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Q9ZZ64 (COX1_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
OrganismCanis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis ›

Protein attributes

Sequence length514 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 – 514514Cytochrome c oxidase subunit 1
PRO_0000183299

Regions

Topological domain1 – 1111Mitochondrial matrix By similarity
Transmembrane12 – 4029Helical; Name=I; By similarity
Topological domain41 – 5010Mitochondrial intermembrane By similarity
Transmembrane51 – 8636Helical; Name=II; By similarity
Topological domain87 – 948Mitochondrial matrix By similarity
Transmembrane95 – 11723Helical; Name=III; By similarity
Topological domain118 – 14023Mitochondrial intermembrane By similarity
Transmembrane141 – 17030Helical; Name=IV; By similarity
Topological domain171 – 18212Mitochondrial matrix By similarity
Transmembrane183 – 21230Helical; Name=V; By similarity
Topological domain213 – 22715Mitochondrial intermembrane By similarity
Transmembrane228 – 26134Helical; Name=VI; By similarity
Topological domain262 – 2698Mitochondrial matrix By similarity
Transmembrane270 – 28617Helical; Name=VII; By similarity
Topological domain287 – 29812Mitochondrial intermembrane By similarity
Transmembrane299 – 32729Helical; Name=VIII; By similarity
Topological domain328 – 3358Mitochondrial matrix By similarity
Transmembrane336 – 35722Helical; Name=IX; By similarity
Topological domain358 – 37013Mitochondrial intermembrane By similarity
Transmembrane371 – 40030Helical; Name=X; By similarity
Topological domain401 – 4066Mitochondrial matrix By similarity
Transmembrane407 – 43327Helical; Name=XI; By similarity
Topological domain434 – 44613Mitochondrial intermembrane By similarity
Transmembrane447 – 47832Helical; Name=XII; By similarity
Topological domain479 – 51436Mitochondrial matrix By similarity

Sites

Metal binding611Iron (heme A axial ligand) 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

Sequences

Sequence LengthMass (Da)Tools
Q9ZZ64 [UniParc].

Last modified August 14, 2001. Version 2.
Checksum: 44D2B3E8E04CBF6F

FASTA51457,039
        10         20         30         40         50         60 
MFINRWLFST NHKDIGTLYL LFGAWAGMVG TALSLLIRAE LGQPGTLLGD DQIYNVIVTA 

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

       130        140        150        160        170        180 
GAGTGWTVYP PLAGNLAHAG ASVDLTIFSL HLAGVSSILG AINFITTIIN MKPPAMSQYQ 

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

       250        260        270        280        290        300 
PEVYILILPG FGMISHIVTY YSGKKEPFGY MGMVWAMMSI GFLGFIVWAH HMFTVGMDVD 

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

       370        380        390        400        410        420 
SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM GGFAHWFPLF SGYTLNDTWA KIHFTIMFVG 

       430        440        450        460        470        480 
VNMTFFPQHF LGLSGMPRRY SDYPDAYTTW NTVSSMGSFI SLTAVMLMIF MIWEAFASKR 

       490        500        510 
EVAMVELTTT NIEWLHGCPP PYHTFEEPTY VIQK

« Hide

References

[1]"The complete nucleotide sequence of the domestic dog (Canis familiaris) mitochondrial genome."
Kim K.S., Lee S.E., Jeong H.W., Ha J.H.
Mol. Phylogenet. Evol. 10:210-220(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Kim K.S., Lee S.E., Jeong H.W., Jeong S.Y., Sohn H.S., Ha J.H.
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 240; 323 AND 479.
[3]"The complete mitochondrial DNA sequence of the Beagle dog (Canis familiaris)."
Zhu S., Xu Q., Chang H.
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U96639 Genomic DNA. Translation: AAD04765.2.
AY729880 Genomic DNA. Translation: AAU12151.1.
PIRT11495.
RefSeqNP_008473.4. NC_002008.4.

3D structure databases

ProteinModelPortalQ9ZZ64.
SMRQ9ZZ64. Positions 1-511.
ModBaseSearch...

Protein-protein interaction databases

STRING9615.ENSCAFP00000030311.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSCAFT00000034830; ENSCAFP00000030311; ENSCAFG00000022723.
GeneID804478.
KEGGcfa:804478.

Organism-specific databases

CTD4512.

Phylogenomic databases

eggNOGCOG0843.
GeneTreeENSGT00390000001518.
HOGENOMHOG000085274.
HOVERGENHBG003841.
InParanoidQ9ZZ64.
KOK02256.
OMAHYIVMGA.
OrthoDBEOG4BG8VW.
ProtClustDBMTH00103.

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...

Other

NextBio20934083.

Entry information

Entry nameCOX1_CANFA
AccessionPrimary (citable) accession number: Q9ZZ64
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 14, 2001
Last modified: April 3, 2013
This is version 95 of the entry and version 2 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents