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Protein

Cytochrome c oxidase subunit 2

Gene
N/A
Organism
Leishmania tarentolae (Sauroleishmania tarentolae)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

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 bindingi157 – 1571Copper ACurated
Metal bindingi192 – 1921Copper ACurated
Metal bindingi196 – 1961Copper ACurated
Metal bindingi200 – 2001Copper ACurated

GO - Molecular functioni

  1. copper ion binding Source: InterPro
  2. cytochrome-c oxidase activity Source: UniProtKB-EC
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
Encoded oniMitochondrion
OrganismiLeishmania tarentolae (Sauroleishmania tarentolae)
Taxonomic identifieri5689 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmanializard Leishmania

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2020Mitochondrial intermembraneSequence AnalysisAdd
BLAST
Transmembranei21 – 4222HelicalSequence AnalysisAdd
BLAST
Topological domaini43 – 6018Mitochondrial matrixSequence AnalysisAdd
BLAST
Transmembranei61 – 8626HelicalSequence AnalysisAdd
BLAST
Topological domaini87 – 210124Mitochondrial intermembraneSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 210210Cytochrome c oxidase subunit 2PRO_0000183616Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP14545.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di2.60.40.420. 1 hit.
InterProiIPR001505. Copper_CuA.
IPR008972. Cupredoxin.
IPR002429. Cyt_c_oxidase_su2_C.
[Graphical view]
PfamiPF00116. COX2. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 1 hit.
PROSITEiPS00078. COX2. 1 hit.
PS50857. COX2_CUA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P14545-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFILSFWMI FLLDSVIVLL SFVCFVCVWI CALLFSTVLL VSKLNNIYCT
60 70 80 90 100
WDFTASKFID VYWFTIGGMF SLGLLLRLCL LLYFGHLNFV SFDLCKVVGF
110 120 130 140 150
QWYWVYFIFG ETTIFSNLIL ESDYMIGDLR LLQCNHVLTL LSLVIYKLWL
160 170 180 190 200
SAVDVIHSFA ISSLGVKVDC IPGRCNEIVL FSSNNATVYG QCSELCGVLH
210
GFMPIVICFI
Length:210
Mass (Da):23,977
Last modified:October 1, 1996 - v2
Checksum:iB3A0544E258047C2
GO

RNA editingi

Some positions are modified by RNA editing via nucleotide insertion.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07544 mRNA. Translation: AAA31876.1.
M10126 Genomic DNA. No translation available.
PIRiI22848.

Keywords - Coding sequence diversityi

RNA editing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07544 mRNA. Translation: AAA31876.1.
M10126 Genomic DNA. No translation available.
PIRiI22848.

3D structure databases

ProteinModelPortaliP14545.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.60.40.420. 1 hit.
InterProiIPR001505. Copper_CuA.
IPR008972. Cupredoxin.
IPR002429. Cyt_c_oxidase_su2_C.
[Graphical view]
PfamiPF00116. COX2. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 1 hit.
PROSITEiPS00078. COX2. 1 hit.
PS50857. COX2_CUA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Sequences of six genes and several open reading frames in the kinetoplast maxicircle DNA of Leishmania tarentolae."
    de la Cruz V.F., Neckelmann N., Simpson L.
    J. Biol. Chem. 259:15136-15147(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Mapping and 5' end determination of kinetoplast maxicircle gene transcripts from Leishmania tarentolae."
    Simpson A.M., Necklemann N., la Cruz V.F., Muhich M.L., Simpson L.
    Nucleic Acids Res. 13:5977-5993(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Internal frameshifts within the mitochondrial genes for cytochrome oxidase subunit II and maxicircle unidentified reading frame 3 of Leishmania tarentolae are corrected by RNA editing: evidence for translation of the edited cytochrome oxidase subunit II mRNA."
    Shaw J., Campbell D., Simpson L.
    Proc. Natl. Acad. Sci. U.S.A. 86:6220-6224(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA EDITING.

Entry informationi

Entry nameiCOX2_LEITA
AccessioniPrimary (citable) accession number: P14545
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: October 1, 1996
Last modified: January 7, 2015
This is version 91 of the entry and version 2 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.