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COX9_DEBHA
ID   COX9_DEBHA              Reviewed;          61 AA.
AC   Q6BPV1;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Cytochrome c oxidase subunit 9, mitochondrial;
DE   AltName: Full=Cytochrome c oxidase polypeptide VIIA;
DE   Flags: Precursor;
GN   Name=COX9; OrderedLocusNames=DEHA2E10626g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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:P07255}.
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000250|UniProtKB:P07255}.
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:P07255}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P07255}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:P07255}.
CC   -!- SIMILARITY: Belongs to the fungal cytochrome c oxidase subunit 7a
CC       family. {ECO:0000305}.
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DR   EMBL; CR382137; CAG88008.1; -; Genomic_DNA.
DR   RefSeq; XP_459769.1; XM_459769.1.
DR   AlphaFoldDB; Q6BPV1; -.
DR   SMR; Q6BPV1; -.
DR   STRING; 4959.XP_459769.1; -.
DR   EnsemblFungi; CAG88008; CAG88008; DEHA2E10626g.
DR   GeneID; 2902769; -.
DR   KEGG; dha:DEHA2E10626g; -.
DR   VEuPathDB; FungiDB:DEHA2E10626g; -.
DR   eggNOG; ENOG502SBM8; Eukaryota.
DR   HOGENOM; CLU_196969_0_0_1; -.
DR   InParanoid; Q6BPV1; -.
DR   OMA; ASYWWWG; -.
DR   OrthoDB; 1638792at2759; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000000599; Chromosome E.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR   GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR014368; Cyt_c_oxidase_su7a_fun.
DR   PIRSF; PIRSF000283; COX9; 1.
PE   3: Inferred from homology;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..56
FT                   /note="Cytochrome c oxidase subunit 9, mitochondrial"
FT                   /id="PRO_0000041767"
FT   PROPEP          57..61
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P07255"
FT                   /id="PRO_0000041768"
FT   TOPO_DOM        1..13
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P07255"
FT   TRANSMEM        14..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        37..56
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P07255"
SQ   SEQUENCE   61 AA;  6776 MW;  A3CC72BEE6AF8545 CRC64;
     MAIAPITGTL KRKIITDISI GFACGFALAT GYWYIEHKPL IVKREAYYAK LKAQQEAEDS
     A
 
 
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