CX6C1_THUOB
ID CX6C1_THUOB Reviewed; 76 AA.
AC P80977; Q71SZ9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Cytochrome c oxidase subunit 6C-1;
DE AltName: Full=Cytochrome c oxidase polypeptide VIc-1;
OS Thunnus obesus (Bigeye tuna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Pelagiaria; Scombriformes; Scombridae; Thunnus.
OX NCBI_TaxID=8241;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Weisheit G., Huettemann M., Kadenbach B.;
RT "Evolution of nuclear coded cytochrome c oxidase subunit VIc of fishes.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-14; 35-43 AND 51-76.
RC TISSUE=Heart, and Liver;
RX PubMed=9310366; DOI=10.1111/j.1432-1033.1997.t01-1-00099.x;
RA Arnold S., Lee I., Kim M., Song E., Linder D., Lottspeich F., Kadenbach B.;
RT "The subunit structure of cytochrome-c oxidase from tuna heart and liver.";
RL Eur. J. Biochem. 248:99-103(1997).
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:P04038}.
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000250|UniProtKB:P04038}.
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 COX4I, COX5A,
CC COX5B, COX6A, COX6B, COX6C, COX7A, COX7B, COX7C, COX8 and NDUFA4, which
CC are encoded in the nuclear genome. The complex exists as a monomer or a
CC 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)).
CC {ECO:0000250|UniProtKB:P04038}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P04038}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P04038}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 6c family.
CC {ECO:0000305}.
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DR EMBL; AF255348; AAQ14272.1; -; mRNA.
DR PIR; S77986; S77986.
DR AlphaFoldDB; P80977; -.
DR SMR; P80977; -.
DR UniPathway; UPA00705; -.
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:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IEA:InterPro.
DR CDD; cd00927; Cyt_c_Oxidase_VIc; 1.
DR Gene3D; 4.10.93.10; -; 1.
DR InterPro; IPR004204; COX6C.
DR InterPro; IPR034884; Cytochrome_c_oxidase_VIc/VIIs.
DR InterPro; IPR037169; Cytochrome_c_oxidase_VIc_sf.
DR Pfam; PF02937; COX6C; 1.
DR SUPFAM; SSF81415; SSF81415; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9310366"
FT CHAIN 2..76
FT /note="Cytochrome c oxidase subunit 6C-1"
FT /id="PRO_0000191306"
FT TOPO_DOM 2..10
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P04038"
FT TRANSMEM 11..51
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P04038"
FT TOPO_DOM 52..76
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P04038"
FT CONFLICT 2..3
FT /note="SL -> LK (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="K -> KK (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="E -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 76 AA; 8543 MW; 7541F9E60EDDFA01 CRC64;
MSLAKPAMRG LLGKRLRFHL PIAFTLSLVA ALGFKYGVTE PRKQAYADFY KQYDAVKDFN
AMREAGIFES VRPSGE
