CX7A2_BOVIN
ID CX7A2_BOVIN Reviewed; 83 AA.
AC P13184; Q3SZX6;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Cytochrome c oxidase subunit 7A2, mitochondrial;
DE AltName: Full=Cytochrome c oxidase subunit VIIa-liver/heart;
DE Short=Cytochrome c oxidase subunit VIIa-L;
DE Flags: Precursor;
GN Name=COX7A2; Synonyms=COX7AL;
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].
RX PubMed=2549516; DOI=10.1093/nar/17.15.6410;
RA Seelan R.S., Scheuner D., Lomax M.I., Grossman L.I.;
RT "Nucleotide sequence of a cDNA for bovine cytochrome c oxidase subunit
RT VIIa.";
RL Nucleic Acids Res. 17:6410-6410(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SEQUENCE REVISION.
RX PubMed=1717471; DOI=10.1016/s0021-9258(18)55056-0;
RA Seelan R.S., Grossman L.I.;
RT "Cytochrome c oxidase subunit VIIa isoforms. Characterization and
RT expression of bovine cDNAs.";
RL J. Biol. Chem. 266:19752-19757(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8307562; DOI=10.1016/s0888-7543(11)80009-1;
RA Seelan R.S., Grossman L.I.;
RT "Structural organization and evolution of the liver isoform gene for bovine
RT cytochrome c oxidase subunit VIIa.";
RL Genomics 18:527-536(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 24-60.
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).
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:P10174}.
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000250|UniProtKB:P10174}.
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 (By similarity). 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)) (By similarity).
CC Interacts with PET100 (By similarity). {ECO:0000250|UniProtKB:P14406}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P10174}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P10174}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase VIIa family.
CC {ECO:0000305}.
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DR EMBL; X15235; CAA33313.1; -; mRNA.
DR EMBL; L09603; AAA18218.1; -; Genomic_DNA.
DR EMBL; BC102664; AAI02665.1; -; mRNA.
DR PIR; A49355; A49355.
DR RefSeq; NP_787001.1; NM_175807.1.
DR AlphaFoldDB; P13184; -.
DR SMR; P13184; -.
DR CORUM; P13184; -.
DR STRING; 9913.ENSBTAP00000006715; -.
DR PaxDb; P13184; -.
DR PeptideAtlas; P13184; -.
DR PRIDE; P13184; -.
DR GeneID; 327688; -.
DR KEGG; bta:327688; -.
DR CTD; 1347; -.
DR eggNOG; ENOG502S4DT; Eukaryota.
DR HOGENOM; CLU_173437_0_0_1; -.
DR InParanoid; P13184; -.
DR OrthoDB; 1548349at2759; -.
DR TreeFam; TF105067; -.
DR BRENDA; 7.1.1.9; 908.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005746; C:mitochondrial respirasome; IBA:GO_Central.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IEA:InterPro.
DR GO; GO:0097250; P:mitochondrial respirasome assembly; IBA:GO_Central.
DR GO; GO:0002082; P:regulation of oxidative phosphorylation; IBA:GO_Central.
DR CDD; cd00928; Cyt_c_Oxidase_VIIa; 1.
DR Gene3D; 4.10.91.10; -; 1.
DR InterPro; IPR039297; COX7a.
DR InterPro; IPR036539; Cyt_c_oxidase_su7a_sf.
DR InterPro; IPR003177; Cytc_oxidase_su7a_met.
DR PANTHER; PTHR10510; PTHR10510; 1.
DR Pfam; PF02238; COX7a; 1.
DR SUPFAM; SSF81419; SSF81419; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Oxidoreductase; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2844245"
FT CHAIN 24..83
FT /note="Cytochrome c oxidase subunit 7A2, mitochondrial"
FT /id="PRO_0000006144"
FT TOPO_DOM 24..48
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P14406"
FT TRANSMEM 49..77
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P07470"
FT TOPO_DOM 78..83
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P14406"
FT MOD_RES 33
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48771"
FT CONFLICT 52..53
FT /note="AL -> NI (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="L -> R (in Ref. 1; CAA33313)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="A -> V (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="L -> M (in Ref. 4; AAI02665 and 5; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 83 AA; 9305 MW; 254D7610F2EF106F CRC64;
MLRNLLALRQ IAKRTISTSS RRQFENKVPE KQKLFQEDNG IPVHLKGGIA DALLYRATLI
LTVGGTAYAM YELAVASFPK KQD
