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Reviewed, UniProtKB/Swiss-Prot O99041 (COX1_COLPO)

Last modified June 16, 2009. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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-CO1
Synonyms: COI, COXI, MTCO1
Encoded onMitochondrion
OrganismColobus polykomos (Western black-and-white colobus monkey)
Taxonomic identifier9572 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Colobinae › Colobus

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Protein attributes

Sequence length514 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 514514Cytochrome c oxidase subunit 1
PRO_0000183315

Regions

Transmembrane17 – 3721 Potential
Transmembrane56 – 7621 Potential
Transmembrane77 – 9721 Potential
Transmembrane102 – 12221 Potential
Transmembrane145 – 16521 Potential
Transmembrane183 – 20321 Potential
Transmembrane234 – 25421 Potential
Transmembrane268 – 28821 Potential
Transmembrane305 – 32521 Potential
Transmembrane338 – 35821 Potential
Transmembrane380 – 40021 Potential
Transmembrane414 – 43421 Potential
Transmembrane457 – 47721 Potential

Sites

Metal binding611Iron (heme A axial ligand) Probable
Metal binding2401Copper B Probable
Metal binding2441Copper B Probable
Metal binding2901Copper B Probable
Metal binding2911Copper B Probable
Metal binding3761Iron (heme A3 axial ligand) Probable
Metal binding3781Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link240 ↔ 2441'-histidyl-3'-tyrosine (His-Tyr) By similarity

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Sequences

Sequence LengthMass (Da)Tools
O99041-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: F495DE844C657885

FASTA51457,168
        10         20         30         40         50         60 
MLVNRWLFST NHKDIGTLYL LFGAWAGMMG MAMSLLIRAE LGQPGNLLGN DHIYNVIVTA 

        70         80         90        100        110        120 
HAFVMIFFMV MPIMIGGFGN WLVPLMIGAP DMAFPRLNNM SFWLLPPSFL LLLASAAVEA 

       130        140        150        160        170        180 
GAGTGWTVYP PLAGNFSHPG ASVDLTIFSL HLAGISSILG AINFITTIIN MKPPAISQYQ 

       190        200        210        220        230        240 
TPLFVWSVMI TAVLLLLSLP VLAAGITMLL TDRNLNTTFF DPAGGGDPIL YQHLFWFFGH 

       250        260        270        280        290        300 
PEVYILILPG FGMISHLVTY YSGKKEPFGY MGMVWAMMSI GFLGFIVWAH HMFTVGMDVD 

       310        320        330        340        350        360 
TRAYFTSATM IIAIPTGVKV FSWLATLHGR NIKWSPAMLW ALGFIFLFTV GGLTGIVLAN 

       370        380        390        400        410        420 
SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM GGFIHWFPLF SGYTLNQVCA KAHFMIMFVG 

       430        440        450        460        470        480 
VNLTFFPQHF LGLSGMPRRY SDYPDAYTMW NIVSSTGSFI SLVAMLLMVY MIWEAFASKR 

       490        500        510 
KILLIEQPTS NLEWLHGSPP PYHTFDEPVF IKIK

« Hide

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References

[1]"Evolutionary rate acceleration of cytochrome c oxidase subunit I in simian primates."
Andrews T.D., Easteal S.
J. Mol. Evol. 50:562-568(2000) [PubMed: 10835486] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

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Cross-references

Sequence databases

AB016731 Genomic DNA. Translation: BAA74720.1.

3D structure databases

HSSPHSSP built from PDB template 2OCC based on UniProtKB P00396.
SMRO99041. Positions 1-514.
ModBaseSearch...

Phylogenomic databases

HOVERGENO99041.

Family and domain databases

InterProIPR000883. Cyt_c_oxidase_su1.
[Graphical view]
Gene3DG3DSA:1.20.210.10. COX1. 1 hit.
PANTHERPTHR10422. COX1. 1 hit.
PfamPF00115. COX1. 1 hit.
[Graphical view]
PRINTSPR01165. CYCOXIDASEI.
PROSITEPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameCOX1_COLPO
AccessionPrimary (citable) accession number: O99041
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: May 1, 1999
Last modified: June 16, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents