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P24881 (COX1_ASCSU) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 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
Encoded onMitochondrion
OrganismAscaris suum (Pig roundworm) (Ascaris lumbricoides)
Taxonomic identifier6253 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaAscarididaAscaridoideaAscarididaeAscaris

Protein attributes

Sequence length525 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 – 525525Cytochrome c oxidase subunit 1
PRO_0000183288

Regions

Transmembrane25 – 4521Helical; Potential
Transmembrane71 – 9121Helical; Potential
Transmembrane108 – 12821Helical; Potential
Transmembrane152 – 17221Helical; Potential
Transmembrane190 – 21021Helical; Potential
Transmembrane241 – 26121Helical; Potential
Transmembrane274 – 29421Helical; Potential
Transmembrane317 – 33721Helical; Potential
Transmembrane344 – 36421Helical; Potential
Transmembrane387 – 40721Helical; Potential
Transmembrane420 – 44021Helical; Potential
Transmembrane459 – 47921Helical; Potential

Sites

Metal binding691Iron (heme A axial ligand) Probable
Metal binding2471Copper B Probable
Metal binding2511Copper B Probable
Metal binding2971Copper B Probable
Metal binding2981Copper B Probable
Metal binding3831Iron (heme A3 axial ligand) Probable
Metal binding3851Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link247 ↔ 2511'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

Sequence LengthMass (Da)Tools
P24881 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: 2EFB6A50522F7FBE

FASTA52558,529
        10         20         30         40         50         60 
MSGFYKYQGG LSVWLESSNH KDIGTLYFLF GLWSGMVGTS LSLVIRLELA KPGLLLGSGQ 

        70         80         90        100        110        120 
LYNSVITAHA ILMIFFMVMP TMIGGFGNWM LPLMLGAPDM SFPRLNNLSF WLLPTAMFLI 

       130        140        150        160        170        180 
LDACFVDMGC GTSWTVYPPL STMGHPGGSV DLAIFSLHCA GVSSILGAIN FMTTTKNLRS 

       190        200        210        220        230        240 
SSISLEHMSL FVWTVFVTVF LLVLSLPVLA GAITMLLTDR NLNTSFFDPS TGGNPLIYQH 

       250        260        270        280        290        300 
LFWFFGHPEV YILILPAFGI ISQSSLYLTG KKEVFGSLGM VYAILSIGLI GCVVWAHHMY 

       310        320        330        340        350        360 
TVGMDLDSRA YFTAATMVIA VPTGVKVFSW LATLFGMKMV FQPLLLWVMG FIFLFTIGGL 

       370        380        390        400        410        420 
TGVMLSNSSL DIILHDTYYV VSHFHYVLSL GAVFGIFTGV TLWWSFITGF VYDKMMMSSV 

       430        440        450        460        470        480 
FVLMFVGVNL TFFPLHFAGI HGYPRKYLDY PDVYSVWNIM ASYGSMISVF ALFLFIYVLL 

       490        500        510        520 
ESFVGHRIFL FDYYVNSGPE YSLSGYVFGH SYQSEIFYSS IVFKF 

« Hide

References

[1]"The mitochondrial genomes of two nematodes, Caenorhabditis elegans and Ascaris suum."
Okimoto R., Macfarlane J.L., Clary D.O., Wolstenholme D.R.
Genetics 130:471-498(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Body wall muscle and Egg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X54253 Genomic DNA. Translation: CAA38171.1.
PIRS26022.
RefSeqNP_006949.1. NC_001327.1.

3D structure databases

ProteinModelPortalP24881.
SMRP24881. Positions 12-512.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID807671.

Organism-specific databases

CTD4512.

Phylogenomic databases

ProtClustDBMTH00079.

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_ASCSU
AccessionPrimary (citable) accession number: P24881
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: November 1, 1995
Last modified: March 19, 2014
This is version 85 of the entry and version 2 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