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P33504 (COX1_ANOQU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 85. 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 quadrimaculatus (Common malaria mosquito)
Taxonomic identifier7166 [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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 514514Cytochrome c oxidase subunit 1
PRO_0000183283

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
Transmembrane413 – 43321Helical; 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
P33504 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: D00A0F6F3D52B266

FASTA51456,871
        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 RAPGITLDRM 

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

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

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

       370        380        390        400        410        420 
SIDIVLHDTY YVVAHFHYVL SMGAVFAIMA GFIHWYPLLT GLTMNPNWLK LQFAMMFVGV 

       430        440        450        460        470        480 
NLTFFPQHFL GLAGMPRRYS DFPDSYLAWN IVSSLGSTIS LFAILYFLFI IWESMITQRT 

       490        500        510 
PAFPMQLSSS IEWYHTLPPA EHTYAELPLL TNNF 

« Hide

References

[1]"Cloning of the mitochondrial genome of Anopheles quadrimaculatus."
Cockburn A.F., Mitchell S.E., Seawright J.A.
Arch. Insect Biochem. Physiol. 14:31-36(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Orlando.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L04272 Genomic DNA. Translation: AAA93541.1.

3D structure databases

ProteinModelPortalP33504.
SMRP33504. Positions 4-506.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

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_ANOQU
AccessionPrimary (citable) accession number: P33504
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: April 16, 2014
This is version 85 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