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Protein

Cytochrome c oxidase subunit 1

Gene

COI

Organism
Albinaria turrita (Door snail) (Clausilia turrita)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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 activityi

4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O.

Pathway:ioxidative phosphorylation

This protein is involved in the pathway oxidative phosphorylation, which is part of Energy metabolism.
View all proteins of this organism that are known to be involved in the pathway oxidative phosphorylation and in Energy metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi42 – 421Iron (heme A axial ligand)Curated
Metal bindingi50 – 501Copper BCurated

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Keywords - Ligandi

Copper, Heme, Iron, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00705.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome c oxidase subunit 1 (EC:1.9.3.1)
Alternative name(s):
Cytochrome c oxidase polypeptide I
Gene namesi
Name:COI
Encoded oniMitochondrion
OrganismiAlbinaria turrita (Door snail) (Clausilia turrita)
Taxonomic identifieri27820 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaHeterobranchiaEuthyneuraPanpulmonataEupulmonataStylommatophoraSigmurethraClausilioideaClausiliidaeAlopiinaeAlbinaria

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei12 – 3221HelicalSequence AnalysisAdd
BLAST
Transmembranei59 – 7921HelicalSequence AnalysisAdd
BLAST
Transmembranei88 – 10821HelicalSequence AnalysisAdd
BLAST
Transmembranei131 – 15121HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 195›195Cytochrome c oxidase subunit 1PRO_0000183278Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ09333.
SMRiQ09333. Positions 1-188.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di1.20.210.10. 1 hit.
InterProiIPR000883. COX1.
IPR023616. Cyt_c_Oxase_su1_dom.
[Graphical view]
PANTHERiPTHR10422. PTHR10422. 1 hit.
PfamiPF00115. COX1. 1 hit.
[Graphical view]
PRINTSiPR01165. CYCOXIDASEI.
SUPFAMiSSF81442. SSF81442. 1 hit.
PROSITEiPS50855. COX1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Q09333-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
IYGSKVQYTA SMYWVLGFIF LFTLGGLTGI VLSNSSLDIM LHDTYYVVAH
60 70 80 90 100
FHYVLSMGAV FAIFAGFNFW FPVMTGLVLH ERLAKAQFIV MFIAVNMTFF
110 120 130 140 150
PQHFLGLAGM PRRYSDYPDS YFMWNQLSSY GSLMSVFAVL LFVLIVWEAF
160 170 180 190
LSQRSLLFVD ATLYSREWSD GYFPPDFHSN IYQSYITIYK TYYSK
Length:195
Mass (Da):22,648
Last modified:November 1, 1995 - v1
Checksum:i863E2B82623E7060
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X71393 Genomic DNA. Translation: CAA50515.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X71393 Genomic DNA. Translation: CAA50515.1.

3D structure databases

ProteinModelPortaliQ09333.
SMRiQ09333. Positions 1-188.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00705.

Family and domain databases

Gene3Di1.20.210.10. 1 hit.
InterProiIPR000883. COX1.
IPR023616. Cyt_c_Oxase_su1_dom.
[Graphical view]
PANTHERiPTHR10422. PTHR10422. 1 hit.
PfamiPF00115. COX1. 1 hit.
[Graphical view]
PRINTSiPR01165. CYCOXIDASEI.
SUPFAMiSSF81442. SSF81442. 1 hit.
PROSITEiPS50855. COX1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Novel features of metazoan mtDNA revealed from sequence analysis of three mitochondrial DNA segments of the land snail Albinaria turrita (Gastropoda: Clausiliidae)."
    Lecanidou R., Douris V., Rodakis G.C.
    J. Mol. Evol. 38:369-382(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiCOX1_ALBTU
AccessioniPrimary (citable) accession number: Q09333
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: January 7, 2015
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.