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P15544 (COX1_STRPU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. 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
OrganismStrongylocentrotus purpuratus (Purple sea urchin) [Reference proteome]
Taxonomic identifier7668 [NCBI]
Taxonomic lineageEukaryotaMetazoaEchinodermataEleutherozoaEchinozoaEchinoideaEuechinoideaEchinaceaEchinoidaStrongylocentrotidaeStrongylocentrotus

Protein attributes

Sequence length517 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 – 517517Cytochrome c oxidase subunit 1
PRO_0000183423

Regions

Transmembrane17 – 3721Helical; Potential
Transmembrane63 – 8321Helical; Potential
Transmembrane102 – 12221Helical; Potential
Transmembrane145 – 16521Helical; Potential
Transmembrane183 – 20321Helical; Potential
Transmembrane234 – 25421Helical; Potential
Transmembrane268 – 28821Helical; Potential
Transmembrane305 – 32521Helical; Potential
Transmembrane338 – 35821Helical; Potential
Transmembrane380 – 40021Helical; Potential
Transmembrane414 – 43421Helical; Potential
Transmembrane456 – 47621Helical; Potential

Sites

Metal binding611Iron (heme A axial ligand) Probable
Metal binding2401Copper B Probable
Metal binding2441Copper B Probable
Metal binding2901Copper B Probable
Metal binding2911Copper B Probable
Metal binding3761Iron (heme A3 axial ligand) Probable
Metal binding3781Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link240 ↔ 2441'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

Sequence LengthMass (Da)Tools
P15544 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: A3FBC0A23C9042FE

FASTA51757,306
        10         20         30         40         50         60 
MQLSRWLFST NHKDIGTLYL IFGAWAGMVG TAMSVIIRAE LAQPGSLLND DQIYNVVVTA 

        70         80         90        100        110        120 
HALVMIFFMV MPIMIGGFGN WLIPLMIGAP DMAFPRMNNM SFWLIPPSFI LLLASAGVEN 

       130        140        150        160        170        180 
GAGTGWTIYP PLSSNITHAG SSVDLAIFSL HLAGASSILG LINFITTIIN MRTPGMSLDR 

       190        200        210        220        230        240 
LPLFVWSVFV TAFLLLLSLP VLAGAITMLL TDRNINTTFF DPAGGGDPIL FQHLFWLFGH 

       250        260        270        280        290        300 
PEVYILILPG FGMISHVIAH YSGKREPFGY LGLVYAMIAI GVLGFLVWAH HMFTVGMDVD 

       310        320        330        340        350        360 
TRAYFTAATM IIAVPTGLKV FSWMAKLQGS NLQWSLPLLW TLGIVFLFTL GGLTGIVLAN 

       370        380        390        400        410        420 
SSIDFVLHDT YYVVAHFHYV LSMGAVFAIF AGFTHWFPLF SGYSLHPLWG KVHFFIMFVG 

       430        440        450        460        470        480 
VNLTFFPQHF LGLAGMPRRY SDYPDAYTLW NTISSIGSTI SVVAMLFFLF LIWEAFASQR 

       490        500        510 
EGITPEFSHA SLEWQYTSFP PSHHTFDETP STIIIVK 

« Hide

References

[1]"Nucleotide sequence and gene organization of sea urchin mitochondrial DNA."
Jacobs H.T., Elliott D.J., Math V.B., Farquharson A.
J. Mol. Biol. 202:185-217(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Egg.
[2]Erratum
Jacobs H.T., Elliott D.J., Math V.B., Farquharson A.
J. Mol. Biol. 211:663-663(1990)
Cited for: SEQUENCE REVISION TO 61-62.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X12631 Genomic DNA. Translation: CAA31153.1.
PIRS01501.
RefSeqNP_006967.1. NC_001453.1.

3D structure databases

ProteinModelPortalP15544.
SMRP15544. Positions 3-508.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7668.P15544.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2652718.
KEGGspu:2652718.

Organism-specific databases

CTD4512.

Phylogenomic databases

eggNOGCOG0843.
InParanoidP15544.
KOK02256.
ProtClustDBMTH00037.

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_STRPU
AccessionPrimary (citable) accession number: P15544
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: April 16, 2014
This is version 98 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