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P24984 (COX1_COTJA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
OrganismCoturnix coturnix japonica (Japanese quail) (Coturnix japonica)
Taxonomic identifier93934 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Perdicinae › Coturnix

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_0000183316

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

Experimental info

Sequence conflict4741W → L in AAA76729. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P24984 [UniParc].

Last modified September 26, 2003. Version 3.
Checksum: 34779829B535B2B6

FASTA51656,985
        10         20         30         40         50         60 
MTFINRWLFS TNHKDIGTLY LIFGTWAGMA GTALSLLIRA ELGQPGTLLG DDQIYNVIVT 

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

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

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

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

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

       370        380        390        400        410        420 
NSSLDIALHD TYYVVAHFHY VLSMGAVFAI LAGFTHWFPL FTGFTLHPTW TKAHFGVMFT 

       430        440        450        460        470        480 
GVNLTFFPQH FLGLAGMPRR YSDYPDAYTL WNTLSSIGSL ISMTAVIMLM FIVWEAFSAK 

       490        500        510 
RKVLQPELTA TNIEWIHGCP PPYHTFEEPA FVQVQE

« Hide

References

[1]"Complete sequence of the Japanese quail (Coturnix japonica) mitochondrial genome and its genetic relationship with related species."
Nishibori M., Hayashi T., Tsudzuki M., Yamamoto Y., Yasue H.
Anim. Genet. 32:380-385(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Blood.
[2]"Nucleotide sequence and evolution of coding and noncoding regions of a quail mitochondrial genome."
Desjardins P., Morais R.
J. Mol. Evol. 32:153-161(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-102.
Tissue: Liver.
[3]"Nucleotide sequence of mitochondrial genes for COI, tRNAs Lys, Asp, Ser (UCN), COII and ATPases 8 and 6 of the quail Coturnix japonica."
Ramirez V., Morais R.
Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 463-516.
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP003195 Genomic DNA. Translation: BAB62917.1.
X57246 Genomic DNA. Translation: CAA40524.1.
U36794 Genomic DNA. Translation: AAA76729.1.
PIRS25424.
RefSeqNP_572016.1. NC_003408.1.

3D structure databases

ProteinModelPortalP24984.
SMRP24984. Positions 3-515.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID804670.

Organism-specific databases

CTD4512.

Phylogenomic databases

HOVERGENHBG003841.
ProtClustDBMTH00116.

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. COX1. 1 hit.
PROSITEPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX1_COTJA
AccessionPrimary (citable) accession number: P24984
Secondary accession number(s): Q8SEX1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: September 26, 2003
Last modified: April 3, 2013
This is version 87 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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