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Q34345 (COX1_DROMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytochrome c oxidase subunit 1

EC=1.9.3.1
Alternative name(s):
Cytochrome c oxidase polypeptide I
Gene names
Name:mt:CoI
Synonyms:CoI
Encoded onMitochondrion
OrganismDrosophila mauritiana (Fruit fly)
Taxonomic identifier7226 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length511 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.

Catalytic activity

4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O.

Pathway

Energy metabolism; oxidative phosphorylation.

Subcellular location

Mitochondrion inner membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the heme-copper respiratory oxidase family.

Caution

There is no mitochondrial-type translation initiation codon present in frame in the sequence. In Ref.4, the authors suggest the presence of a novel start codon coding for either Pro or Ser in Drosophila CoI transcripts.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 511511Cytochrome c oxidase subunit 1
PRO_0000183324

Regions

Transmembrane15 – 3521Helical; Potential
Transmembrane54 – 7421Helical; Potential
Transmembrane100 – 12021Helical; Potential
Transmembrane143 – 16321Helical; Potential
Transmembrane181 – 20121Helical; Potential
Transmembrane232 – 25221Helical; Potential
Transmembrane266 – 28621Helical; Potential
Transmembrane303 – 32321Helical; Potential
Transmembrane336 – 35621Helical; Potential
Transmembrane378 – 39821Helical; Potential
Transmembrane412 – 43221Helical; Potential
Transmembrane450 – 47021Helical; Potential

Sites

Metal binding591Iron (heme A axial ligand) Probable
Metal binding2381Copper B Probable
Metal binding2421Copper B Probable
Metal binding2881Copper B Probable
Metal binding2891Copper B Probable
Metal binding3741Iron (heme A3 axial ligand) Probable
Metal binding3761Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link238 ↔ 2421'-histidyl-3'-tyrosine (His-Tyr) By similarity

Natural variations

Natural variant4111H → Q in strain: G52 and BG1. Ref.1 Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q34345 [UniParc].

Last modified November 28, 2012. Version 3.
Checksum: CD7F3FEBB056369E

FASTA51156,384
        10         20         30         40         50         60 
PRQWLFSTNH KDIGTLYFIF GAWAGMVGTS LSILIRAELG HPGALIGDDQ IYNVIVTAHA 

        70         80         90        100        110        120 
FIMIFFMVMP IMIGGFGNWL VPLMLGAPDM AFPRMNNMSF WLLPPALSLL LVSSMVENGA 

       130        140        150        160        170        180 
GTGWTVYPPL SAGIAHGGAS VDLAIFSLHL AGISSILGAV NFITTVINMR STGISLDRMP 

       190        200        210        220        230        240 
LFVWSVVITA LLLLLSLPVL AGAITMLLTD RNLNTSFFDP AGGGDPILYQ HLFWFFGHPE 

       250        260        270        280        290        300 
VYILILPGFG MISHIISQES GKKETFGSLG MIYAMLAIGL LGFIVWAHHM FTVGMDVDTR 

       310        320        330        340        350        360 
AYFTSATMII AVPTGIKIFS WLATLHGTQL SYSPAILWAL GFVFLFTVGG LTGVVLANSS 

       370        380        390        400        410        420 
VDIILHDTYY VVAHFHYVLS MGAVFAIMAG FIHWYPLFTG LTLNNKWLKS HFIIMFIGVN 

       430        440        450        460        470        480 
LTFFPQHFLG LAGMPRRYSD YPDAYTTWNV VSTIGSTISL LGILFFFYII WESLVSQRQV 

       490        500        510 
IYPIQLNSSI EWYQNTPPAE HSYSELPLLT N 

« Hide

References

[1]"Evolution of Drosophila mitochondrial DNA and the history of the melanogaster subgroup."
Satta Y., Takahata N.
Proc. Natl. Acad. Sci. U.S.A. 87:9558-9562(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-411.
Strain: G52 and Mauritius island.
[2]"Comparative genomics of mitochondrial DNA in members of the Drosophila melanogaster subgroup."
Ballard J.W.O.
J. Mol. Evol. 51:48-63(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-411.
Strain: BG1 and G52.
[3]"Analysis of nucleotide substitutions of mitochondrial DNAs in Drosophila melanogaster and its sibling species."
Satta Y., Ishiwa H., Chigusa S.I.
Mol. Biol. Evol. 4:638-650(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-101.
Strain: Mauritius island.
[4]"Comparative genomics of Drosophila mtDNA: Novel features of conservation and change across functional domains and lineages."
Montooth K.L., Abt D.N., Hofmann J.W., Rand D.M.
J. Mol. Evol. 69:94-114(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M18073 Genomic DNA. Translation: AAA69804.2.
M57907 Genomic DNA. Translation: AAB02280.1.
AF200830 Genomic DNA. Translation: AAF77258.1.
AF200831 Genomic DNA. Translation: AAF77277.1.
M57912 Genomic DNA. Translation: AAA99051.1.
RefSeqNP_987108.2. NC_005779.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2760929.

Organism-specific databases

CTD4512.
FlyBaseFBgn0012510. Dmau\mt:CoI.

Enzyme and pathway databases

UniPathwayUPA00705.

Family and domain databases

Gene3D1.20.210.10. 1 hit.
InterProIPR000883. Cyt_c_Oxase_su1.
IPR023615. Cyt_c_Oxase_su1_BS.
IPR023616. Cyt_c_Oxase_su1_dom.
[Graphical view]
PANTHERPTHR10422. PTHR10422. 1 hit.
PfamPF00115. COX1. 1 hit.
[Graphical view]
PRINTSPR01165. CYCOXIDASEI.
SUPFAMSSF81442. SSF81442. 1 hit.
PROSITEPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX1_DROMA
AccessionPrimary (citable) accession number: Q34345
Secondary accession number(s): Q34346 expand/collapse secondary AC list , Q34350, Q7IV58, Q7IV62
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 28, 2012
Last modified: May 14, 2014
This is version 85 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase