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COX7A_DROME
ID   COX7A_DROME             Reviewed;          89 AA.
AC   Q9VHS2; B9EQX3;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Cytochrome c oxidase subunit 7A, mitochondrial;
DE   AltName: Full=Cytochrome c oxidase subunit VIIa;
DE   Flags: Precursor;
GN   Name=COX7A {ECO:0000312|FlyBase:FBgn0040529};
GN   ORFNames=CG9603 {ECO:0000312|FlyBase:FBgn0040529};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Ovary;
RA   Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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 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:P10174}.
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; AE014297; AAF54227.1; -; Genomic_DNA.
DR   EMBL; BT058048; ACM78490.1; -; mRNA.
DR   RefSeq; NP_652184.2; NM_143927.4.
DR   AlphaFoldDB; Q9VHS2; -.
DR   SMR; Q9VHS2; -.
DR   BioGRID; 72497; 2.
DR   DIP; DIP-17309N; -.
DR   IntAct; Q9VHS2; 3.
DR   STRING; 7227.FBpp0296960; -.
DR   PaxDb; Q9VHS2; -.
DR   PRIDE; Q9VHS2; -.
DR   DNASU; 50002; -.
DR   EnsemblMetazoa; FBtr0081855; FBpp0081344; FBgn0040529.
DR   GeneID; 50002; -.
DR   KEGG; dme:Dmel_CG9603; -.
DR   UCSC; CG9603-RA; d. melanogaster.
DR   CTD; 50002; -.
DR   FlyBase; FBgn0040529; COX7A.
DR   VEuPathDB; VectorBase:FBgn0040529; -.
DR   eggNOG; ENOG502SBK9; Eukaryota.
DR   HOGENOM; CLU_188593_0_0_1; -.
DR   InParanoid; Q9VHS2; -.
DR   OMA; YKQLKHI; -.
DR   OrthoDB; 1548349at2759; -.
DR   PhylomeDB; Q9VHS2; -.
DR   Reactome; R-DME-5628897; TP53 Regulates Metabolic Genes.
DR   Reactome; R-DME-611105; Respiratory electron transport.
DR   Reactome; R-DME-9707564; Cytoprotection by HMOX1.
DR   UniPathway; UPA00705; -.
DR   BioGRID-ORCS; 50002; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; COX7A; fly.
DR   GenomeRNAi; 50002; -.
DR   PRO; PR:Q9VHS2; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0040529; Expressed in adult Malpighian tubule (Drosophila) and 26 other tissues.
DR   ExpressionAtlas; Q9VHS2; baseline and differential.
DR   Genevisible; Q9VHS2; DM.
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:0005739; C:mitochondrion; HDA:FlyBase.
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; IPR036539; Cyt_c_oxidase_su7a_sf.
DR   InterPro; IPR003177; Cytc_oxidase_su7a_met.
DR   PANTHER; PTHR10510; PTHR10510; 1.
DR   SUPFAM; SSF81419; SSF81419; 1.
PE   3: Inferred from homology;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW   Reference proteome; Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..31
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..89
FT                   /note="Cytochrome c oxidase subunit 7A, mitochondrial"
FT                   /id="PRO_0000006153"
FT   TOPO_DOM        32..58
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P10174"
FT   TRANSMEM        59..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        82..89
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P10174"
SQ   SEQUENCE   89 AA;  9902 MW;  9220331ED2D07F20 CRC64;
     MMNLSRAVVR SFATTAGRRS AAVPKDQIEK GYFEIRKVQE HFQKKDGKPV FLKGSVVDNV
     LYRVTVALAL VGIGGMGKLF YELSVPKKE
 
 
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