Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q33375 (COX1_CANSI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 81. 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
OrganismCanis simensis (Ethiopian wolf) (Simenia simensis)
Taxonomic identifier32534 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis

Protein attributes

Sequence length196 AA.
Sequence statusFragment.
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

Chain‹1 – ›196›196Cytochrome c oxidase subunit 1
PRO_0000183301

Regions

Transmembrane9 – 2921Helical; Potential
Transmembrane34 – 5421Helical; Potential
Transmembrane76 – 9621Helical; Potential
Transmembrane104 – 12421Helical; Potential
Transmembrane146 – 16621Helical; Potential
Transmembrane176 – 19621Helical; Potential

Sites

Metal binding61Copper B Probable
Metal binding101Copper B Probable
Metal binding561Copper B Probable
Metal binding571Copper B Probable
Metal binding1421Iron (heme A3 axial ligand) Probable
Metal binding1441Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link6 ↔ 101'-histidyl-3'-tyrosine (His-Tyr) By similarity

Experimental info

Non-terminal residue11
Non-terminal residue1961

Sequences

Sequence LengthMass (Da)Tools
Q33375 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 8C5CE47EC8CE515C

FASTA19622,107
        10         20         30         40         50         60 
XWFFGHPEVY ILILPGFGMI SHIVTYYSGK KEPFGYMGMV WAMMSIGFLG FIVWAHHMFT 

        70         80         90        100        110        120 
VGMDVDTRAY FTSATMIIAI PTGVKVFSWL ATLHGGNIKW SPAMLWALGF IFLFTVGGLT 

       130        140        150        160        170        180 
GIVLANSSLD IVLHDTYYVV AHFHYVLSMG AVFAIMGGFA HWFPLFSGYT LNDTWAKIHF 

       190 
TIMFVGVNMT FFPQHF 

« Hide

References

[1]"Molecular genetics of the most endangered canid: the Ethiopian wolf Canis simensis."
Gottelli D., Sillero-Zubiri C., Applebaum G.D., Roy M.S., Girman D.J., Garcia-Moreno J., Ostrander E.A., Wayne R.K.
Mol. Ecol. 3:301-312(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L29413 Genomic DNA. Translation: AAA53663.2. Sequence problems.

3D structure databases

ProteinModelPortalQ33375.
SMRQ33375. Positions 2-196.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_CANSI
AccessionPrimary (citable) accession number: Q33375
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: May 14, 2014
This is version 81 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