Cytochrome c oxidase subunit 2 - Caenorhabditis elegans

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P24894 (COX2_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 104. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Cytochrome c oxidase subunit 2
EC=1.9.3.1

Alternative name(s):
Cytochrome c oxidase polypeptide II

Gene names

Name:	cox-2
Synonyms:	coII
ORF Names:	MTCE.31

Encoded on

Mitochondrion

Organism

Caenorhabditis elegans [Reference proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Ecdysozoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	231 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
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.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mitochondrial electron transport, cytochrome c to oxygen Non-traceable author statement Ref.2. Source: UniProtKB
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial inner membrane Non-traceable author statement Ref.2. Source: UniProtKB respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	copper ion binding Inferred from electronic annotation. Source: InterPro cytochrome-c oxidase activity Non-traceable author statement Ref.2. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 231

231

Cytochrome c oxidase subunit 2

PRO_0000183526

Regions

Topological domain

1 – 30

Mitochondrial intermembrane Potential

Transmembrane

31 – 52

Helical; Potential

Topological domain

53 – 69

Mitochondrial matrix Potential

Transmembrane

70 – 89

Helical; Potential

Topological domain

90 – 231

142

Mitochondrial intermembrane Potential

Sites

Metal binding

164

Copper A Probable

Metal binding

199

Copper A Probable

Metal binding

203

Copper A Probable

Metal binding

207

Copper A Probable

Natural variations

Natural variant

132

S → N in strain: PB303. Ref.1

Natural variant

143

N → I in strain: CB4857. Ref.1

Natural variant

186

S → N in strain: AB2, CB4852, CB4853, CB4855, CB4858 and PB306. Ref.1

Natural variant

216

V → M in strain: AB1 and KR314. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P24894 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: FCD8D458D1B0DDAA
Show »

FASTA

231

26,549

        10         20         30         40         50         60 
MNNFFQGYNL LFQHSLFASY MDWFHSFNCS LLLGVLVFVT LLFGYLIFGT FYFKSKKIEY 

        70         80         90        100        110        120 
QFGELLCSIF PTIILLMQMV PSLSLLYYYG LMNLDSNLTV KVTGHQWYWS YEYSDIPGLE 

       130        140        150        160        170        180 
FDSYMKSLDQ LSLGEPRLLE VDNRCVIPCD TNIRFCITSA DVIHAWALNS LSVKLDAMSG 

       190        200        210        220        230 
ILSTFSYSFP MVGVFYGQCS EICGANHSFM PIALEVTLLD NFKSWCFGTM E

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Phylogenetics in Caenorhabditis elegans: an analysis of divergence and outcrossing." Denver D.R., Morris K., Thomas W.K. Mol. Biol. Evol. 20:393-400(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASN-132; ILE-143; ASN-186 AND MET-216. Strain: AB1, AB2, Bristol N2, CB4852, CB4853, CB4854, CB4855, CB4856, CB4857, CB4858, KR314, PB303, PB306, RW7000 and TR403.
[2]	"The mitochondrial genomes of two nematodes, Caenorhabditis elegans and Ascaris suum." Okimoto R., Macfarlane J.L., Clary D.O., Wolstenholme D.R. Genetics 130:471-498(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[3]	"Evidence for the frequent use of TTG as the translation initiation codon of mitochondrial protein genes in the nematodes, Ascaris suum and Caenorhabditis elegans." Okimoto R., Macfarlane J.L., Wolstenholme D.R. Nucleic Acids Res. 18:6113-6118(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY171193 Genomic DNA. Translation: AAO16253.1. AY171194 Genomic DNA. Translation: AAO16257.1. AY171195 Genomic DNA. Translation: AAO16261.1. AY171196 Genomic DNA. Translation: AAO16265.1. AY171197 Genomic DNA. Translation: AAO16269.1. AY171198 Genomic DNA. Translation: AAO16273.1. AY171199 Genomic DNA. Translation: AAO16277.1. AY171200 Genomic DNA. Translation: AAO16281.1. AY171201 Genomic DNA. Translation: AAO16285.1. AY171202 Genomic DNA. Translation: AAO16289.1. AY171203 Genomic DNA. Translation: AAO16293.1. AY171204 Genomic DNA. Translation: AAO16297.1. AY171205 Genomic DNA. Translation: AAO16301.1. AY171206 Genomic DNA. Translation: AAO16305.1. AY171207 Genomic DNA. Translation: AAO16309.1. X54252 Genomic DNA. Translation: CAA38160.1.
PIR	S26035.
RefSeq	NP_006962.1. NC_001328.1.
3D structure databases
ProteinModelPortal	P24894.
SMR	P24894. Positions 15-225.
ModBase	Search...
Proteomic databases
PaxDb	P24894.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2565697.
KEGG	cel:COX2.
Organism-specific databases
CTD	4513.
WormBase	MTCE.31; CE35351; WBGene00010965; cox-2.
Phylogenomic databases
eggNOG	COG1622.
HOGENOM	HOG000264988.
KO	K02261.
ProtClustDB	MTH00080.
Gene expression databases
ArrayExpress	P24894.
Family and domain databases
Gene3D	1.10.287.90. 1 hit. 2.60.40.420. 1 hit.
InterPro	IPR001505. Copper_CuA. IPR008972. Cupredoxin. IPR002429. Cyt_c_oxidase_su2_C. IPR011759. Cyt_c_oxidase_su2_TM_dom. [Graphical view]
Pfam	PF00116. COX2. 1 hit. PF02790. COX2_TM. 1 hit. [Graphical view]
SUPFAM	SSF49503. Cupredoxin. 1 hit. SSF81464. Cyt_c_oxidase_II-like_TM. 1 hit.
PROSITE	PS00078. COX2. 1 hit. PS50857. COX2_CUA. 1 hit. PS50999. COX2_TM. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	953869.

Entry information

Entry name

COX2_CAEEL

Accession

Primary (citable) accession number: P24894

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Natural variations

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents