Skip Header

Contribute Send feedback
Read comments (?) or add your own

O21400 (COX2_STRCA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 83. 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
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:MT-CO2
Synonyms:COII, COXII, MTCO2
Encoded onMitochondrion
OrganismStruthio camelus (Ostrich)
Taxonomic identifier8801 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Palaeognathae › Struthioniformes › Struthionidae › Struthio

Protein attributes

Sequence length229 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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 229229Cytochrome c oxidase subunit 2
PRO_0000183696

Regions

Topological domain1 – 2626Mitochondrial intermembrane Potential
Transmembrane27 – 4721Helical; Potential
Topological domain48 – 6114Mitochondrial matrix Potential
Transmembrane62 – 8120Helical; Potential
Topological domain82 – 229148Mitochondrial intermembrane Potential

Sites

Metal binding1601Copper A Probable
Metal binding1951Copper A Probable
Metal binding1991Copper A Probable
Metal binding2031Copper A Probable

Sequences

Sequence LengthMass (Da)Tools
O21400 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: B9377617BACB14EF

FASTA22925,700
        10         20         30         40         50         60 
MANPSQFGFQ DASSPIMEEL VEFHDHALMV ALAICSLVLY LLALMLVEKL SSNTVDAQEV 

        70         80         90        100        110        120 
ELIWTILPAI VLILLALPSL QILYMMDEID EPDLTLKAIG HQWYWSYEYT DFKDLTFDSY 

       130        140        150        160        170        180 
MIPTSELPPG HFRLLEVDHR VVVPMESPIR VIITAGDVLH SWAVPTLGVK TDAIPGRLNQ 

       190        200        210        220 
TSFITTRPGI FYGQCSEICG ANHSYMPIVV ESTPLTYFES WSSLLSTDS

« Hide

References

[1]"The mtDNA sequence of the ostrich and the divergence between paleognathous and neognathous birds."
Harlid A., Janke A., Arnason U.
Mol. Biol. Evol. 14:754-761(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Primers for a PCR-based approach to complete mitochondrial genome sequencing."
Sorenson M.D., Dimcheff D.E., Ast J.C., Yuri T., Mindell D.P.
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Complete mitochondrial DNA genome sequences of extinct birds: ratite phylogenetics and the vicariance biogeography hypothesis."
Haddrath O., Baker A.J.
Proc. R. Soc. B 268:939-945(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Phylogenetic relationships of the ratite birds: resolving conflicts between molecular and morphological data sets."
Lee K., Feinstein J., Cracraft J.
(In) Mindell D.P. (eds.); Avian molecular evolution and systematics, pp.1-1, Academic Press, New York (1997)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-229.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Y12025 Genomic DNA. Translation: CAA72747.1.
AF069429 Genomic DNA. Translation: AAD09386.1.
AF338715 Genomic DNA. Translation: AAK53348.1.
U76069 Genomic DNA. Translation: AAB61329.1. Different termination.
PIRD90612.
T12412.
RefSeqNP_115444.1. NC_002785.1.

3D structure databases

ProteinModelPortalO21400.
SMRO21400. Positions 1-223.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID803280.

Organism-specific databases

CTD4513.

Phylogenomic databases

HOVERGENHBG012727.
ProtClustDBMTH00117.

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. Cupredoxin. 1 hit.
SSF81464. Cyt_c_oxidase_II-like_TM. 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_STRCA
AccessionPrimary (citable) accession number: O21400
Secondary accession number(s): O03894
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: May 1, 2013
This is version 83 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents