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COX6A_CAEEL
ID   COX6A_CAEEL             Reviewed;         128 AA.
AC   Q20779;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Cytochrome c oxidase subunit 6A, mitochondrial {ECO:0000305};
DE   AltName: Full=Cytochrome c oxidase polypeptide VIa {ECO:0000305};
DE   Flags: Precursor;
GN   Name=cox-6A {ECO:0000312|WormBase:F54D8.2};
GN   Synonyms=tag-174 {ECO:0000312|WormBase:F54D8.2};
GN   ORFNames=F54D8.2 {ECO:0000312|WormBase:F54D8.2};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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 a catalytic core of 3 subunits and
CC       several supernumerary subunits. The complex exists as a monomer or a
CC       dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC       membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1
CC       complex, complex III, CIII). {ECO:0000250|UniProtKB:P32799}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P32799}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:P32799}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 6A family.
CC       {ECO:0000305}.
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DR   EMBL; BX284603; CCD67407.1; -; Genomic_DNA.
DR   PIR; E88449; E88449.
DR   RefSeq; NP_498082.1; NM_065681.5.
DR   AlphaFoldDB; Q20779; -.
DR   SMR; Q20779; -.
DR   BioGRID; 40925; 57.
DR   IntAct; Q20779; 1.
DR   MINT; Q20779; -.
DR   STRING; 6239.F54D8.2.1; -.
DR   EPD; Q20779; -.
DR   PaxDb; Q20779; -.
DR   PeptideAtlas; Q20779; -.
DR   EnsemblMetazoa; F54D8.2.1; F54D8.2.1; WBGene00006519.
DR   EnsemblMetazoa; F54D8.2.2; F54D8.2.2; WBGene00006519.
DR   EnsemblMetazoa; F54D8.2.3; F54D8.2.3; WBGene00006519.
DR   EnsemblMetazoa; F54D8.2.4; F54D8.2.4; WBGene00006519.
DR   GeneID; 175693; -.
DR   KEGG; cel:CELE_F54D8.2; -.
DR   UCSC; F54D8.2.1; c. elegans.
DR   CTD; 175693; -.
DR   WormBase; F54D8.2; CE01308; WBGene00006519; cox-6A.
DR   eggNOG; KOG3469; Eukaryota.
DR   GeneTree; ENSGT00940000168355; -.
DR   HOGENOM; CLU_122515_0_2_1; -.
DR   InParanoid; Q20779; -.
DR   OMA; HKKHMSH; -.
DR   OrthoDB; 1591077at2759; -.
DR   PhylomeDB; Q20779; -.
DR   UniPathway; UPA00705; -.
DR   PRO; PR:Q20779; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00006519; Expressed in larva and 4 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:0005739; C:mitochondrion; HDA:WormBase.
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   SUPFAM; SSF81411; SSF81411; 1.
DR   PROSITE; PS01329; COX6A; 1.
PE   3: Inferred from homology;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW   Reference proteome; Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..19
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..128
FT                   /note="Cytochrome c oxidase subunit 6A, mitochondrial"
FT                   /id="PRO_0000006125"
FT   TOPO_DOM        20..53
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        54..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        72..128
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   128 AA;  14743 MW;  EF4EA56A1CE6A233 CRC64;
     MNRLAQPATR SVVKTFQRKS SGSFYGSNNV EGFKESYVTP LKQAHNASET WKKIFFIASI
     PCLALTMYAA FKDHKKHMSH ERPEHVEYAF LNVRNKPFPW SDGNHSLFHN KAEQFVPGVG
     FEADREKH
 
 
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