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P43373 (COX2_CANGA) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 2

EC=1.9.3.1
Alternative name(s):
Cytochrome c oxidase polypeptide II
Gene names
Name:COX2
Encoded onMitochondrion
OrganismCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) [Complete proteome]
Taxonomic identifier284593 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeNakaseomycesmitosporic Nakaseomyces

Protein attributes

Sequence length251 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. Subunit 2 transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit 1.

Catalytic activity

4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O.

Cofactor

Copper A.

Subcellular location

Mitochondrion inner membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the cytochrome c oxidase subunit 2 family.

Sequence caution

The sequence CAD54426.1 differs from that shown. Reason: Frameshift at position 225.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 251251Cytochrome c oxidase subunit 2
PRO_0000183535

Regions

Transmembrane42 – 6221Helical; Potential
Transmembrane83 – 10321Helical; Potential

Sites

Metal binding1861Copper A Probable
Metal binding2211Copper A Probable
Metal binding2251Copper A Probable
Metal binding2291Copper A Probable

Experimental info

Sequence conflict181P → A in CAA49205. Ref.1
Sequence conflict901A → E in CAA49205. Ref.1
Sequence conflict971A → V in CAA49205. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P43373 [UniParc].

Last modified October 11, 2004. Version 2.
Checksum: AFA07BDBC0336028

FASTA25128,602
        10         20         30         40         50         60 
MLNLLNTLFL NVISNDVPTP YGIYFQDSAT PNQEGILELH DNIMFYLFII LGLVSWMLFT 

        70         80         90        100        110        120 
IVKTYSKNPM AYKYIKHGQT IEIIWTMFPA VILLIIAFPS FILLYLCDEV ISPAMTIKAI 

       130        140        150        160        170        180 
GYQWYWKYEY SDFINDNGET IEFESYVIPD DLLEEGQLRL LDTDTSVVVP VDTHIRFVVT 

       190        200        210        220        230        240 
GADVIHDFAI PSLGIKVDAN PGRLNQVSAL IQREGVFYGQ CSELCGVNHA AMPIKIEAVS 

       250 
LPKFLEWLNE Q 

« Hide

References

« Hide 'large scale' references
[1]"The structure of the small mitochondrial DNA of Kluyveromyces thermotolerans is likely to reflect the ancestral gene order in fungi."
Clark-Walker G.D., Weiller G.F.
J. Mol. Evol. 38:593-601(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65.
[2]"The complete mitochondrial genome sequence of the pathogenic yeast Candida (Torulopsis) glabrata."
Koszul R., Malpertuy A., Frangeul L., Bouchier C., Wincker P., Thierry A., Duthoy S., Ferris S., Hennequin C., Dujon B.
FEBS Lett. 534:39-48(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X69430 Genomic DNA. Translation: CAA49205.1.
AJ511533 Genomic DNA. Translation: CAD54426.1. Frameshift.
PIRS45438.
RefSeqNP_818785.1. NC_004691.1.

3D structure databases

ProteinModelPortalP43373.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID807024.
KEGGcgr:CaglfMp11.

Phylogenomic databases

HOGENOMHOG000264988.
KOK02261.
OrthoDBEOG7WDNDC.

Family and domain databases

Gene3D1.10.287.90. 1 hit.
2.60.40.420. 1 hit.
InterProIPR001505. Copper_CuA.
IPR008972. Cupredoxin.
IPR014222. Cyt_c_oxidase_su2.
IPR002429. Cyt_c_oxidase_su2_C.
IPR011759. Cyt_c_oxidase_su2_TM_dom.
[Graphical view]
PfamPF00116. COX2. 1 hit.
PF02790. COX2_TM. 1 hit.
[Graphical view]
SUPFAMSSF49503. SSF49503. 1 hit.
SSF81464. SSF81464. 1 hit.
TIGRFAMsTIGR02866. CoxB. 1 hit.
PROSITEPS00078. COX2. 1 hit.
PS50857. COX2_CUA. 1 hit.
PS50999. COX2_TM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX2_CANGA
AccessionPrimary (citable) accession number: P43373
Secondary accession number(s): Q85Q97
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 11, 2004
Last modified: March 19, 2014
This is version 98 of the entry and version 2 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