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Q36097 (COX1_THEPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 78. 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
OrganismTheileria parva (East coast fever infection agent) [Reference proteome]
Taxonomic identifier5875 [NCBI]
Taxonomic lineageEukaryotaAlveolataApicomplexaAconoidasidaPiroplasmidaTheileriidaeTheileria

Protein attributes

Sequence length481 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 By similarity.

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 caution

The sequence CAA80798.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 481481Cytochrome c oxidase subunit 1
PRO_0000232688

Regions

Transmembrane22 – 4221Helical; Potential
Transmembrane64 – 8421Helical; Potential
Transmembrane109 – 12921Helical; Potential
Transmembrane151 – 17121Helical; Potential
Transmembrane194 – 21421Helical; Potential
Transmembrane240 – 26021Helical; Potential
Transmembrane278 – 29821Helical; Potential
Transmembrane309 – 32921Helical; Potential
Transmembrane343 – 36321Helical; Potential
Transmembrane382 – 40221Helical; Potential
Transmembrane420 – 44021Helical; Potential
Transmembrane459 – 47921Helical; Potential

Sites

Metal binding691Iron (heme A axial ligand) By similarity
Metal binding2461Copper B By similarity
Metal binding2501Copper B By similarity
Metal binding3821Iron (heme A3 axial ligand) By similarity
Metal binding3841Iron (heme A axial ligand) By similarity

Amino acid modifications

Cross-link246 ↔ 2501'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q36097 [UniParc].

Last modified May 2, 2006. Version 3.
Checksum: AE044B09BFB9FC86

FASTA48153,792
        10         20         30         40         50         60 
MKFEGLFLVF NSVSGNHKII GISYLWLAYW FGMIGFYMSV LIRTELSMSG LKIITMDTLE 

        70         80         90        100        110        120 
IYNLLFTLHG LIMVFFNIMT GLFGGIGNYL YPVLLGYCDV VYPRVNLYSL LFQPIGFVLV 

       130        140        150        160        170        180 
VSSIYLEIGS GTGWTLYPPL STSLSNVGID FIIFGLLAAG IASTLSSVNF ITTFTSVKTI 

       190        200        210        220        230        240 
GFVIDRISPA AWSIVLTSFL LLLSLPVVTA VFLMVFLDRH YNTMFFESSN SGDPVLYQHL 

       250        260        270        280        290        300 
FWFFGHPEVY IMILPGFGII SLLLSTYTTK EMFGNQTMIL AMGFNSFVRL FGLGTSYVHI 

       310        320        330        340        350        360 
RFGSRYSRYF TTVTILIALP TGNKIFNWVT TLQCVESIKS LGLVLFTVLF IVNFVIGGTT 

       370        380        390        400        410        420 
GVVLGNAGID LALHDTVYVV GHFHFVLSIG AIISMICFII YIQRMLLFGI ILSNRLSSLI 

       430        440        450        460        470        480 
APIFMISVLL TFLPMHFTGF SPLPRRIPDY PDEMWGWNFI CTLGATMMLV LKLAILFIIS 


L 

« Hide

References

[1]"A 7.1 kb linear DNA molecule of Theileria parva has scrambled rDNA sequences and open reading frames for mitochondrially-encoded proteins."
Kairo A., Fairlamb A., Gobright E., Nene V.
EMBO J. 13:898-905(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Muguga.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z23263 Genomic DNA. Translation: CAA80798.1. Different initiation.
PIRS41689.
RefSeqYP_001994285.1. NC_011005.1.

3D structure databases

ProteinModelPortalQ36097.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6741532.

Enzyme and pathway databases

UniPathwayUPA00705.

Family and domain databases

Gene3D1.20.210.10. 1 hit.
InterProIPR000883. Cyt_c_Oxase_su1.
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.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX1_THEPA
AccessionPrimary (citable) accession number: Q36097
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: May 2, 2006
Last modified: May 14, 2014
This is version 78 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways