CX6A1_BOVIN
ID CX6A1_BOVIN Reviewed; 109 AA.
AC P13182; Q24JY9;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Cytochrome c oxidase subunit 6A1, mitochondrial;
DE AltName: Full=Cytochrome c oxidase polypeptide VIa-liver;
DE AltName: Full=Cytochrome c oxidase subunit SSG;
DE Flags: Precursor;
GN Name=COX6A1;
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 [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-109.
RC TISSUE=Liver;
RX PubMed=1720401; DOI=10.1016/0014-5793(91)80839-u;
RA Ewart G.D., Zhang Y.-Z., Capaldi R.A.;
RT "Switching of bovine cytochrome c oxidase subunit VIa isoforms in skeletal
RT muscle during development.";
RL FEBS Lett. 292:79-84(1991).
RN [3]
RP PROTEIN SEQUENCE OF 25-56.
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 unsing 4 electrons from cytochrome c in the IMS and 4
CC protons from the mitochondrial matrix. {ECO:0000250|UniProtKB:P32799}.
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 (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 {ECO:0000250|UniProtKB:P12074}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P12074}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P12074}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 6A family.
CC {ECO:0000305}.
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DR EMBL; BC114182; AAI14183.1; -; mRNA.
DR EMBL; M38520; AAA30437.1; -; mRNA.
DR PIR; S18314; S18314.
DR RefSeq; NP_001071299.1; NM_001077831.2.
DR AlphaFoldDB; P13182; -.
DR SMR; P13182; -.
DR CORUM; P13182; -.
DR STRING; 9913.ENSBTAP00000016993; -.
DR PaxDb; P13182; -.
DR PRIDE; P13182; -.
DR Ensembl; ENSBTAT00000071537; ENSBTAP00000072266; ENSBTAG00000012788.
DR GeneID; 282199; -.
DR KEGG; bta:282199; -.
DR CTD; 1337; -.
DR VEuPathDB; HostDB:ENSBTAG00000012788; -.
DR eggNOG; KOG3469; Eukaryota.
DR GeneTree; ENSGT00940000154612; -.
DR HOGENOM; CLU_122515_1_1_1; -.
DR InParanoid; P13182; -.
DR OMA; GYEGHDE; -.
DR OrthoDB; 1591077at2759; -.
DR TreeFam; TF105064; -.
DR Reactome; R-BTA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-BTA-611105; Respiratory electron transport.
DR Reactome; R-BTA-9707564; Cytoprotection by HMOX1.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000012788; Expressed in retina and 104 other tissues.
DR ExpressionAtlas; P13182; baseline and differential.
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: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 Direct protein sequencing; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Oxidoreductase; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2844245"
FT CHAIN 25..109
FT /note="Cytochrome c oxidase subunit 6A1, mitochondrial"
FT /id="PRO_0000193447"
FT TOPO_DOM 25..34
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P07471"
FT TRANSMEM 35..59
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P07471"
FT TOPO_DOM 60..109
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P07471"
FT CONFLICT 43
FT /note="Y -> L (in Ref. 2; AAA30437)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="V -> L (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="M -> T (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="L -> M (in Ref. 2; AAA30437)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 109 AA; 12073 MW; 35454123D34A4258 CRC64;
MAAAAGSRVF GLLGRSRLQL SRCMSSGAHG EEGSARMWKA LTYFVALPGV GVSMLNVFLK
SHHGEEERPE FVAYPHLRIR SKPFPWGDGN HTLFHNPHVN PLPTGYEDE