Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P34838 (COX1_ANOGA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 93. 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 1

EC=1.9.3.1
Alternative name(s):
Cytochrome c oxidase polypeptide I
Gene names
Name:COI
Encoded onMitochondrion
OrganismAnopheles gambiae (African malaria mosquito) [Reference proteome]
Taxonomic identifier7165 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeAnophelinaeAnopheles

Protein attributes

Sequence length514 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. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.

Catalytic activity

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

Pathway

Energy metabolism; oxidative phosphorylation.

Subcellular location

Mitochondrion inner membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the heme-copper respiratory oxidase family.

Sequence caution

The sequence AAD12191.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 514514Cytochrome c oxidase subunit 1
PRO_0000183282

Regions

Transmembrane16 – 3621Helical; Potential
Transmembrane55 – 7521Helical; Potential
Transmembrane101 – 12121Helical; Potential
Transmembrane144 – 16421Helical; Potential
Transmembrane182 – 20221Helical; Potential
Transmembrane233 – 25321Helical; Potential
Transmembrane267 – 28721Helical; Potential
Transmembrane304 – 32421Helical; Potential
Transmembrane337 – 35721Helical; Potential
Transmembrane379 – 39921Helical; Potential
Transmembrane415 – 43521Helical; Potential
Transmembrane451 – 47121Helical; Potential

Sites

Metal binding601Iron (heme A axial ligand) Probable
Metal binding2391Copper B Probable
Metal binding2431Copper B Probable
Metal binding2891Copper B Probable
Metal binding2901Copper B Probable
Metal binding3751Iron (heme A3 axial ligand) Probable
Metal binding3771Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link239 ↔ 2431'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

Sequence LengthMass (Da)Tools
P34838 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 6459AC46AD258336

FASTA51456,841
        10         20         30         40         50         60 
MSRQWLFSTN HKDIGTLYFI FGAWAGMVGT SLSILIRAEL GHPGAFIGDD QIYNVIVTAH 

        70         80         90        100        110        120 
AFIMIFFMVM PIMIGGFGNW LVPLMLGAPD MAFPRMNNMS FWMLPPSLTL LISSSMVENG 

       130        140        150        160        170        180 
AGTGWTVYPP LSSGIAHAGA SVDLAIFSLH LAGISSILGA VNFITTVINM RSPGITLDRM 

       190        200        210        220        230        240 
PLFVWSVVIT AVLLLLSLPV LAGAITMLLT DRNLNTSFFD PAGGGDPILY QHLFWFFGHP 

       250        260        270        280        290        300 
EVYILILPGF GMISHIITQE SGKKETFGNL GMIYAMLAIG LLGFIVWAHH MFTVGMDVDT 

       310        320        330        340        350        360 
RAYFTSATMI IAVPTGIKIF SWLATLHGTQ LTYSPAMLWA FGFVFLFTVG GLTGVVLANS 

       370        380        390        400        410        420 
SIDIVLHDTY YVVAHFHYVL SMGAVFAIMA GFVHWYPLLT GLTMNPTWLK IQFSIMFVGV 

       430        440        450        460        470        480 
NLTFFPQHFL GLAGMPRRYS DFPDSYLTWN VVSSLGSTIS LFAILYFLFI IWESMITQRT 

       490        500        510 
PAFPMQLSSS IEWYHTLPPA EHTYAELPLL TNNF 

« Hide

References

[1]"The mitochondrial genome of the mosquito Anopheles gambiae: DNA sequence, genome organization, and comparisons with mitochondrial sequences of other insects."
Beard C.B., Hamm D.M., Collins F.H.
Insect Mol. Biol. 2:103-124(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: G3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L20934 Genomic DNA. Translation: AAD12191.1. Different initiation.
PIRT09801.
RefSeqNP_008070.1. NC_002084.1.

3D structure databases

ProteinModelPortalP34838.
SMRP34838. Positions 4-506.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1267414.
KEGGaga:COX1.

Organism-specific databases

CTD4512.

Phylogenomic databases

KOK02256.
ProtClustDBMTH00153.

Enzyme and pathway databases

UniPathwayUPA00705.

Family and domain databases

Gene3D1.20.210.10. 1 hit.
InterProIPR000883. Cyt_c_Oxase_su1.
IPR023615. Cyt_c_Oxase_su1_BS.
IPR023616. Cyt_c_Oxase_su1_dom.
[Graphical view]
PANTHERPTHR10422. PTHR10422. 1 hit.
PfamPF00115. COX1. 1 hit.
[Graphical view]
PRINTSPR01165. CYCOXIDASEI.
SUPFAMSSF81442. SSF81442. 1 hit.
PROSITEPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX1_ANOGA
AccessionPrimary (citable) accession number: P34838
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: April 16, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways