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P00396 (COX1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 123. 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-CO1
Synonyms:COI, COXI, MTCO1
Encoded onMitochondrion
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length514 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Post-translational modification

His-240 and Tyr-244 are involved in the formation of a copper-coordinated covalent cross-link at the active site of the catalytic subunit I.

Sequence similarities

Belongs to the heme-copper respiratory oxidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 514514Cytochrome c oxidase subunit 1
PRO_0000183294

Regions

Topological domain1 – 1111Mitochondrial matrix Ref.2
Transmembrane12 – 4029Helical; Name=I
Topological domain41 – 5010Mitochondrial intermembrane Ref.5
Transmembrane51 – 8636Helical; Name=II
Topological domain87 – 948Mitochondrial matrix Ref.2
Transmembrane95 – 11723Helical; Name=III
Topological domain118 – 14023Mitochondrial intermembrane Ref.2
Transmembrane141 – 17030Helical; Name=IV
Topological domain171 – 18212Mitochondrial matrix Ref.2
Transmembrane183 – 21230Helical; Name=V
Topological domain213 – 22715Mitochondrial intermembrane Ref.2
Transmembrane228 – 26134Helical; Name=VI
Topological domain262 – 2698Mitochondrial matrix Ref.2
Transmembrane270 – 28617Helical; Name=VII
Topological domain287 – 29812Mitochondrial intermembrane Ref.2
Transmembrane299 – 32729Helical; Name=VIII
Topological domain328 – 3358Mitochondrial matrix
Transmembrane336 – 35722Helical; Name=IX
Topological domain358 – 37013Mitochondrial intermembrane
Transmembrane371 – 40030Helical; Name=X
Topological domain401 – 4066Mitochondrial matrix Ref.2
Transmembrane407 – 43327Helical; Name=XI
Topological domain434 – 44613Mitochondrial intermembrane
Transmembrane447 – 47832Helical; Name=XII
Topological domain479 – 51436Mitochondrial matrix Ref.2

Sites

Metal binding611Iron (heme A axial ligand) Ref.2
Metal binding2401Copper B Ref.2
Metal binding2901Copper B Ref.2
Metal binding2911Copper B Ref.2
Metal binding3681Magnesium; shared with chain II Ref.2
Metal binding3761Iron (heme A3 axial ligand) Ref.2
Metal binding3781Iron (heme A axial ligand) Ref.2
Binding site2441Oxygen Probable

Amino acid modifications

Modified residue11N-formylmethionine Ref.2
Cross-link240 ↔ 2441'-histidyl-3'-tyrosine (His-Tyr) Ref.4

Secondary structure

................................................................... 514
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00396 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 0D7C807D7FA3996C

FASTA51457,032
        10         20         30         40         50         60 
MFINRWLFST NHKDIGTLYL LFGAWAGMVG TALSLLIRAE LGQPGTLLGD DQIYNVVVTA 

        70         80         90        100        110        120 
HAFVMIFFMV MPIMIGGFGN WLVPLMIGAP DMAFPRMNNM SFWLLPPSFL LLLASSMVEA 

       130        140        150        160        170        180 
GAGTGWTVYP PLAGNLAHAG ASVDLTIFSL HLAGVSSILG AINFITTIIN MKPPAMSQYQ 

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

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

       310        320        330        340        350        360 
TRAYFTSATM IIAIPTGVKV FSWLATLHGG NIKWSPAMMW ALGFIFLFTV GGLTGIVLAN 

       370        380        390        400        410        420 
SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM GGFVHWFPLF SGYTLNDTWA KIHFAIMFVG 

       430        440        450        460        470        480 
VNMTFFPQHF LGLSGMPRRY SDYPDAYTMW NTISSMGSFI SLTAVMLMVF IIWEAFASKR 

