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Q9ZZ52 (COX1_SQUAC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 84. 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
OrganismSqualus acanthias (Spiny dogfish)
Taxonomic identifier7797 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataChondrichthyesElasmobranchiiSqualimorphiiSqualiformesSqualidaeSqualus

Protein attributes

Sequence length518 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 – 518518Cytochrome c oxidase subunit 1
PRO_0000183421

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

Sequences

Sequence LengthMass (Da)Tools
Q9ZZ52 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 4D90C32D7739ECF5

FASTA51857,267
        10         20         30         40         50         60 
MAINRWFFST NHKDIGTLYL IFGAWAGMVG TALSLLIRAE LSQPGTLLGD DQIYNVIVTA 

        70         80         90        100        110        120 
HAFVMIFFMV MPVMIGGFGN WLVPLMIGAP DMAFPRMNNM SFWLLPPSLL LLLASAGVEA 

       130        140        150        160        170        180 
GAGTGWTVYP PLAGNMAHAG ASVDLAIFSL HLAGISSILA SINFITTIIN MKPPAISQYQ 

       190        200        210        220        230        240 
TPLFVWSILV TTILLLLSLP VLAAAITMLL TDRNLNTTFF DPAGGGDPIL YQHLFWFFGH 

       250        260        270        280        290        300 
PEVYILILPG FGMISHVVAY YSGKKEPFGY MGMVWAMMAI GLLGFIVWAH HMFTVGMDVD 

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

       370        380        390        400        410        420 
SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM AGFIHWFPLF SGYTLHSTWT KTQFLVMFIG 

       430        440        450        460        470        480 
VNLTFFPQHF LGLAGMPRRY SDYPDAYALW NTVSSIGSLI SLVAVIMFLF IIWEAFAPSG 

       490        500        510 
KVLSVELPHT NVEWLHGCPP PYHTYEEPAF VQVQRTYF 

« Hide

References

[1]"Phylogenetic studies of complete mitochondrial DNA molecules place cartilaginous fishes within the tree of bony fishes."
Rasmussen A.S., Arnason U.
J. Mol. Evol. 48:118-123(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y18134 Genomic DNA. Translation: CAA77051.1.
PIRT11536.
RefSeqNP_008525.1. NC_002012.1.

3D structure databases

ProteinModelPortalQ9ZZ52.
SMRQ9ZZ52. Positions 3-514.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID808385.

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_SQUAC
AccessionPrimary (citable) accession number: Q9ZZ52
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: May 14, 2014
This is version 84 of the entry and version 1 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