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Q01555 (COX1_TRIRU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 83. 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
Encoded onMitochondrion
OrganismTrichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum)
Taxonomic identifier5551 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesArthrodermataceaemitosporic ArthrodermataceaeTrichophyton

Protein attributes

Sequence length528 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 – 528528Cytochrome c oxidase subunit 1
PRO_0000183427

Regions

Transmembrane17 – 3721Helical; Potential
Transmembrane64 – 8421Helical; Potential
Transmembrane100 – 12021Helical; Potential
Transmembrane146 – 16621Helical; Potential
Transmembrane182 – 20221Helical; Potential
Transmembrane235 – 25521Helical; Potential
Transmembrane267 – 28721Helical; Potential
Transmembrane305 – 32521Helical; Potential
Transmembrane338 – 35821Helical; Potential
Transmembrane377 – 39721Helical; Potential
Transmembrane407 – 42721Helical; Potential
Transmembrane452 – 47221Helical; Potential

Sites

Metal binding621Iron (heme A axial ligand) Probable
Metal binding2411Copper B Probable
Metal binding2451Copper 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-link241 ↔ 2451'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q01555 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 313FE9CADC97718A

FASTA52858,460
        10         20         30         40         50         60 
MWKERWFLST NAKDIGTLYL MFRYFSGLVG TAFSVLIRLE LSAPGVQYIA DNQLYNSIIT 

        70         80         90        100        110        120 
AHAILMIFFM VMPALIGGFG NFLLPLLVGG PDMAFPRLNN ISFWLLIPSL LLFVFASIIE 

       130        140        150        160        170        180 
NGAGTGWTLY PPLASIQSHS GPSVDLAIFG LHLSGISSLL GAMNFITTII NMRSPGIRLH 

       190        200        210        220        230        240 
KLALFGWAVL ITAVLLLLSL PVLAGAITML LTDRNFNTSF FELAGGGDPI FIQHLFWFFG 

       250        260        270        280        290        300 
HPEVYILIVP GFGIISTVIS ANSSKNVFGY LGMVYAMMSI GILGFVFWSH HMYTVGLDVD 

       310        320        330        340        350        360 
TRAYFIAATL IIAVPTGIKI FSWLATCYGG SLNLTPAMLF ALGFVVMFTI GGLSGVVLAN 

       370        380        390        400        410        420 
ASLDIAFHDT YYVVAHFHYV LSMGAVFALF SGWYFWIPKL LGLSYDLFAG KVHFWILFVG 

       430        440        450        460        470        480 
VNLTLFPQHF LGLQGMPRRI GDYPDAFAGW NLISSFGSIV SVVATWYFLN ILYLQLTQGS 

       490        500        510        520 
PVSRYPWLTP QYFSDLFQHL FTRNNSSLEW CLNSPPKPHA FDCLPVQS 

« Hide

References

[1]"Mitochondrial DNA sequence analysis of the cytochrome oxidase subunit I and II genes, the ATPase9 gene, the NADH dehydrogenase ND4L and ND5 gene complex, and the glutaminyl, methionyl and arginyl tRNA genes from Trichophyton rubrum."
de Bievre C., Dujon B.
Curr. Genet. 22:229-234(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: IP 1817.89.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X65223 Genomic DNA. Translation: CAA46325.1.
PIRS26948.

3D structure databases

ProteinModelPortalQ01555.
SMRQ01555. Positions 1-522.
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_TRIRU
AccessionPrimary (citable) accession number: Q01555
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways