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P20374 (COX1_APILI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:COI
Encoded onMitochondrion
OrganismApis mellifera ligustica (Common honeybee) (Italian honeybee)
Taxonomic identifier7469 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaHymenopteraApocritaAculeataApoideaApidaeApis

Protein attributes

Sequence length521 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 521521Cytochrome c oxidase subunit 1
PRO_0000183284

Regions

Transmembrane15 – 3521Helical; Potential
Transmembrane61 – 8121Helical; Potential
Transmembrane98 – 11821Helical; Potential
Transmembrane143 – 16321Helical; Potential
Transmembrane184 – 20421Helical; Potential
Transmembrane232 – 25221Helical; Potential
Transmembrane265 – 28521Helical; Potential
Transmembrane303 – 32321Helical; Potential
Transmembrane336 – 35621Helical; Potential
Transmembrane383 – 40321Helical; Potential
Transmembrane412 – 43221Helical; Potential
Transmembrane451 – 47121Helical; 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 variant1081F → L in strain: Isolate ligus8.
Natural variant2701S → G in strain: Isolate ligus8.
Natural variant2711M → I in strain: Isolate ligus2.
Natural variant4371R → P in strain: Isolate ligus7.

Sequences

Sequence LengthMass (Da)Tools
P20374 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 2149417AC981CE64

FASTA52159,294
        10         20         30         40         50         60 
MMKWFMSTNH KNIGILYIIL ALWSGMLGSS MSLIIRMELS SPGSWISNDQ IYNTIVTSHA 

        70         80         90        100        110        120 
FLMIFFMVMP FLIGGFGNWL IPLMLGSPDM AFPRMNNISF WLLPPSLFML LLSNLFYPSP 

       130        140        150        160        170        180 
GTGWTVYPPL SAYLYHSSPS VDFAIFSLHM SGISSIMGSL NLMVTIMMMK NFSMNYDQIS 

       190        200        210        220        230        240 
LFPWSVFITA ILLIMSLPVL AGAITMLLFD RNFNTSFFDP MGGGDPILYQ HLFWFFGHPE 

       250        260        270        280        290        300 
VYILILPGFG LISHIVMNES GKKEIFGNLS MIYAMLGIGF LGFIVWAHHM FTVGLDVDTR 

       310        320        330        340        350        360 
AYFTSATMII AVPTGIKVFS WLATYHGSKL KLNISILWSL GFIMLFTIGG LTGIMLSNSS 

       370        380        390        400        410        420 
IDIILHDTYY VVGHFHYVLS MGAVFAIISS FIHWYPLITG LLLNIKWLKI QFIMMFIGVN 

       430        440        450        460        470        480 
LTFFPQHFLG LMSMPRRYSD YPDSYYCWNS ISSMGSMISL NSMIFLIFII LESLISKRML 

       490        500        510        520 
LFKFNQSSLE WLNFLPPLDH SHLEIPLLIK NLNLKSILIK F 

« Hide

References

[1]"The CO-I and CO-II region of honeybee mitochondrial DNA: evidence for variation in insect mitochondrial evolutionary rates."
Crozier R.H., Crozier Y.C., Mackinlay A.G.
Mol. Biol. Evol. 6:399-411(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Thorax.
[2]"The mitochondrial genome of the honeybee Apis mellifera: complete sequence and genome organization."
Crozier R.H., Crozier Y.C.
Genetics 133:97-117(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Thorax.
[3]"ND2 and CO1 mitochondrial genes in Apis mellifera L.: a molecular approach to Mediterranean populations monitoring."
Marino A., Mantovani B., Carpana E., Sabatini A.G., Lodesani M.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 93-507.
Strain: Isolate ligus2, Isolate ligus3, Isolate ligus4, Isolate ligus5, Isolate ligus6, Isolate ligus7, Isolate ligus8 and Isolate ligus9.
[4]"Putative origin and function of the intergenic region between COI and COII of Apis mellifera L. mitochondrial DNA."
Cornuet J.-M., Garnery L., Solignac M.
Genetics 128:393-403(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 338-521.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M23409 Genomic DNA. Translation: AAA18476.1.
L06178 Genomic DNA. Translation: AAB96799.1.
AY114452 Genomic DNA. Translation: AAM76437.1.
AY114453 Genomic DNA. Translation: AAM76438.1.
AY114454 Genomic DNA. Translation: AAM76439.1.
AY114455 Genomic DNA. Translation: AAM76440.1.
AY114456 Genomic DNA. Translation: AAM76441.1.
AY114457 Genomic DNA. Translation: AAM76442.1.
AY114458 Genomic DNA. Translation: AAM76443.1.
AY114460 Genomic DNA. Translation: AAM76445.1.
PIRA32431.
RefSeqNP_008083.1. NC_001566.1.

3D structure databases

ProteinModelPortalP20374.
SMRP20374. Positions 3-504.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID807695.

Organism-specific databases

CTD4512.

Phylogenomic databases

InParanoidP20374.

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_APILI
AccessionPrimary (citable) accession number: P20374
Secondary accession number(s): Q8LUG0 expand/collapse secondary AC list , Q8LXP4, Q8LXP6, Q8LXP7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: May 14, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways