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

P26856 (COX1_MARPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 87. 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:COX1
Synonyms:COXI
Encoded onMitochondrion
OrganismMarchantia polymorpha (Liverwort) (Marchantia aquatica)
Taxonomic identifier3197 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaMarchantiophytaMarchantiopsidaMarchantiidaeMarchantialesMarchantiaceaeMarchantia

Protein attributes

Sequence length522 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 – 522522Cytochrome c oxidase subunit 1
PRO_0000183360

Regions

Transmembrane19 – 3921Helical; Potential
Transmembrane67 – 8721Helical; Potential
Transmembrane104 – 12421Helical; Potential
Transmembrane149 – 16921Helical; Potential
Transmembrane187 – 20721Helical; Potential
Transmembrane238 – 25821Helical; Potential
Transmembrane270 – 29021Helical; Potential
Transmembrane313 – 33321Helical; Potential
Transmembrane341 – 36121Helical; Potential
Transmembrane380 – 40021Helical; Potential
Transmembrane417 – 43721Helical; Potential
Transmembrane459 – 47921Helical; Potential

Sites

Metal binding651Iron (heme A axial ligand) Probable
Metal binding2441Copper B Probable
Metal binding2481Copper B Probable
Metal binding2931Copper B Probable
Metal binding2941Copper B Probable
Metal binding3791Iron (heme A3 axial ligand) Probable
Metal binding3811Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link244 ↔ 2481'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

Sequence LengthMass (Da)Tools
P26856 [UniParc].

Last modified February 1, 1994. Version 2.
Checksum: 4B88E16F03A11D01

FASTA52257,552
        10         20         30         40         50         60 
MNNFAQRWLF STNHKDIGTL YLIFGAIAGV MGTCFSVLIR MELAQPGNQI LGGNHQLYNV 

        70         80         90        100        110        120 
LITAHAFLMI FFMVMPAMIG GFGNWFVPIL IGSPDMAFPR LNNISFWLLP PSLLLLLSSA 

       130        140        150        160        170        180 
LVEVGCGSGW TVYPPLSGIT SHSGGSVDLA IFSLHLSGVS SILGSINFIT TIFNMRAPGL 

       190        200        210        220        230        240 
TMHRLPLFVW SVLVTAFLLL LSLPVLAGAI TMLLTDRNFN TTFFDPAGGG DPILYQHLFW 

       250        260        270        280        290        300 
FFGHPEVYIL ILPGFGIISH IVSTFSRKPV FGYLGMVYAM ISIGVLGFIV WAHHMFTVGL 

       310        320        330        340        350        360 
DVDTRAYFTA ATMIIAVPTG IKIFSWIATM WGGSIQYKTP MLFAVGFIFL FTVGGLTGIV 

       370        380        390        400        410        420 
LANSGVDIAL HDTYYVVAHF HYVLSMGAVF ALFAGFYYWI GKITGLQYPE TLGQIHFWIT 

       430        440        450        460        470        480 
FFGVNLTFFP MHFLGLAGMP RRIPDYPDAY AGWNAFSSFG SYVSVVGIFC FFVVVFLTLT 

       490        500        510        520 
SENKCAPSPW AVEQNSTTLE WMVPSPPAFH TFEELPAIKE SI 

« Hide

References

[1]"Gene organization deduced from the complete sequence of liverwort Marchantia polymorpha mitochondrial DNA. A primitive form of plant mitochondrial genome."
Oda K., Yamato K., Ohta E., Nakamura Y., Takemura M., Nozato N., Akashi K., Kanegae T., Ogura Y., Kohchi T., Ohyama K.
J. Mol. Biol. 223:1-7(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M68929 Genomic DNA. Translation: AAC09451.1.
PIRS25956.
RefSeqNP_054454.1. NC_001660.1.

3D structure databases

ProteinModelPortalP26856.
SMRP26856. Positions 4-514.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2702483.

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.
IPR014241. Cyt_c_oxidase_su1_bac.
[Graphical view]
PANTHERPTHR10422. PTHR10422. 1 hit.
PfamPF00115. COX1. 1 hit.
[Graphical view]
PRINTSPR01165. CYCOXIDASEI.
SUPFAMSSF81442. SSF81442. 1 hit.
TIGRFAMsTIGR02891. CtaD_CoxA. 1 hit.
PROSITEPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX1_MARPO
AccessionPrimary (citable) accession number: P26856
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: February 1, 1994
Last modified: April 16, 2014
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways