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P14545 (COX2_LEITA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytochrome c oxidase subunit 2

EC=1.9.3.1
Alternative name(s):
Cytochrome c oxidase polypeptide II
Encoded onMitochondrion
OrganismLeishmania tarentolae (Sauroleishmania tarentolae)
Taxonomic identifier5689 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmanializard Leishmania

Protein attributes

Sequence length210 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 activity

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

Cofactor

Copper A.

Subcellular location

Mitochondrion inner membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the cytochrome c oxidase subunit 2 family.

RNA editing

Modified position: not applicable.
Some positions are modified by RNA editing via nucleotide insertion. Ref.3

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 210210Cytochrome c oxidase subunit 2
PRO_0000183616

Regions

Topological domain1 – 2020Mitochondrial intermembrane Potential
Transmembrane21 – 4222Helical; Potential
Topological domain43 – 6018Mitochondrial matrix Potential
Transmembrane61 – 8626Helical; Potential
Topological domain87 – 210124Mitochondrial intermembrane Potential

Sites

Metal binding1571Copper A Probable
Metal binding1921Copper A Probable
Metal binding1961Copper A Probable
Metal binding2001Copper A Probable

Sequences

Sequence LengthMass (Da)Tools
P14545 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: B3A0544E258047C2

FASTA21023,977
        10         20         30         40         50         60 
MAFILSFWMI FLLDSVIVLL SFVCFVCVWI CALLFSTVLL VSKLNNIYCT WDFTASKFID 

        70         80         90        100        110        120 
VYWFTIGGMF SLGLLLRLCL LLYFGHLNFV SFDLCKVVGF QWYWVYFIFG ETTIFSNLIL 

       130        140        150        160        170        180 
ESDYMIGDLR LLQCNHVLTL LSLVIYKLWL SAVDVIHSFA ISSLGVKVDC IPGRCNEIVL 

       190        200        210 
FSSNNATVYG QCSELCGVLH GFMPIVICFI 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L07544 mRNA. Translation: AAA31876.1.
M10126 Genomic DNA. No translation available.
PIRI22848.

3D structure databases

ProteinModelPortalP14545.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.40.420. 1 hit.
InterProIPR001505. Copper_CuA.
IPR008972. Cupredoxin.
IPR002429. Cyt_c_oxidase_su2_C.
[Graphical view]
PfamPF00116. COX2. 1 hit.
[Graphical view]
SUPFAMSSF49503. SSF49503. 1 hit.
PROSITEPS00078. COX2. 1 hit.
PS50857. COX2_CUA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX2_LEITA
AccessionPrimary (citable) accession number: P14545
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families