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Protein

Cytochrome c oxidase subunit 2

Gene

COII

Organism
Choristoneura rosaceana (Oblique banded leafroller)
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. 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi161 – 1611Copper ACurated
Metal bindingi196 – 1961Copper ACurated
Metal bindingi200 – 2001Copper ACurated
Metal bindingi204 – 2041Copper ACurated

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Keywords - Ligandi

Copper, 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
OrganismiChoristoneura rosaceana (Oblique banded leafroller)
Taxonomic identifieri27543 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaTortricoideaTortricidaeTortricinaeChoristoneura

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2626Mitochondrial intermembraneSequence AnalysisAdd
BLAST
Transmembranei27 – 5125HelicalSequence AnalysisAdd
BLAST
Topological domaini52 – 6211Mitochondrial matrixSequence AnalysisAdd
BLAST
Transmembranei63 – 8119HelicalSequence AnalysisAdd
BLAST
Topological domaini82 – 227146Mitochondrial intermembraneSequence 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
Chaini1 – 227227Cytochrome c oxidase subunit 2PRO_0000183553Add
BLAST

Proteomic databases

PRIDEiP98030.

Structurei

3D structure databases

ProteinModelPortaliP98030.
SMRiP98030. Positions 1-225.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di1.10.287.90. 1 hit.
2.60.40.420. 1 hit.
InterProiIPR001505. Copper_CuA.
IPR008972. Cupredoxin.
IPR014222. Cyt_c_oxidase_su2.
IPR002429. Cyt_c_oxidase_su2_C.
IPR011759. Cyt_c_oxidase_su2_TM_dom.
[Graphical view]
PfamiPF00116. COX2. 1 hit.
PF02790. COX2_TM. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 1 hit.
SSF81464. SSF81464. 1 hit.
TIGRFAMsiTIGR02866. CoxB. 1 hit.
PROSITEiPS00078. COX2. 1 hit.
PS50857. COX2_CUA. 1 hit.
PS50999. COX2_TM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P98030-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATWSNFNLQ NSASPLMEQI IFFHDHTLVI LIMITILVGY LMISLFFNSY
60 70 80 90 100
INRFLLEGQM IELIWTILPA ITLIFIALPS LRLLYLLDEL NNPLITLKSI
110 120 130 140 150
GHQWYWSYEY SDFKNIQFDS YMIPINEMKN DNFRLLDVDN RIVLPMNNQI
160 170 180 190 200
RILVTATDVI HSWTIPSLGV KVDANPGRLN QTNFFINRPG IFYGQCSEIC
210 220
GANHSFMPIV IESISIKNFI NWINNYS
Length:227
Mass (Da):26,435
Last modified:October 1, 1996 - v1
Checksum:i3C3D62BE1DF41B24
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19099 Genomic DNA. Translation: AAA53649.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19099 Genomic DNA. Translation: AAA53649.1.

3D structure databases

ProteinModelPortaliP98030.
SMRiP98030. Positions 1-225.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP98030.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di1.10.287.90. 1 hit.
2.60.40.420. 1 hit.
InterProiIPR001505. Copper_CuA.
IPR008972. Cupredoxin.
IPR014222. Cyt_c_oxidase_su2.
IPR002429. Cyt_c_oxidase_su2_C.
IPR011759. Cyt_c_oxidase_su2_TM_dom.
[Graphical view]
PfamiPF00116. COX2. 1 hit.
PF02790. COX2_TM. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 1 hit.
SSF81464. SSF81464. 1 hit.
TIGRFAMsiTIGR02866. CoxB. 1 hit.
PROSITEiPS00078. COX2. 1 hit.
PS50857. COX2_CUA. 1 hit.
PS50999. COX2_TM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Mitochondrial DNA sequence variation in the spruce budworm species complex (Choristoneura: Lepidoptera)."
    Sperling F.A.H., Hickey D.A.
    Mol. Biol. Evol. 11:656-665(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 205.

Entry informationi

Entry nameiCOX2_CHORO
AccessioniPrimary (citable) accession number: P98030
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 7, 2015
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. 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.