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O99818 (COX1_RHISA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. 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
OrganismRhipicephalus sanguineus (Brown dog tick) (Ixodes sanguineus)
Taxonomic identifier34632 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaAcariParasitiformesIxodidaIxodoideaIxodidaeRhipicephalinaeRhipicephalusRhipicephalus

Protein attributes

Sequence length512 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 – 512512Cytochrome c oxidase subunit 1
PRO_0000183408

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
Transmembrane382 – 40221Helical; Potential
Transmembrane413 – 43321Helical; Potential
Transmembrane456 – 47621Helical; 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
O99818 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 53D6374C4DF11AB6

FASTA51257,126
        10         20         30         40         50         60 
MLPRWMYSTN HKDIGTMYLI FGAWSGMLGL SMSMLIRMEL GQPGTLIGND QIYNVIVTAH 

        70         80         90        100        110        120 
AFIMIFFMVM PIMIGGFGNW LVPIMLGAPD MAFPRMNNMS FWLLPPSLFL LINSSLIESG 

       130        140        150        160        170        180 
AGTGWTVYPP LSSNLSHYGP SVDLAIFSLH LAGASSILGA INFITTIVNM RSIGMTMERM 

       190        200        210        220        230        240 
PLFVWSVLIT AILLLLSLPV LAGAITMLLT DRNFNTSFFD PSGGGDPILY QHLFWFFGHP 

       250        260        270        280        290        300 
EVYILILPGF GMISQIICYN TGKKEPFGNL GMIYAMAAIG LLGFIVWAHH MFTVGMDVDT 

       310        320        330        340        350        360 
RAYFTSATMI IAVPTGIKIF SWLATLHGSH IKFNTSILWA LGFVFLFTVG GLTGIMLANS 

       370        380        390        400        410        420 
SIDIVLHDTY YVVAHFHYVL SMGAVFGIMG AIIHWFPMFL GLNLNSMLTK VQFMITFIGV 

       430        440        450        460        470        480 
NLTFFPQHFL GLAGMPRRYS DYPDFFTKWN FISSLGSLIS LMGVIMLIII IWTSIIEKKM 

       490        500        510 
INFSSFTNSS IEWMLNFPPS EHSFNQNNII LK 

« Hide

References

[1]"Mitochondrial gene order is not conserved in arthropods: prostriate and metastriate tick mitochondrial genomes."
Black W.C. IV, Roehrdanz R.L.
Mol. Biol. Evol. 15:1772-1785(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF081829 Genomic DNA. Translation: AAD05518.1.
PIRT11154.
RefSeqNP_008511.1. NC_002074.1.

3D structure databases

ProteinModelPortalO99818.
SMRO99818. Positions 4-506.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID808364.

Organism-specific databases

CTD4512.

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_RHISA
AccessionPrimary (citable) accession number: O99818
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 88 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