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Protein

Cytochrome c oxidase subunit 2

Gene

COII

Organism
Adalia bipunctata (Two-spotted ladybird beetle) (Coccinella bipunctata)
Status
Reviewed-Annotation score: -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. Subunit 2 transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit 1.

Catalytic activityi

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

Cofactori

Cu cationNote: Binds a copper A center.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi161Copper ACurated1
Metal bindingi196Copper ACurated1
Metal bindingi200Copper ACurated1
Metal bindingi204Copper ACurated1

GO - Molecular functioni

Keywordsi

Molecular functionOxidoreductase
Biological processElectron transport, Respiratory chain, Transport
LigandCopper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome c oxidase subunit 2 (EC:1.9.3.1)
Alternative name(s):
Cytochrome c oxidase polypeptide II
Gene namesi
Name:COII
Encoded oniMitochondrion
OrganismiAdalia bipunctata (Two-spotted ladybird beetle) (Coccinella bipunctata)
Taxonomic identifieri7084 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaColeopteraPolyphagaCucujiformiaCoccinellidaeCoccinellinaeCoccinelliniAdalia

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 26Mitochondrial intermembraneSequence analysisAdd BLAST26
Transmembranei27 – 48HelicalSequence analysisAdd BLAST22
Topological domaini49 – 62Mitochondrial matrixSequence analysisAdd BLAST14
Transmembranei63 – 82HelicalSequence analysisAdd BLAST20
Topological domaini83 – 228Mitochondrial intermembraneSequence analysisAdd BLAST146

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001834851 – 228Cytochrome c oxidase subunit 2Add BLAST228

Structurei

3D structure databases

ProteinModelPortaliP29871
SMRiP29871
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

CDDicd13912 CcO_II_C, 1 hit
Gene3Di1.10.287.90, 1 hit
2.60.40.420, 1 hit
InterProiView protein in InterPro
IPR002429 CcO_II-like_C
IPR034210 CcO_II_C
IPR001505 Copper_CuA
IPR008972 Cupredoxin
IPR011759 Cyt_c_oxidase_su2_TM_dom
IPR036257 Cyt_c_oxidase_su2_TM_sf
PfamiView protein in Pfam
PF00116 COX2, 1 hit
PF02790 COX2_TM, 1 hit
SUPFAMiSSF49503 SSF49503, 1 hit
SSF81464 SSF81464, 1 hit
PROSITEiView protein in PROSITE
PS00078 COX2, 1 hit
PS50857 COX2_CUA, 1 hit
PS50999 COX2_TM, 1 hit

Sequencei

Sequence statusi: Complete.

P29871-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTWKSSLFL DSSSFLLEQL RFFHDHALLI LNMITGAVAY IMISLLFNKY
60 70 80 90 100
NHRFLLEGHT VETIWTILPA FTLIFIALPS LKLIYLIDEI RNPLVTLKTI
110 120 130 140 150
GHQWYWTYEY SDFKKLEFDS YMLSYDNLNP FNFRLLEVDN RTILPYLSNI
160 170 180 190 200
RLLTSSADVI HSWTIPSSGV KIDASPGRLN QMSFTLNRTG IFYGQCSEIC
210 220
GANHSFMPIS IESISPSNFI KWVNKSSL
Length:228
Mass (Da):26,370
Last modified:November 1, 1995 - v2
Checksum:iA040F20E8AECABA9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M83965 Genomic DNA Translation: AAA31616.2
PIRiE45170

Similar proteinsi

Entry informationi

Entry nameiCOX2_ADABI
AccessioniPrimary (citable) accession number: P29871
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 1, 1995
Last modified: March 28, 2018
This is version 103 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health