       490        500        510 
EVLTVDLTTT NLEWLNGCPP PYHTFEEPTY VNLK 

« Hide

References

[1]"Complete sequence of bovine mitochondrial DNA. Conserved features of the mammalian mitochondrial genome."
Anderson S., de Bruijn M.H.L., Coulson A.R., Eperon I.C., Sanger F., Young I.G.
J. Mol. Biol. 156:683-717(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Heart.
[2]"Studies on cytochrome-c oxidase, XIV. The amino-acid sequence of subunit I -- proteinchemical methods for the analysis of a large hydrophobic membrane protein."
Hensel S., Buse G.
Biol. Chem. Hoppe-Seyler 371:411-422(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Heart.
[3]"Bos taurus mitochondrial protein coding regions."
Wettstein P.J.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 65, 66, D and F.
[4]"Evidence for a copper-coordinated histidine-tyrosine cross-link in the active site of cytochrome oxidase."
Buse G., Soulimane T., Dewor M., Meyer H.E., Blueggel M.
Protein Sci. 8:985-990(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: COVALENT BOND.
[5]"The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A."
Tsukihara T., Aoyama H., Yamashita E., Tomizaki T., Yamaguchi H., Shinzawa-Itoh K., Nakashima R., Yaono R., Yoshikawa S.
Science 272:1136-1144(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[6]"Structure analysis of bovine heart cytochrome c oxidase at 2.8 A resolution."
Tomizaki T., Yamashita E., Yamaguchi H., Aoyama H., Tsukihara T., Shinzawa-Itoh K., Nakashima R., Yaono R., Yoshikawa S.
Acta Crystallogr. D 55:31-45(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
Tissue: Heart.
[7]"X-ray structure of azide-bound fully oxidized cytochrome c oxidase from bovine heart at 2.9 A resolution."
Fei M.J., Yamashita E., Inoue N., Yao M., Yamaguchi H., Tsukihara T., Shinzawa-Itoh K., Nakashima R., Yoshikawa S.
Acta Crystallogr. D 56:529-535(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
Tissue: Heart.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V00654 Genomic DNA. Translation: CAA23999.1.
AF490528 Genomic DNA. Translation: AAM08330.1.
AF490529 Genomic DNA. Translation: AAM08343.1.
AF493541 Genomic DNA. Translation: AAM12791.1.
AF493542 Genomic DNA. Translation: AAM12804.1.
PIRODBO1. A00464.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OCCX-ray2.80A/N1-514[»]
1OCOX-ray2.80A/N1-514[»]
1OCRX-ray2.35A/N1-514[»]
1OCZX-ray2.90A/N1-514[»]
1V54X-ray1.80A/N1-514[»]
1V55X-ray1.90A/N1-514[»]
2DYRX-ray1.80A/N1-514[»]
2DYSX-ray2.20A/N1-514[»]
2EIJX-ray1.90A/N1-514[»]
2EIKX-ray2.10A/N1-514[»]
2EILX-ray2.10A/N1-514[»]
2EIMX-ray2.60A/N1-514[»]
2EINX-ray2.70A/N1-514[»]
2OCCX-ray2.30A/N1-514[»]
2Y69X-ray1.95A/N1-514[»]
2YBBelectron microscopy19.00L1-514[»]
2ZXWX-ray2.50A/N1-514[»]
3ABKX-ray2.00A/N1-514[»]
3ABLX-ray2.10A/N1-514[»]
3ABMX-ray1.95A/N1-514[»]
3AG1X-ray2.20A/N1-514[»]
3AG2X-ray1.80A/N1-514[»]
3AG3X-ray1.80A/N1-514[»]
3AG4X-ray2.05A/N1-514[»]
3ASNX-ray3.00A/N1-514[»]
3ASOX-ray2.30A/N1-514[»]
ProteinModelPortalP00396.
SMRP00396. Positions 1-514.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

TCDB3.D.4.7.1. the proton-translocating cytochrome oxidase (cox) superfamily.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0843.
HOGENOMHOG000085274.
HOVERGENHBG003841.
InParanoidP00396.

Enzyme and pathway databases

SABIO-RKP00396.
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

EvolutionaryTraceP00396.

Entry information

Entry nameCOX1_BOVIN
AccessionPrimary (citable) accession number: P00396
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: March 19, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways