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P24985 (COX1_CYPCA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. 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
OrganismCyprinus carpio (Common carp)
Taxonomic identifier7962 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeCyprinus

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_0000183320

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
Transmembrane412 – 43221Helical; 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
P24985 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: 1C937D0188EEA381

FASTA51656,863
        10         20         30         40         50         60 
MAITRWFFST NHKDIGTLYL VFGAWAGMVG TALSLLIRAE LSQPGSLLSD DQIYNVIVTA 

        70         80         90        100        110        120 
HAFVMIFFMV MPILIGGFGN WLVPLMIGAP DMAFPRMNNM SFWLLPPSFL LLLASSGVEA 

       130        140        150        160        170        180 
GAGTGWSVYP PLAGNLAHAG ASVDLTIFSL HLAGVSSILG AINFITTTIN MKPPAISQYQ 

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

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

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

       370        380        390        400        410        420 
SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM AAFVHWFPLL TGYTLHSTWT KIHFGVMFIG 

       430        440        450        460        470        480 
VNLTFFPQHF LGLSAMPRRY SDYPDAYALW NTVSSIGSLI SLVAVIMFLF ILWEAFAAKR 

       490        500        510 
EVLSVELTAT NVEWLHGCPP PYHTYEEPAF VQIQSN 

« Hide

References

[1]"The complete nucleotide sequence and gene organization of carp (Cyprinus carpio) mitochondrial genome."
Chang Y.S., Huang F.L., Lo T.B.
J. Mol. Evol. 38:138-155(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X61010 Genomic DNA. Translation: CAA43339.1.
PIRS36008.
RefSeqNP_007084.1. NC_001606.1.

3D structure databases

ProteinModelPortalP24985.
SMRP24985. Positions 3-514.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID807765.

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_CYPCA
AccessionPrimary (citable) accession number: P24985
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: April 16, 2014
This is version 88 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