P50693 (COX2_CULQU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 78.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames 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 |
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| Encoded on | Mitochondrion | ||||
| Organism | Culex quinquefasciatus (Southern house mosquito) (Culex pungens) | ||||
| Taxonomic identifier | 7176 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Nematocera › Culicoidea › Culicidae › Culicinae › Culicini › Culex › Culex › ![]() |
Protein attributes
| Sequence length | 228 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred 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 | |
| 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 |
| Domain | Transmembrane Transmembrane helix |
| Ligand | Copper Metal-binding |
| Molecular function | Oxidoreductase |
| Gene Ontology (GO) | |
| Biological_process | electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial inner membraneInferred from electronic annotation. Source: UniProtKB-SubCell respiratory chainInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | copper ion binding Inferred from electronic annotation. Source: InterPro cytochrome-c oxidase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 228 | 228 | Cytochrome c oxidase subunit 2 | PRO_0000183561 | |||||
Regions | |||||||||
| Topological domain | 1 – 26 | 26 | Mitochondrial intermembrane Potential | ||||||
| Transmembrane | 27 – 48 | 22 | Helical; Potential | ||||||
| Topological domain | 49 – 62 | 14 | Mitochondrial matrix Potential | ||||||
| Transmembrane | 63 – 82 | 20 | Helical; Potential | ||||||
| Topological domain | 83 – 228 | 146 | Mitochondrial intermembrane Potential | ||||||
Sites | |||||||||
| Metal binding | 161 | 1 | Copper A Probable | ||||||
| Metal binding | 196 | 1 | Copper A Probable | ||||||
| Metal binding | 200 | 1 | Copper A Probable | ||||||
| Metal binding | 204 | 1 | Copper A Probable | ||||||
Experimental info | |||||||||
| Sequence conflict | 8 | 1 | G → W in AAK14328. Ref.2 | ||||||
| Sequence conflict | 135 | 1 | L → S in AAK14328. Ref.2 | ||||||
Sequences
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References
| [1] | "Gene for cytochrome c oxidase subunit II in the mitochondrial DNA of Culex quinquefasciatus and Aedes aegypti (Diptera: Culicidae)." Ho C.M., Liu Y.M., Wei Y.H., Hu S.T. J. Med. Entomol. 32:174-180(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Yi-lan. Tissue: Larva. |
| [2] | "Molecular evolution of the mitochondrial cytochrome oxidase II gene in three mosquitoes." Wang J., Huang C. Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [3] | "Phylogenetic relationships of some common Culex mosquitoes of Bangladesh based on nuclear and mitochondrial DNA." Hasan A.U., Suguri S., Abedin S.M., Fujimoto C., Itaki R., Harada M., Zaman R.U., Al Mamun M.A., Rahman M.A. Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L34351 Genomic DNA. Translation: AAA79167.1. AF325716 Genomic DNA. Translation: AAK14328.1. EU014281 Genomic DNA. Translation: ABS52760.1. EU014282 Genomic DNA. Translation: ABS52761.1. |
3D structure databases | |
| ProteinModelPortal | P50693. |
| SMR | P50693. Positions 1-227. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| Gene3D | 1.10.287.90. 1 hit. 2.60.40.420. 1 hit. |
| InterPro | IPR001505. Copper_CuA. IPR008972. Cupredoxin. IPR014222. Cyt_c_oxidase_su2. 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. |
| TIGRFAMs | TIGR02866. CoxB. 1 hit. |
| PROSITE | PS00078. COX2. 1 hit. PS50857. COX2_CUA. 1 hit. PS50999. COX2_TM. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | COX2_CULQU | ||||||||
| Accession | Primary (citable) accession number: P50693 Secondary accession number(s): A7LGN8, Q9B813 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
