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Q2I3H2 (COX1_ELEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 42. 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:MT-CO1
Synonyms:COI, COXI, MTCO1
Encoded onMitochondrion
OrganismElephas maximus (Indian elephant)
Taxonomic identifier9783 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaAfrotheriaProboscideaElephantidaeElephas

Protein attributes

Sequence length515 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 – 515515Cytochrome c oxidase subunit 1
PRO_0000232840

Regions

Transmembrane17 – 3721Helical; Potential
Transmembrane63 – 8321Helical; Potential
Transmembrane100 – 12021Helical; Potential
Transmembrane145 – 16521Helical; Potential
Transmembrane183 – 20321Helical; Potential
Transmembrane234 – 25421Helical; Potential
Transmembrane268 – 28821Helical; Potential
Transmembrane310 – 33021Helical; 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
Q2I3H2 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: DF28109BCDC07449

FASTA51557,165
        10         20         30         40         50         60 
MFANRWLYST NHKDIGTLYL LFGAWAGMVG TAFSILIRAE LGQPGSLLGD DQIYNVIVTA 

        70         80         90        100        110        120 
HAFVMIFFMV MPIMIGGFGN WLIPLMIGAP DMAFPRMNNM SFWLLPPSFL LLLASSMVEA 

       130        140        150        160        170        180 
GTGTGWTVYP PLAGNLAHAG ASVDLTIFSL HLAGVSSILS AINFITTIIN MKPPAMSQYH 

       190        200        210        220        230        240 
MPLFVWSILV TAVLLLLSLP VLAAGITMLL TDRNLNTTFF DPAGGGDPVL YQHLFWFFGH 

       250        260        270        280        290        300 
PEVYILILPG FGMVSHIVTY YSGKKEPFGY MGMVWAMMSI GFLGFIVWAH HMFTVGMDVD 

       310        320        330        340        350        360 
TRAYFTSATM IIAIPTGVKV FSWLATLHGG NIKWSPAMMW ALGFIFLFTI GGLTGIVLAN 

       370        380        390        400        410        420 
SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM GGFIHWFPLF SGYTLNYTWA KIQFLVMFIG 

       430        440        450        460        470        480 
VNLTFFPQHF LGLSGMPRRY SDYPDAYTAW NTASSMGSFI SLVAVILMVF MIWEAFASKR 

       490        500        510 
EVSMMELMTT NVEWLNGCPP PHHTFEEPAY VKSNS 

« Hide

References

[1]"Complete mitochondrial genome and phylogeny of Pleistocene mammoth Mammuthus primigenius."
Rogaev E.I., Moliaka Y.K., Malyarchuk B.A., Kondrashov F.A., Derenko M.V., Chumakov I., Grigorenko A.P.
PLoS Biol. 4:403-410(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Blood.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ316068 Genomic DNA. Translation: ABC17893.1.
RefSeqYP_626369.1. NC_005129.2.

3D structure databases

ProteinModelPortalQ2I3H2.
SMRQ2I3H2. Positions 1-511.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2610363.

Organism-specific databases

CTD4512.

Phylogenomic databases

HOVERGENHBG003841.
ProtClustDBMTH00103.

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_ELEMA
AccessionPrimary (citable) accession number: Q2I3H2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: March 7, 2006
Last modified: March 19, 2014
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways