A; G/T=13-97.
DR PDB; 5B1B; X-ray; 1.60 A; G/T=13-97.
DR PDB; 5B3S; X-ray; 1.68 A; G/T=13-97.
DR PDB; 5GPN; EM; 5.40 A; 4=13-96.
DR PDB; 5IY5; X-ray; 2.00 A; G/T=13-96.
DR PDB; 5LUF; EM; 9.10 A; 4=13-96.
DR PDB; 5W97; X-ray; 2.30 A; G/g=13-97.
DR PDB; 5WAU; X-ray; 1.95 A; G/g=13-97.
DR PDB; 5X19; X-ray; 2.20 A; G/T=13-97.
DR PDB; 5X1B; X-ray; 2.40 A; G/T=13-97.
DR PDB; 5X1F; X-ray; 2.20 A; G/T=13-97.
DR PDB; 5XDQ; X-ray; 1.77 A; G/T=13-97.
DR PDB; 5XDX; X-ray; 1.99 A; G/T=13-97.
DR PDB; 5XTH; EM; 3.90 A; 3=13-96.
DR PDB; 5XTI; EM; 17.40 A; 3/B3=13-96.
DR PDB; 5Z84; X-ray; 1.85 A; G/T=13-97.
DR PDB; 5Z85; X-ray; 1.85 A; G/T=13-97.
DR PDB; 5Z86; X-ray; 1.85 A; G/T=13-97.
DR PDB; 5ZCO; X-ray; 1.90 A; G/T=13-97.
DR PDB; 5ZCP; X-ray; 1.65 A; G/T=13-97.
DR PDB; 5ZCQ; X-ray; 1.65 A; G/T=13-97.
DR PDB; 6J8M; X-ray; 1.90 A; G/T=13-97.
DR PDB; 6JUW; X-ray; 1.80 A; G/T=13-96.
DR PDB; 6JY3; X-ray; 1.85 A; G=13-97.
DR PDB; 6JY4; X-ray; 1.95 A; G=13-97.
DR PDB; 6NKN; X-ray; 2.50 A; G/T=13-97.
DR PDB; 6NMF; X-ray; 2.80 A; G/T=13-97.
DR PDB; 6NMP; X-ray; 2.90 A; G/T=13-97.
DR PDB; 7COH; X-ray; 1.30 A; G/T=13-97.
DR PDB; 7CP5; X-ray; 1.76 A; G/T=13-96.
DR PDB; 7D5W; X-ray; 1.84 A; G/T=13-96.
DR PDB; 7D5X; X-ray; 1.74 A; G/T=13-96.
DR PDB; 7EV7; X-ray; 1.70 A; G/T=13-97.
DR PDB; 7THU; X-ray; 1.93 A; GGG/TTT=13-97.
DR PDB; 7TIE; X-ray; 1.90 A; GGG/TTT=13-97.
DR PDB; 7TIH; X-ray; 2.35 A; GGG/TTT=13-97.
DR PDB; 7TII; X-ray; 2.45 A; GGG/TTT=13-97.
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; P07471; -.
DR SMR; P07471; -.
DR CORUM; P07471; -.
DR DIP; DIP-39018N; -.
DR IntAct; P07471; 2.
DR STRING; 9913.ENSBTAP00000026002; -.
DR PaxDb; P07471; -.
DR PRIDE; P07471; -.
DR Ensembl; ENSBTAT00000026002; ENSBTAP00000026002; ENSBTAG00000019521.
DR GeneID; 282200; -.
DR KEGG; bta:282200; -.
DR CTD; 1339; -.
DR VEuPathDB; HostDB:ENSBTAG00000019521; -.
DR VGNC; VGNC:27637; COX6A2.
DR eggNOG; KOG3469; Eukaryota.
DR GeneTree; ENSGT00940000162257; -.
DR HOGENOM; CLU_122515_1_1_1; -.
DR InParanoid; P07471; -.
DR OMA; IRTKPYC; -.
DR OrthoDB; 1591077at2759; -.
DR TreeFam; TF105064; -.
DR BRENDA; 7.1.1.9; 908.
DR UniPathway; UPA00705; -.
DR EvolutionaryTrace; P07471; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000019521; Expressed in laryngeal cartilage and 44 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IBA:GO_Central.
DR GO; GO:0045277; C:respiratory chain complex IV; IDA:UniProtKB.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR CDD; cd00925; Cyt_c_Oxidase_VIa; 1.
DR Gene3D; 4.10.95.10; -; 1.
DR InterPro; IPR001349; Cyt_c_oxidase_su6a.
DR InterPro; IPR018507; Cyt_c_oxidase_su6a_CS.
DR InterPro; IPR036418; Cyt_c_oxidase_su6a_sf.
DR PANTHER; PTHR11504; PTHR11504; 1.
DR Pfam; PF02046; COX6A; 1.
DR PIRSF; PIRSF000277; COX6A1; 1.
DR SUPFAM; SSF81411; SSF81411; 1.
DR PROSITE; PS01329; COX6A; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Oxidoreductase; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..12
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2994692"
FT CHAIN 13..97
FT /note="Cytochrome c oxidase subunit 6A2, mitochondrial"
FT /id="PRO_0000006115"
FT TOPO_DOM 13..24
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TRANSMEM 25..49
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TOPO_DOM 50..97
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:27605664"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:1OCR"
FT HELIX 25..34
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 36..50
FT /evidence="ECO:0007829|PDB:7COH"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:7COH"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:7COH"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:1OCC"
SQ SEQUENCE 97 AA; 10800 MW; 59B408A1B9B6AF4F CRC64;
MALPLKSLSR GLASAAKGDH GGTGARTWRF LTFGLALPSV ALCTLNSWLH SGHRERPAFI
PYHHLRIRTK PFSWGDGNHT FFHNPRVNPL PTGYEKP
