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Reviewed, UniProtKB/Swiss-Prot P34188 (COX1_CROLA)

Last modified June 16, 2009. Version 62. 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

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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
OrganismCrossostoma lacustre (Oriental stream loach)
Taxonomic identifier7980 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Ostariophysi › Cypriniformes › Balitoridae › Balitorinae › Crossostoma

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Protein attributes

Sequence length516 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 516516Cytochrome c oxidase subunit 1
PRO_0000183318

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
Transmembrane414 – 43421 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

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Sequences

Sequence LengthMass (Da)Tools
P34188-1 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: E5DBD18C495E9167

FASTA51656,953
        10         20         30         40         50         60 
MAITRWFFST NHKDIGTLYL VFGAWAGMVG TALSLLIRAE LNQPGALLGD DQIYNVIVTA 

        70         80         90        100        110        120 
HAFVMIFFMV MPILIGGFGN WLVPLMIGAP HMAFPRMNNM SFWLLPPSFL LLLASSGVEA 

       130        140        150        160        170        180 
GAGTGWTVYP PLAGNLAHAG ASVDLTIFSL HLAGVSSILG AINFITTTIN MKPPALSQYQ 

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

       250        260        270        280        290        300 
PEVYILILPG FGIISHVVAY YAGKKEPFGY MGMVWAMMAI GLLGFIVWAH HMFTVGMDVD 

       310        320        330        340        350        360 
TRAYFTSATM IIAIPTGVKV FSWLATLHGG TIKWDTPMLW ALGFIFLFTV GGLTGIVLSN 

       370        380        390        400        410        420 
SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM AGFVHWFPLF TGFSLHDTWT KIHFGVMFIG 

       430        440        450        460        470        480 
VNLTFFPQHF LGLAGMPRRY SDYPDAYTLW NTVSSIGSLI SLVAVIIFLF ILWEAFASKR 

       490        500        510 
QVMSVELTMT NVEWLHGCPP PYHTFEEPAF VQVRSN

« Hide

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References

[1]"The complete nucleotide sequence of the Crossostoma lacustre mitochondrial genome: conservation and variations among vertebrates."
Tzeng C.-S., Hui C.-F., Shen S.-C., Huang P.C.
Nucleic Acids Res. 20:4853-4858(1992) [PubMed: 1408800] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Oocyte.

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Cross-references

Sequence databases

M91245 Genomic DNA. Translation: AAB96813.1.
PIRS35464.
RefSeqNP_008305.1.

3D structure databases

HSSPHSSP built from PDB template 2OCC based on UniProtKB P00396.
SMRP34188. Positions 1-514.
ModBaseSearch...

Genome annotation databases

GeneID807987.

Phylogenomic databases

HOVERGENP34188.

Enzyme and pathway databases

BRENDA1.9.3.1. 300770.

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...

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Entry information

Entry nameCOX1_CROLA
AccessionPrimary (citable) accession number: P34188
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 16, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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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