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P48887 (COX1_ALBCO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 82. 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:COI
Encoded onMitochondrion
OrganismAlbinaria coerulea (Land snail)
Taxonomic identifier42349 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaMolluscaGastropodaHeterobranchiaEuthyneuraPanpulmonataEupulmonataStylommatophoraSigmurethraClausilioideaClausiliidaeAlopiinaeAlbinaria

Protein attributes

Sequence length509 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 – 509509Cytochrome c oxidase subunit 1
PRO_0000183277

Regions

Transmembrane14 – 3421Helical; Potential
Transmembrane52 – 7221Helical; Potential
Transmembrane98 – 11821Helical; Potential
Transmembrane141 – 16121Helical; Potential
Transmembrane179 – 19921Helical; Potential
Transmembrane230 – 25021Helical; Potential
Transmembrane263 – 28321Helical; Potential
Transmembrane302 – 32221Helical; Potential
Transmembrane333 – 35321Helical; Potential
Transmembrane380 – 40021Helical; Potential
Transmembrane409 – 42921Helical; Potential
Transmembrane452 – 47221Helical; Potential

Sites

Metal binding571Iron (heme A axial ligand) Probable
Metal binding2361Copper B Probable
Metal binding2401Copper B Probable
Metal binding2851Copper B Probable
Metal binding2861Copper B Probable
Metal binding3711Iron (heme A3 axial ligand) Probable
Metal binding3731Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link236 ↔ 2401'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

Sequence LengthMass (Da)Tools
P48887 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 07236D1343151A6B

FASTA50957,034
        10         20         30         40         50         60 
MRWFYSTNHK DIGTLYMLFG IWCGMVGTGL SLLIRLELGT SGTLTDDHFY NVIVTAHAFV 

        70         80         90        100        110        120 
MIFFMVMPIM IGGFGNWMVP LLIGAPDMSF PRMNNMSFWL LPPAFILLIC SSMVEGGAGT 

       130        140        150        160        170        180 
GWTVYPPLSS SLAHSGASVD LAIFSLHLAG MSSILGAINF ITTIFNMRSP GMTMERVSLF 

       190        200        210        220        230        240 
VWSILVTVFL LLLSLPVLAG AITMLLTDRN FNTSFFDPAG GGDPILYQHL FWFFGHPEVY 

       250        260        270        280        290        300 
ILILPGFGMI SHILGNSAMK QPFGTLGMIY AMISIGILGF IVWAHHMFTV GMDVDTRAYF 

       310        320        330        340        350        360 
TAATMIIAIP TGIKVFSWLM TIYGSKVQYT ASMYWVLGFI FLFTLGGLTG IVLSNSSLDI 

       370        380        390        400        410        420 
MLHDTYYVVA HFHYVLSMGA VFAIFAGFNF WFPVMTGLIL HERLAKAQFV VMFIAVNMTF 

       430        440        450        460        470        480 
FPQHFLGLAG MPRRYSDYPD SYFMWNQLSS YGSLMSVFAV LLFVLIVWEA FLSQRSLLFV 

       490        500 
DATLYSREWS DGYFPPDFHS NIYQSYITI 

« Hide

References

[1]"Complete sequence and gene organization of the mitochondrial genome of the land snail Albinaria coerulea."
Hatzoglou E., Rodakis G.C., Lecanidou R.
Genetics 140:1353-1366(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X83390 Genomic DNA. Translation: CAA58307.1.
PIRS59154.
RefSeqNP_007340.1. NC_001761.1.

3D structure databases

ProteinModelPortalP48887.
SMRP48887. Positions 2-509.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID807999.

Organism-specific databases

CTD4512.

Phylogenomic databases

ProtClustDBMTH00223.

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_ALBCO
AccessionPrimary (citable) accession number: P48887
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 82 of the entry and version 1 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