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P05503 (COX1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. 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:Mtco1
Synonyms:Coi, mt-Co1
Encoded onMitochondrion
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length514 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

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.

Ontologies

Keywords
   Biological processElectron transport
Respiratory chain
Transport
   Cellular componentMembrane
Mitochondrion
Mitochondrion inner membrane
   DomainTransmembrane
Transmembrane helix
   LigandCopper
Heme
Iron
Metal-binding
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaerobic respiration

Inferred from electronic annotation. Source: InterPro

aging

Inferred from expression pattern PubMed 9701770. Source: RGD

cerebellum development

Inferred from expression pattern PubMed 2465379. Source: RGD

hydrogen ion transmembrane transport

Inferred from sequence or structural similarity. Source: GOC

oxidative phosphorylation

Inferred from electronic annotation. Source: UniProtKB-UniPathway

response to copper ion

Inferred from expression pattern PubMed 18567746. Source: RGD

response to electrical stimulus

Inferred from expression pattern PubMed 14519661. Source: RGD

response to oxidative stress

Inferred from direct assay PubMed 17870132. Source: RGD

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial inner membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 18567746. Source: RGD

respiratory chain complex IV

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functioncytochrome-c oxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

heme binding

Inferred from electronic annotation. Source: InterPro

iron ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 514514Cytochrome c oxidase subunit 1
PRO_0000183406

Regions

Transmembrane17 – 3721Helical; Potential
Transmembrane56 – 7621Helical; Potential
Transmembrane102 – 12221Helical; Potential
Transmembrane145 – 16521Helical; Potential
Transmembrane183 – 20321Helical; Potential
Transmembrane234 – 25421Helical; Potential
Transmembrane268 – 28821Helical; Potential
Transmembrane310 – 33021Helical; Potential
Transmembrane338 – 35821Helical; Potential
Transmembrane380 – 40021Helical; Potential
Transmembrane414 – 43421Helical; Potential
Transmembrane456 – 47621Helical; 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

Experimental info

Sequence conflict51R → G in AAD15016. Ref.2
Sequence conflict121H → P in AAD15016. Ref.2
Sequence conflict441P → L in AAD15016. Ref.2
Sequence conflict571I → L in AAD15016. Ref.2
Sequence conflict216 – 2183NTT → EFP in AAB21298. Ref.4
Sequence conflict2271D → G in AAD15016. Ref.2
Sequence conflict2491P → L in AAD15016. Ref.2
Sequence conflict2521G → E in AAD15016. Ref.2
Sequence conflict2761T → A in AAB21298. Ref.4
Sequence conflict3921G → C in AAD15016. Ref.2
Sequence conflict3921G → C in AAB21298. Ref.4
Sequence conflict4131H → L in AAD15016. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P05503 [UniParc].

Last modified October 1, 1989. Version 2.
Checksum: 20BCE1C7857ED6FD

FASTA51456,937
        10         20         30         40         50         60 
MFVNRWLFST NHKDIGTLYL LFGAWAGMVG TALSILIRAE LGQPGALLGD DQIYNVIVTA 

        70         80         90        100        110        120 
HAFVMIFFMV MPMMIGGFGN WLVPLMIGAP DMAFPRMNNM SFWLLPPSFL LLLASSMVEA 

       130        140        150        160        170        180 
GAGTGWTVYP PLAGNLAHAG VSVDLTIFSL HLAGVSSILG AINFITTIIN MKPPAMTQYQ 

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

       250        260        270        280        290        300 
PEVYILILPG FGIISHVVTY YSGKKEPFGY MGMVWTMMSI GFLGFIVWAH HMFTVGLDVD 

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

       370        380        390        400        410        420 
SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM AGFVHWFPLF SGYTLNDTWA KAHFAIMFVG 

       430        440        450        460        470        480 
VNMTFFPQHF LGLAGMPRRY SDYPDAYTTW NTVSSMGSFI SLTAVLVMIF MIWEAFASKR 

       490        500        510 
EVLSISYSST NLEWLHGCPP PYHTFEEPSY VKVK 

« Hide

References

[1]"The complete nucleotide sequence of the Rattus norvegicus mitochondrial genome: cryptic signals revealed by comparative analysis between vertebrates."
Gadaleta G., Pepe G., de Candia G., Quagliariello C., Sbisa E., Saccone C.
J. Mol. Evol. 28:497-516(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Wistar.
[2]"Analysis of a DNA segment from rat liver mitochondria containing the genes for the cytochrome oxidase subunits I, II, II, ATPase subunit 6, and several tRNA genes."
Grosskopf R., Feldmann H.
Curr. Genet. 4:151-158(1981)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Sprague-Dawley.
Tissue: Liver.
[3]"Tumor-associated mutations of rat mitochondrial transfer RNA genes."
Taira M., Yoshida E., Kobayashi M., Yaginuma K., Koike K.
Nucleic Acids Res. 11:1635-1643(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
[4]"Hormonal regulation of cytochrome oxidase subunit messenger RNAs in rat Sertoli cells."
Ku C.Y., Lu Q., Ussuf K.K., Weinstock G.M., Sanborn B.M.
Mol. Endocrinol. 5:1669-1676(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 216-514.
Tissue: Sertoli cell.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14848 Genomic DNA. Translation: CAA32956.1.
J01435 Genomic DNA. Translation: AAD15016.1.
V00676 Genomic DNA. Translation: CAA24046.1.
V00678 Genomic DNA. Translation: CAA24050.1.
S79304 mRNA. Translation: AAB21298.2.
PIRS04749.
RefSeqAP_004894.1. AC_000022.2.

3D structure databases

ProteinModelPortalP05503.
SMRP05503. Positions 1-514.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbP05503.
PRIDEP05503.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

RGD621871. mt-Co1.

Phylogenomic databases

eggNOGCOG0843.
HOGENOMHOG000085274.
HOVERGENHBG003841.
InParanoidP05503.
PhylomeDBP05503.

Enzyme and pathway databases

UniPathwayUPA00705.

Gene expression databases

GenevestigatorP05503.

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...

Other

NextBio35584672.
PROP05503.

Entry information

Entry nameCOX1_RAT
AccessionPrimary (citable) accession number: P05503
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 1, 1989
Last modified: July 9, 2014
This is version 118 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