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Reviewed, UniProtKB/Swiss-Prot P41310 (COX1_DIDMA)

Last modified November 24, 2009. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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
OrganismDidelphis marsupialis virginiana (North American opossum)
Taxonomic identifier9267 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaMetatheriaDidelphimorphiaDidelphidaeDidelphis

Protein attributes

Sequence length513 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 – 513513Cytochrome c oxidase subunit 1
PRO_0000183322

Regions

Transmembrane17 – 3721 Potential
Transmembrane56 – 7621 Potential
Transmembrane102 – 12221 Potential
Transmembrane145 – 16521 Potential
Transmembrane183 – 20321 Potential
Transmembrane234 – 25421 Potential
Transmembrane268 – 28821 Potential
Transmembrane310 – 33021 Potential
Transmembrane338 – 35821 Potential
Transmembrane380 – 40021 Potential
Transmembrane412 – 43221 Potential
Transmembrane456 – 47621 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
P41310-1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: FFDAF8036663E8C0

FASTA51357,002
        10         20         30         40         50         60 
MFINRWLFST NHKDIGTLYL LFGAWAGMVG TALSLLIRAE LGQPGTLIGD DQIYNVIVTA 

        70         80         90        100        110        120 
HAFIMIFFMV MPIMIGGFGN WLVPLMIGAP DMAFPRMNNM SFWLLPPSFL LLLASSTIEA 

       130        140        150        160        170        180 
GAGTGWTVYP PLAGNLAHAG ASVDLAIFSL HLAGISSILG AINFITTIIN MKPPAMSQYQ 

       190        200        210        220        230        240 
TPLFVWSVMI TAVLLLLSLP VLAAGITMLL TDRNLNTTFF DPAGGGDPIL YQHLFWFFGH 

       250        260        270        280        290        300 
PEVYILILPG FGMISHIVTY YSGKKEPFGY MGMVWAMMSI GFLGFIVWAH HMFTVGLDVD 

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

       370        380        390        400        410        420 
SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM GGFVHWFPLF TGYMLNDMWA KIHFFIMFVG 

       430        440        450        460        470        480 
VNLTFFPQHF LGLSGMPRRY SDYPDAYTMW NVVSSIGSFI SLTAVILMVF IIWEAFASKR 

       490        500        510 
EVLDVELTTT NIEWLYGCPP PYHTFEQPVF IKA 

« Hide

References

[1]"The marsupial mitochondrial genome and the evolution of placental mammals."
Janke A., Feldmaier-Fuchs G., Thomas K., von Haeseler A., Paabo S.
Genetics 137:243-256(1994) [PubMed: 8056314] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z29573 Genomic DNA. Translation: CAA82679.1.
PIRS47872.
RefSeqNP_007097.1.

3D structure databases

SMRP41310. Positions 1-511.
ModBaseSearch...

Genome annotation databases

GeneID807779.

Organism-specific databases

CTD807779.

Phylogenomic databases

HOVERGENP41310.

Enzyme and pathway databases

BRENDA1.9.3.1. 281319.

Family and domain databases

InterProIPR000883. Cyt_c_oxidase_su1.
[Graphical view]
Gene3DG3DSA:1.20.210.10. COX1. 1 hit.
PANTHERPTHR10422. COX1. 1 hit.
PfamPF00115. COX1. 1 hit.
[Graphical view]
PRINTSPR01165. CYCOXIDASEI.
PROSITEPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX1_DIDMA
AccessionPrimary (citable) accession number: P41310
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 24, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents