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Protein

Cytochrome c oxidase subunit 2

Gene

MT-CO2

Organism
Tinamus major (Great tinamou) (Tetrao major)
Status
Reviewed-Annotation score: Annotation score: 4 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 bindingi128 – 1281Copper ACurated
Metal bindingi163 – 1631Copper ACurated
Metal bindingi167 – 1671Copper ACurated
Metal bindingi171 – 1711Copper ACurated

GO - Molecular functioni

  1. copper ion binding Source: InterPro
  2. cytochrome-c oxidase activity Source: UniProtKB-EC

GO - Biological processi

  1. electron transport chain Source: InterPro
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:MT-CO2
Synonyms:COII, COXII, MTCO2
Encoded oniMitochondrion
OrganismiTinamus major (Great tinamou) (Tetrao major)
Taxonomic identifieri30468 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesPalaeognathaeTinamiformesTinamidaeTinamus

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei‹1 – 15›15HelicalSequence AnalysisAdd
BLAST
Topological domaini16 – 2914Mitochondrial matrixSequence AnalysisAdd
BLAST
Transmembranei30 – 4920HelicalSequence AnalysisAdd
BLAST
Topological domaini50 – 198149Mitochondrial intermembraneSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. mitochondrial inner membrane Source: UniProtKB-SubCell
  3. respiratory chain complex IV Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 198›198Cytochrome c oxidase subunit 2PRO_0000183704Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliO03895.
SMRiO03895. Positions 2-191.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG012727.

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: Fragment.

O03895-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
AICSLVLYLL TLMLMEKLSS NTVDAQEVEL IWTILPAIVL ILLALPSLQI
60 70 80 90 100
LYMMDEIDEP DLTLKAIGHQ WYWSYEYTDF KDLSFDSYMI PTPDLPTGYF
110 120 130 140 150
RLLEVDNRVV IPMESPIRMI ITAADVLHSW AVPTLGVKTD AIPGRLNQTS
160 170 180 190
FITTRPGIFY GQCSEICGAN HSFMPIVVES TPLPHFESWS SLLSTSSL
Length:198
Mass (Da):22,305
Last modified:July 1, 1997 - v1
Checksum:iE655564EED39BA89
GO

Experimental Info

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U76070 Genomic DNA. Translation: AAB61332.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U76070 Genomic DNA. Translation: AAB61332.1.

3D structure databases

ProteinModelPortaliO03895.
SMRiO03895. Positions 2-191.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG012727.

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. "Phylogenetic relationships of the ratite birds: resolving conflicts between molecular and morphological data sets."
    Lee K., Feinstein J., Cracraft J.
    (In) Mindell D.P. (eds.); Avian molecular evolution and systematics, pp.1-1, Academic Press, New York (1997)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiCOX2_TINMA
AccessioniPrimary (citable) accession number: O03895
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: February 4, 2015
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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.