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P29654 (COX1_SCAPL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 80. 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
OrganismScaphirhynchus platorynchus (Shovelnose sturgeon) (Acipenser platorynchus)
Taxonomic identifier7910 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiChondrosteiAcipenseriformesAcipenseridaeScaphirhynchus

Protein attributes

Sequence length157 AA.
Sequence statusFragment.
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

Chain‹1 – ›157›157Cytochrome c oxidase subunit 1
PRO_0000183413

Regions

Transmembrane9 – 2921Helical; Potential
Transmembrane34 – 5421Helical; Potential
Transmembrane76 – 9621Helical; Potential
Transmembrane104 – 12421Helical; Potential
Transmembrane137 – 15721Helical; Potential

Sites

Metal binding61Copper B Probable
Metal binding101Copper B Probable
Metal binding561Copper B Probable
Metal binding571Copper B Probable
Metal binding1421Iron (heme A3 axial ligand) Probable
Metal binding1441Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link6 ↔ 101'-histidyl-3'-tyrosine (His-Tyr) By similarity

Experimental info

Non-terminal residue11
Non-terminal residue1571

Sequences

Sequence LengthMass (Da)Tools
P29654 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 79C131B0721A6C1B

FASTA15717,424
        10         20         30         40         50         60 
FWFFGHPEVY ILILPGFGMI SHIVAYYAGK KEPFGYMGMV WAMMAIGLLG FIVWAHHMFT 

        70         80         90        100        110        120 
VGMDVDTRAY FTSATMIIAI PTGVKVFSWL ATLHGGSIKW DTPLLWALGF IFLFTVGGLT 

       130        140        150 
GIVLANSSLD IVLHDTYYVV AHFHYVLSMG AVFAIMG 

« Hide

References

[1]"Phylogenetic relationships of neopterygian fishes, inferred from mitochondrial DNA sequences."
Normark B.B., McCune A.R., Harrison R.G.
Mol. Biol. Evol. 8:819-834(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64919 Genomic DNA. Translation: AAB01481.1.

3D structure databases

ProteinModelPortalP29654.
SMRP29654. Positions 1-157.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_SCAPL
AccessionPrimary (citable) accession number: P29654
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: April 16, 2014
This is version 80 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