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P41774 (COX1_MYTED) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 75. 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
OrganismMytilus edulis (Blue mussel)
Taxonomic identifier6550 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaMolluscaBivalviaPteriomorphiaMytiloidaMytiloideaMytilidaeMytilinaeMytilus

Protein attributes

Sequence length551 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 – 551551Cytochrome c oxidase subunit 1
PRO_0000183364

Regions

Transmembrane34 – 5421Helical; Potential
Transmembrane81 – 10121Helical; Potential
Transmembrane126 – 14621Helical; Potential
Transmembrane163 – 18321Helical; Potential
Transmembrane209 – 22921Helical; Potential
Transmembrane252 – 27221Helical; Potential
Transmembrane285 – 30521Helical; Potential
Transmembrane326 – 34621Helical; Potential
Transmembrane356 – 37621Helical; Potential
Transmembrane391 – 41121Helical; Potential
Transmembrane432 – 45221Helical; Potential
Transmembrane475 – 49521Helical; Potential

Sites

Metal binding791Iron (heme A axial ligand) Probable
Metal binding2581Copper B Probable
Metal binding2621Copper B Probable
Metal binding3081Copper B Probable
Metal binding3091Copper B Probable
Metal binding3941Iron (heme A3 axial ligand) Probable
Metal binding3961Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link258 ↔ 2621'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

Sequence LengthMass (Da)Tools
P41774 [UniParc].

Last modified March 1, 2005. Version 2.
Checksum: E1D49E4CD4FC13C0

FASTA55161,644
        10         20         30         40         50         60 
MMKMLKKEEM GGYGEVESWW RRWLWSTNHK DIGTLYLYSG VWGGLFGASL SLMIRMQLGH 

        70         80         90        100        110        120 
PGAVFLKSDW FYNVVVTTHA LMMIFFAVMP ILIEAFGNWL IPLLVGGKDM IYPRMNNLSY 

       130        140        150        160        170        180 
WLSPNALYLL MLSFSTDKGV GAGWTIYPPL SVYPYHSGPS MDVLIVSLHL AGLSSLVGAI 

       190        200        210        220        230        240 
NFASTNKNMP VLEMKGERAE LYVLSISVTA VLLIISIPVL GGGITMILFD RNFNTTFFDP 

       250        260        270        280        290        300 
AGGGDPVLFQ HLFWFFGHPE VYILILPAFG VMSKVIMHCS GKEAVFGLIG MVYAMIGIGG 

       310        320        330        340        350        360 
LGCMVWAHHM FTVGLNVDTR GYFSTATMVI AVPTGVKVFS WLATMAGSKF KMKPAAYWST 

       370        380        390        400        410        420 
GFLFLFTVGG LTGVLLSSAS MDVSLHDTYY VVAHFHYVLS MGAVFGVFCG LNHWLPNFVG 

       430        440        450        460        470        480 
VCFNKKWSKA HFMAMFFGVN TTFFPQHFLG LSGMPRRYMD YADIYAHWHW VSSYGSAVSF 

       490        500        510        520        530        540 
GSLMYFKFLL WEALVSQRGV VFSGGLCGEM DWAGTRDLYP GSKHVYSQLP FVWTNPYNTC 

       550 
ITYIYKKSRN Q 

« Hide

References

[1]"Complete sequences of the highly rearranged molluscan mitochondrial genomes of the scaphopod Graptacme eborea and the bivalve Mytilus edulis."
Boore J.L., Medina M., Rosenberg L.A.
Mol. Biol. Evol. 21:1492-1503(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"A novel mitochondrial genome organization for the blue mussel, Mytilus edulis."
Hoffmann R.J., Boore J.L., Brown W.M.
Genetics 131:397-412(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY484747 Genomic DNA. Translation: AAT98405.1.
PIRS28757.
RefSeqYP_073343.1. NC_006161.1.

3D structure databases

ProteinModelPortalP41774.
SMRP41774. Positions 22-512.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2960249.

Organism-specific databases

CTD4512.

Phylogenomic databases

ProtClustDBMTH00223.

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_MYTED
AccessionPrimary (citable) accession number: P41774
Secondary accession number(s): Q68SR1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: March 1, 2005
Last modified: April 16, 2014
This is version 75 of the entry and version 2 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