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Protein

Cytochrome c oxidase subunit 2

Gene

COX2

Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

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 activityi

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

Cofactori

Cu cationNote: Binds a copper A center.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi182 – 1821Copper ACurated
Metal bindingi217 – 2171Copper ACurated
Metal bindingi221 – 2211Copper ACurated
Metal bindingi225 – 2251Copper ACurated

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome c oxidase subunit 2 (EC:1.9.3.1)
Alternative name(s):
Cytochrome c oxidase polypeptide II
Gene namesi
Name:COX2
Encoded oniMitochondrion
OrganismiKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Taxonomic identifieri284590 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces
ProteomesiUP000000598 Componenti: Mitochondrion

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini12 – 3827Mitochondrial intermembraneSequence AnalysisAdd
BLAST
Transmembranei39 – 5921HelicalSequence AnalysisAdd
BLAST
Topological domaini60 – 7819Mitochondrial matrixSequence AnalysisAdd
BLAST
Transmembranei79 – 10123HelicalSequence AnalysisAdd
BLAST
Topological domaini102 – 247146Mitochondrial intermembraneSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1111By similarityAdd
BLAST
Chaini12 – 247236Cytochrome c oxidase subunit 2PRO_0000006039Add
BLAST

Post-translational modificationi

The signal sequence of COX2 is processed by IMP1.

Interactioni

Protein-protein interaction databases

STRINGi28985.P20387.

Structurei

3D structure databases

ProteinModelPortaliP20387.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000264988.
InParanoidiP20387.
KOiK02261.
OrthoDBiEOG7WDNDC.

Family and domain databases

Gene3Di1.10.287.90. 1 hit.
2.60.40.420. 1 hit.
InterProiIPR001505. Copper_CuA.
IPR008972. Cupredoxin.
IPR014222. Cyt_c_oxidase_su2.
IPR002429. Cyt_c_oxidase_su2_C.
IPR011759. Cyt_c_oxidase_su2_TM_dom.
[Graphical view]
PfamiPF00116. COX2. 1 hit.
PF02790. COX2_TM. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 1 hit.
SSF81464. SSF81464. 1 hit.
TIGRFAMsiTIGR02866. CoxB. 1 hit.
PROSITEiPS00078. COX2. 1 hit.
PS50857. COX2_CUA. 1 hit.
PS50999. COX2_TM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P20387-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFYLLNSIIM NDVPTPYGMY FQDSATPNQE GILELHDNIM FYLFIILGLV
60 70 80 90 100
SWLLFTIVRT YSKNPIAYKY IKHGQTIEII WTIFPAVILL IIAFPSFILL
110 120 130 140 150
YLCDEVISPA MTIKAIGLQW YWKYEYSDFI NDNGETVEFE SYVIPEDLLE
160 170 180 190 200
DGQLRLLDTD TSVVVPVDTH IRFVVTAADV IHDFAVPSLG IKIDAAPGRL
210 220 230 240
NQVSALIQRE GVFYGQCSEI CGQSHSAMPI KIEAVSLPAF LEWLNEQ
Length:247
Mass (Da):28,102
Last modified:October 11, 2004 - v3
Checksum:iAA9261AFC1C138DB
GO

Sequence cautioni

The sequence AAT64953.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti86 – 861A → D (PubMed:2171241).Curated
Sequence conflicti86 – 861A → D (PubMed:15691736).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15999 Genomic DNA. Translation: CAA34129.2.
AY654900 Genomic DNA. Translation: AAT64953.1. Different initiation.
PIRiS11171. OBVK2M.
RefSeqiYP_054502.1. NC_006077.1.

Genome annotation databases

GeneIDi2914081.
KEGGikla:KllafMp06.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15999 Genomic DNA. Translation: CAA34129.2.
AY654900 Genomic DNA. Translation: AAT64953.1. Different initiation.
PIRiS11171. OBVK2M.
RefSeqiYP_054502.1. NC_006077.1.

3D structure databases

ProteinModelPortaliP20387.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi28985.P20387.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2914081.
KEGGikla:KllafMp06.

Phylogenomic databases

HOGENOMiHOG000264988.
InParanoidiP20387.
KOiK02261.
OrthoDBiEOG7WDNDC.

Family and domain databases

Gene3Di1.10.287.90. 1 hit.
2.60.40.420. 1 hit.
InterProiIPR001505. Copper_CuA.
IPR008972. Cupredoxin.
IPR014222. Cyt_c_oxidase_su2.
IPR002429. Cyt_c_oxidase_su2_C.
IPR011759. Cyt_c_oxidase_su2_TM_dom.
[Graphical view]
PfamiPF00116. COX2. 1 hit.
PF02790. COX2_TM. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 1 hit.
SSF81464. SSF81464. 1 hit.
TIGRFAMsiTIGR02866. CoxB. 1 hit.
PROSITEiPS00078. COX2. 1 hit.
PS50857. COX2_CUA. 1 hit.
PS50999. COX2_TM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the cytochrome oxidase subunit 2 and val-tRNA genes and surrounding sequences from Kluyveromyces lactis K8 mitochondrial DNA."
    Hardy C.M., Clark-Walker G.D.
    Yeast 6:403-410(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 90735 / K8.
  2. Hardy C.M.
    Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 81-82.
  3. "Complete nucleotide sequence of the mitochondrial DNA from Kluyveromyces lactis."
    Zivanovic Y., Wincker P., Vacherie B., Bolotin-Fukuhara M., Fukuhara H.
    FEMS Yeast Res. 5:315-322(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 76492 / CBS 2359/152 / CLIB 210.

Entry informationi

Entry nameiCOX2_KLULA
AccessioniPrimary (citable) accession number: P20387
Secondary accession number(s): Q6DN57
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: October 11, 2004
Last modified: January 7, 2015
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.