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P93285 (COX2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. 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 2

EC=1.9.3.1
Alternative name(s):
Cytochrome c oxidase polypeptide II
Gene names
Name:COX2
Synonyms:COXII
Ordered Locus Names:AtMg00160
Encoded onMitochondrion
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length260 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

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 By similarity.

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 Ref.3.

Sequence similarities

Belongs to the cytochrome c oxidase subunit 2 family.

RNA editing

Edited at positions 9, 24, 85, 93, 127, 159, 186, 194, 233, 241 and 248. Ref.2

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 260260Cytochrome c oxidase subunit 2
PRO_0000183502

Regions

Topological domain1 – 4141Mitochondrial intermembrane Potential
Transmembrane42 – 6221Helical; Potential
Topological domain63 – 8624Mitochondrial matrix Potential
Transmembrane87 – 10721Helical; Potential
Topological domain108 – 260153Mitochondrial intermembrane Potential

Sites

Metal binding1871Copper A By similarity
Metal binding2221Copper A By similarity
Metal binding2261Copper A By similarity
Metal binding2301Copper A By similarity

Sequences

Sequence LengthMass (Da)Tools
P93285 [UniParc].

Last modified March 1, 2004. Version 2.
Checksum: 7D2D75A093973985

FASTA26029,674
        10         20         30         40         50         60 
MIVLKWLFFT ISPCDAAEPW QLGFQDAATP IMQGIIDLHH DIFFFLILIL VFVLWILVRA 

        70         80         90        100        110        120 
LWHFHYKKNA IPQRIVHGTT IEILWTIFPS IILMFIAIPS FALLYSMDEV VVDPAITIKA 

       130        140        150        160        170        180 
IGHQWYWTYE YSDYNSSDEQ SLTFDSYMIP EEDLELGQLR LLEVDNRVVV PAKTHLRIIV 

       190        200        210        220        230        240 
TSADVLHSWA VPSLGVKCDA VPGRLNQISI LVQREGVYYG QCSEICGTNH AFMSIVVEAV 

       250        260 
SRKDYGSWVS NQLIPQTGEA 

« Hide

References

« Hide 'large scale' references
[1]"The mitochondrial genome of Arabidopsis thaliana contains 57 genes in 366,924 nucleotides."
Unseld M., Marienfeld J.R., Brandt P., Brennicke A.
Nat. Genet. 15:57-61(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"RNA editing in Arabidopsis mitochondria effects 441 C to U changes in ORFs."
Giege P., Brennicke A.
Proc. Natl. Acad. Sci. U.S.A. 96:15324-15329(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], RNA EDITING.
[3]"Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins."
Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H.
Plant Cell 16:241-256(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Strain: cv. Landsberg erecta.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y08501 Genomic DNA. Translation: CAA69761.3. Sequence problems.
RefSeqNP_085487.1. NC_001284.2.

3D structure databases

ProteinModelPortalP93285.
SMRP93285. Positions 17-253.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid7. 1 interaction.

Proteomic databases

PaxDbP93285.
PRIDEP93285.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID814573.
KEGGath:ArthMp015.

Organism-specific databases

TAIRATMG00160.

Phylogenomic databases

eggNOGCOG1622.
HOGENOMHOG000264988.
KOK02261.

Enzyme and pathway databases

BioCycARA:ATMG00160-MONOMER.
MetaCyc:ATMG00160-MONOMER.

Gene expression databases

GenevestigatorP93285.

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_ARATH
AccessionPrimary (citable) accession number: P93285
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: March 1, 2004
Last modified: April 16, 2014
This is version 104 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

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names