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Q5Y4Q8 (COX1_BOSMU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 48. 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:MT-CO1
Synonyms:COI, COXI, MTCO1
Encoded onMitochondrion
OrganismBos mutus grunniens (Wild yak) (Bos grunniens)
Taxonomic identifier30521 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length514 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 – 514514Cytochrome c oxidase subunit 1
PRO_0000253786

Regions

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

Sites

Metal binding611Iron (heme A axial ligand) 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

Sequences

Sequence LengthMass (Da)Tools
Q5Y4Q8 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 9D7FD418DE78EDC0

FASTA51456,918
        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 LGLSGMPRRS PDYPDAYTMW NTVSSMGSFI SLTAVMLMVF IIWEALASKR 

       490        500        510 
EVLTVDLTTT NLEWLNGCPP PYHTFEEPTY VNLK 

« Hide

References

[1]"Complete sequence of the Yak (Bos grunniens.) mitochondrial genome and its genetic relationship with related species."
Gu Z., Zhao X., Li N., Wu C.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY684273 Genomic DNA. Translation: AAU89108.1.

3D structure databases

ProteinModelPortalQ5Y4Q8.
SMRQ5Y4Q8. Positions 1-514.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG003841.

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_BOSMU
AccessionPrimary (citable) accession number: Q5Y4Q8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: November 23, 2004
Last modified: May 14, 2014
This is version 48 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

PATHWAY comments

Index of metabolic and biosynthesis pathways