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COX1_AEDAE
ID   COX1_AEDAE              Reviewed;         514 AA.
AC   B0FWC7; Q94PR3;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Cytochrome c oxidase subunit 1;
DE            EC=7.1.1.9;
DE   AltName: Full=Cytochrome c oxidase polypeptide I;
GN   Name=mt:CoI {ECO:0000250|UniProtKB:P00399};
GN   Synonyms=COI {ECO:0000312|EMBL:AAK56378.2},
GN   COX1 {ECO:0000312|EMBL:ABY51624.1};
OS   Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OG   Mitochondrion {ECO:0000312|EMBL:ABY51624.1}.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Aedini; Aedes; Stegomyia.
OX   NCBI_TaxID=7159;
RN   [1] {ECO:0000312|EMBL:ABY51624.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LVPib12 {ECO:0000312|EMBL:ABY51624.1};
RA   Lobo N.F., Lovin D., DeBruyn B., Puiu D., Shumway M., Haas B., Nene V.,
RA   Severson D.W.;
RT   "The mitochondrial genome of the Yellow fever mosquito - Aedes aegypti.";
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305, ECO:0000312|EMBL:AAK56378.2}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 2-513.
RC   STRAIN=Formosus {ECO:0000312|EMBL:AAL25640.1},
RC   Liverpool {ECO:0000312|EMBL:AAL25639.1}, Moyo-R, and Red eye;
RC   TISSUE=Midgut {ECO:0000312|EMBL:AAK56378.2};
RX   PubMed=12180346; DOI=10.1080/10425170290030051;
RA   Morlais I., Severson D.W.;
RT   "Complete mitochondrial DNA sequence and amino acid analysis of the
RT   cytochrome C oxidase subunit I (COI) from Aedes aegypti.";
RL   DNA Seq. 13:123-127(2002).
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:P00401}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-
CC         [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436,
CC         Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:29034; EC=7.1.1.9;
CC         Evidence={ECO:0000250|UniProtKB:P00401};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437;
CC         Evidence={ECO:0000250|UniProtKB:P00401};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P00401};
CC       Note=Binds 2 heme A groups non-covalently per subunit.
CC       {ECO:0000250|UniProtKB:P00401};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000250|UniProtKB:P00401};
CC       Note=Binds a copper B center. {ECO:0000250|UniProtKB:P00401};
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000250|UniProtKB:P00401}.
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:P00401}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P00401}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P00401}.
CC   -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC       {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABY51624.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; EU352212; ABY51624.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AF380835; AAK56378.2; -; Genomic_DNA.
DR   EMBL; AF390098; AAK73349.2; -; mRNA.
DR   EMBL; AY056596; AAL25639.1; -; Genomic_DNA.
DR   EMBL; AY056597; AAL25640.1; -; Genomic_DNA.
DR   RefSeq; YP_001649163.1; NC_010241.1.
DR   AlphaFoldDB; B0FWC7; -.
DR   SMR; B0FWC7; -.
DR   STRING; 7159.AAEL018662-PA; -.
DR   VEuPathDB; VectorBase:AAEL018662; -.
DR   eggNOG; KOG4769; Eukaryota.
DR   HOGENOM; CLU_011899_7_3_1; -.
DR   InParanoid; B0FWC7; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000008820; Unassembled WGS sequence.
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:0045277; C:respiratory chain complex IV; IEA:InterPro.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR   CDD; cd01663; Cyt_c_Oxidase_I; 1.
DR   Gene3D; 1.20.210.10; -; 1.
DR   InterPro; IPR023616; Cyt_c_oxase-like_su1_dom.
DR   InterPro; IPR036927; Cyt_c_oxase-like_su1_sf.
DR   InterPro; IPR000883; Cyt_C_Oxase_1.
DR   InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR   InterPro; IPR033944; Cyt_c_oxase_su1_dom.
DR   PANTHER; PTHR10422; PTHR10422; 1.
DR   Pfam; PF00115; COX1; 1.
DR   PRINTS; PR01165; CYCOXIDASEI.
DR   SUPFAM; SSF81442; SSF81442; 1.
DR   PROSITE; PS50855; COX1; 1.
DR   PROSITE; PS00077; COX1_CUB; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Copper; Electron transport; Heme; Iron; Magnesium; Membrane;
KW   Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome; Respiratory chain; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..514
FT                   /note="Cytochrome c oxidase subunit 1"
FT                   /id="PRO_0000347262"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        101..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        233..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        267..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        304..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        337..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        379..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        415..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        451..471
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         39
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         44
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         60
FT                   /ligand="Fe(II)-heme a"
FT                   /ligand_id="ChEBI:CHEBI:61715"
FT                   /ligand_note="low-spin"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         239
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         243
FT                   /ligand="O2"
FT                   /ligand_id="ChEBI:CHEBI:15379"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   BINDING         289
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         290
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         367
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="ligand shared with subunit 2"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         368
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="ligand shared with subunit 2"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         375
FT                   /ligand="heme a3"
FT                   /ligand_id="ChEBI:CHEBI:83282"
FT                   /ligand_note="high-spin"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         377
FT                   /ligand="Fe(II)-heme a"
FT                   /ligand_id="ChEBI:CHEBI:61715"
FT                   /ligand_note="low-spin"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   CROSSLNK        239..243
FT                   /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT                   /evidence="ECO:0000250|UniProtKB:P98002"
FT   CONFLICT        171
FT                   /note="R -> W (in Ref. 1; ABY51624)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   514 AA;  56966 MW;  019CDFE533655F10 CRC64;
     MSRQWLFSTN HKDIGTLYFI FGVWSGMVGT SLSILIRAEL SHPGMFIGND QIYNVIVTAH
     AFIMIFFMVM PIMIGGFGNW LVPLMLGAPD MAFPRMNNMS FWMLPPSLTL LLSSSMVENG
     AGTGWTVYPP LSSGTAHAGA SVDLAIFSLH LAGISSILGA VNFITTVINM RSSGITLDRL
     PLFVWSVVIT AILLLLSLPV LAGAITMLLT DRNLNTSFFD PIGGGDPILY QHLFWFFGHP
     EVYILILPGF GMISHIITQE SGKKETFGTL GMIYAMLTIG LLGFIVWAHH MFTVGMDVDT
     RAYFTSATMI IAVPTGIKIF SWLATLHGTQ LTYSPALLWS LGFVFLFTVG GLTGVVLANS
     SIDIVLHDTY YVVAHFHYVL SMGAVFAIMA GFIHWYPLLT GMVMNPSWLK AQFSMMFIGV
     NLTFFPQHFL GLAGMPRRYS DFPDSYLTWN IISSLGSTIS LFAVIFFLFI IWESMITQRT
     PSFPMQLSSS IEWYHTLPPA EHTYSELPLL SSNF
 
 
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