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O21399 (COX1_STRCA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 90. 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
OrganismStruthio camelus (Ostrich)
Taxonomic identifier8801 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesPalaeognathaeStruthioniformesStruthionidaeStruthio

Protein attributes

Sequence length516 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 – 516516Cytochrome c oxidase subunit 1
PRO_0000183422

Regions

Transmembrane18 – 3821Helical; Potential
Transmembrane57 – 7721Helical; Potential
Transmembrane103 – 12321Helical; Potential
Transmembrane146 – 16621Helical; Potential
Transmembrane184 – 20421Helical; Potential
Transmembrane235 – 25521Helical; Potential
Transmembrane269 – 28921Helical; Potential
Transmembrane311 – 33121Helical; Potential
Transmembrane339 – 35921Helical; Potential
Transmembrane381 – 40121Helical; Potential
Transmembrane415 – 43521Helical; Potential
Transmembrane457 – 47721Helical; Potential

Sites

Metal binding621Iron (heme A axial ligand) Probable
Metal binding2411Copper B Probable
Metal binding2451Copper B Probable
Metal binding2911Copper B Probable
Metal binding2921Copper B Probable
Metal binding3771Iron (heme A3 axial ligand) Probable
Metal binding3791Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link241 ↔ 2451'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

Sequence LengthMass (Da)Tools
O21399 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: 33FFEC4806D80856

FASTA51656,932
        10         20         30         40         50         60 
MTFITRWLFS TNHKDIGTLY LIFGAWAGMV GTALSLLIRA ELGQPGTLLG DDQIYNVIVT 

        70         80         90        100        110        120 
AHAFVMIFFM VMPVMIGGFG NWLVPLMIGA PDMAFPRMNN MSFWLLPPSF LLLLASSTVE 

       130        140        150        160        170        180 
AGAGTGWTVY PPLAGNLAHA GASVDLAIFS LHLAGVSSIL GAINFITTAI NMKPPALSQY 

       190        200        210        220        230        240 
QTPLFVWSVL ITAILLLLSL PVLAAGITML LTDRNLNTTF FDPAGGGDPV LYQHLFWFFG 

       250        260        270        280        290        300 
HPEVYILILP GFGIISHVVT YYAGKKEPFG YMGMVWAMLS IGFLGFIVWA HHMFTVGMDV 

       310        320        330        340        350        360 
DTRAYFTSAT MIIAIPTGIK VFSWLATLHG GTIKWDPPIL WALGFIFLFT IGGLTGIVLA 

       370        380        390        400        410        420 
NSSLDIALHD TYYVVAHFHY VLSMGAVFAI LAGFTHWFPL FTGYTLHPTW AKAHFGVMFT 

       430        440        450        460        470        480 
GVNLTFFPQH FLGLAGMPRR YSDYPDAYTL WNTMSSIGSL ISMTAVIMLM FIIWEAFSSK 

       490        500        510 
RKVLQPELIA TNIEWIHGCP PPHHTFEEPA FVQVQE 

« Hide

References

[1]"The mtDNA sequence of the ostrich and the divergence between paleognathous and neognathous birds."
Harlid A., Janke A., Arnason U.
Mol. Biol. Evol. 14:754-761(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Harlid A.
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Primers for a PCR-based approach to complete mitochondrial genome sequencing."
Sorenson M.D., Dimcheff D.E., Ast J.C., Yuri T., Mindell D.P.
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Complete mitochondrial DNA genome sequences of extinct birds: ratite phylogenetics and the vicariance biogeography hypothesis."
Haddrath O., Baker A.J.
Proc. R. Soc. B 268:939-945(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Phylogenetic relationships of the ratite birds: resolving conflicts between molecular and morphological data sets."
Lee K., Feinstein J., Cracraft J.
(In) Mindell D.P. (eds.); Avian molecular evolution and systematics, pp.1-1, Academic Press, New York (1997)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-337.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y12025 Genomic DNA. Translation: CAA72746.1.
AF069429 Genomic DNA. Translation: AAD09385.1.
AF338715 Genomic DNA. Translation: AAK53347.1.
U76062 Genomic DNA. Translation: AAB61328.1.
PIRC90612.
T12411.
RefSeqNP_115443.1. NC_002785.1.

3D structure databases

ProteinModelPortalO21399.
SMRO21399. Positions 3-515.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID803279.

Organism-specific databases

CTD4512.

Phylogenomic databases

HOVERGENHBG003841.

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_STRCA
AccessionPrimary (citable) accession number: O21399
Secondary accession number(s): O03549
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: December 15, 1998
Last modified: July 9, 2014
This is version 90 of the entry and version 2 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