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P24893 (COX1_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. 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:cox-1
Synonyms:coI
ORF Names:MTCE.26
Encoded onMitochondrion
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length525 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 – 525525Cytochrome c oxidase subunit 1
PRO_0000183298

Regions

Transmembrane25 – 4521Helical; Potential
Transmembrane71 – 9121Helical; Potential
Transmembrane108 – 12821Helical; Potential
Transmembrane152 – 17221Helical; Potential
Transmembrane190 – 21021Helical; Potential
Transmembrane241 – 26121Helical; Potential
Transmembrane274 – 29421Helical; Potential
Transmembrane317 – 33721Helical; Potential
Transmembrane344 – 36421Helical; Potential
Transmembrane387 – 40721Helical; Potential
Transmembrane420 – 44021Helical; Potential
Transmembrane459 – 47921Helical; Potential

Sites

Metal binding691Iron (heme A axial ligand) Probable
Metal binding2471Copper B Probable
Metal binding2511Copper B Probable
Metal binding2971Copper B Probable
Metal binding2981Copper B Probable
Metal binding3831Iron (heme A3 axial ligand) Probable
Metal binding3851Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link247 ↔ 2511'-histidyl-3'-tyrosine (His-Tyr) By similarity

Natural variations

Natural variant121A → S in strain: CB4856 and CB4857. Ref.1
Natural variant4661I → M in strain: AB1, AB2, CB4852, CB4853, CB4855, CB4857, CB4858, KR314 and PB306. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P24893 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: E3D051208B09396F

FASTA52558,464
        10         20         30         40         50         60 
MNLYKKYQGG LAVWLESSNH KDIGTLYFIF GLWSGMVGTS FSLLIRLELA KPGFFLSNGQ 

        70         80         90        100        110        120 
LYNSVITAHA ILMIFFMVMP TMIGGFGNWL LPLMLGAPDM SFPRLNNLSF WLLPTSMLLI 

       130        140        150        160        170        180 
LDACFVDMGC GTSWTVYPPL STMGHPGSSV DLAIFSLHAA GLSSILGGIN FMCTTKNLRS 

       190        200        210        220        230        240 
SSISLEHMTL FVWTVFVTVF LLVLSLPVLA GAITMLLTDR NLNTSFFDPS TGGNPLIYQH 

       250        260        270        280        290        300 
LFWFFGHPEV YILILPAFGI VSQSTLYLTG KKEVFGALGM VYAILSIGLI GCVVWAHHMY 

       310        320        330        340        350        360 
TVGMDLDSRA YFSAATMVIA VPTGVKVFSW LATLFGMKMV FNPLLLWVLG FIFLFTLGGL 

       370        380        390        400        410        420 
TGVVLSNSSL DIILHDTYYV VSHFHYVLSL GAVFGIFTGV TLWWSFITGY VLDKLMMSAV 

       430        440        450        460        470        480 
FILLFIGVNL TFFPLHFAGL HGFPRKYLDY PDVYSVWNII ASYGSIISTA GLFLFIYVLL 

       490        500        510        520 
ESFFSYRLVI SDYYSNSSPE YCMSNYVFGH SYQSEIYFST TSLKN 

« Hide

References

« Hide 'large scale' references
[1]"Phylogenetics in Caenorhabditis elegans: an analysis of divergence and outcrossing."
Denver D.R., Morris K., Thomas W.K.
Mol. Biol. Evol. 20:393-400(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-12 AND MET-466.
Strain: AB1, AB2, Bristol N2, CB4852, CB4853, CB4854, CB4855, CB4856, CB4857, CB4858, KR314, PB303, PB306, RW7000 and TR403.
[2]"The mitochondrial genomes of two nematodes, Caenorhabditis elegans and Ascaris suum."
Okimoto R., Macfarlane J.L., Clary D.O., Wolstenholme D.R.
Genetics 130:471-498(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
[3]"Evidence for the frequent use of TTG as the translation initiation codon of mitochondrial protein genes in the nematodes, Ascaris suum and Caenorhabditis elegans."
Okimoto R., Macfarlane J.L., Wolstenholme D.R.
Nucleic Acids Res. 18:6113-6118(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY171193 Genomic DNA. Translation: AAO16252.1.
AY171194 Genomic DNA. Translation: AAO16256.1.
AY171195 Genomic DNA. Translation: AAO16260.1.
AY171196 Genomic DNA. Translation: AAO16264.1.
AY171197 Genomic DNA. Translation: AAO16268.1.
AY171198 Genomic DNA. Translation: AAO16272.1.
AY171199 Genomic DNA. Translation: AAO16276.1.
AY171200 Genomic DNA. Translation: AAO16280.1.
AY171201 Genomic DNA. Translation: AAO16284.1.
AY171202 Genomic DNA. Translation: AAO16288.1.
AY171203 Genomic DNA. Translation: AAO16292.1.
AY171204 Genomic DNA. Translation: AAO16296.1.
AY171205 Genomic DNA. Translation: AAO16300.1.
AY171206 Genomic DNA. Translation: AAO16304.1.
AY171207 Genomic DNA. Translation: AAO16308.1.
X54252 Genomic DNA. Translation: CAA38159.1.
PIRS26034.
RefSeqNP_006961.1. NC_001328.1.

3D structure databases

ProteinModelPortalP24893.
SMRP24893. Positions 14-501.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP24893. 1 interaction.
STRING6239.MTCE.26.

Proteomic databases

PaxDbP24893.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2565700.
KEGGcel:COX1.

Organism-specific databases

CTD4512.

Phylogenomic databases

eggNOGCOG0843.
HOGENOMHOG000085274.
KOK02256.
PhylomeDBP24893.
ProtClustDBMTH00079.

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...

Other

NextBio953875.

Entry information

Entry nameCOX1_CAEEL
AccessionPrimary (citable) accession number: P24893
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase