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Q37705 (COX1_ARTSF) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 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
Synonyms:CO-I
Encoded onMitochondrion
OrganismArtemia franciscana (Brine shrimp) (Artemia sanfranciscana)
Taxonomic identifier6661 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaCrustaceaBranchiopodaAnostracaArtemiidaeArtemia

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_0000183287

Regions

Transmembrane15 – 3521Helical; Potential
Transmembrane54 – 7421Helical; Potential
Transmembrane100 – 12021Helical; Potential
Transmembrane143 – 16321Helical; Potential
Transmembrane181 – 20121Helical; Potential
Transmembrane232 – 25221Helical; Potential
Transmembrane266 – 28621Helical; Potential
Transmembrane303 – 32321Helical; Potential
Transmembrane336 – 35621Helical; Potential
Transmembrane378 – 39821Helical; Potential
Transmembrane412 – 43221Helical; Potential
Transmembrane450 – 47021Helical; Potential

Sites

Metal binding591Iron (heme A axial ligand) Probable
Metal binding2381Copper B Probable
Metal binding2421Copper B Probable
Metal binding2881Copper B Probable
Metal binding2891Copper B Probable
Metal binding3741Iron (heme A3 axial ligand) Probable
Metal binding3761Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link238 ↔ 2421'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q37705 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 4AA1E1BBE64913E3

FASTA51256,492
        10         20         30         40         50         60 
MQRWFYSTNH KDIGTLYFIF GAWAGMVGTS LSMLIRAELG QPGSLIGDEQ VYNVIVTAHA 

        70         80         90        100        110        120 
FIMIFFMVMP ILIGGFGNWL VPIMLGAPDM AFPRLNNLSF WMLPPSLTLL LASSMVESGA 

       130        140        150        160        170        180 
GTGWTVYPPL SSAIAHAGPS VDLAIFSLHL AGVSSILGAV NFITTIINMR PQSMSIDRMP 

       190        200        210        220        230        240 
LFVWAVGITA VLLLLSLPVL AGAITMLLTD RNLNTSFFDP AGGGDPILYQ HLFWFFGHPE 

       250        260        270        280        290        300 
VYILILPGFG MVSHIISQES GKKEAFGTLG MIYAMLAIGI LGFVVWAHHM FTVGMDVDTR 

       310        320        330        340        350        360 
AYFTAATMII AIPTGIKIFS WIGTLHGTRL TMTPSMLWAL GFVFLFTVGG LTGVVLSNSS 

       370        380        390        400        410        420 
IDIVLHDTYY VVAHFHYVLS MGAVFAIMAG FVHWFPLMTG LSMNQFLLKV HFFIMFLGVN 

       430        440        450        460        470        480 
LTFFPQHFLG LAGMPRRYAD YPDTYASWNV ISSLGSVMSM IATLMFIFCI WEAMIAKRIN 

       490        500        510 
IFSLNLSSSV EWNHPHPPAD HSYEEITMIS TF 

« Hide

References

[1]"Speciation in the Artemia genus: mitochondrial DNA analysis of bisexual and parthenogenetic brine shrimps."
Perez M.L., Valverde J.R., Batuecas B., Amat F., Marco R., Garesse R.
J. Mol. Evol. 38:156-168(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X69067 Genomic DNA. Translation: CAA48806.1.
PIRS60622.
RefSeqNP_007109.1. NC_001620.1.

3D structure databases

ProteinModelPortalQ37705.
SMRQ37705. Positions 1-510.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID807790.

Organism-specific databases

CTD4512.

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_ARTSF
AccessionPrimary (citable) accession number: Q37705
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: May 14, 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