Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P32646 (COX2_VIGUN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. 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, mitochondrial

EC=1.9.3.1
Alternative name(s):
Cytochrome c oxidase polypeptide II
Gene names
Name:COX2
OrganismVigna unguiculata (Cowpea)
Taxonomic identifier3917 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeVigna

Protein attributes

Sequence length376 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide‹1 – ?Mitochondrion Potential
Chain? – 376Cytochrome c oxidase subunit 2, mitochondrialPRO_0000006044

Regions

Topological domain? – 163Mitochondrial intermembrane Potential
Transmembrane164 – 18421Helical; Potential
Topological domain185 – 20420Mitochondrial matrix Potential
Transmembrane205 – 22521Helical; Potential
Topological domain226 – 376151Mitochondrial intermembrane Potential

Sites

Metal binding3091Copper A Probable
Metal binding3441Copper A Probable
Metal binding3481Copper A Probable
Metal binding3521Copper A Probable

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P32646 [UniParc].

Last modified July 25, 2003. Version 2.
Checksum: 8DE459D6C71B65B8

FASTA37642,222
        10         20         30         40         50         60 
STVVGKCCKG NFGMSRFLLS NDFQRKLIVS GKESYYDHFS KRSYSSPSKA PGTESTITST 

        70         80         90        100        110        120 
KIKMPNIGSE GFAFSSFLST VNKNSRMINF SSCLKTPVKP EQIAANPVIL KMTTELEKIP 

       130        140        150        160        170        180 
RALRWMCGGF PAIALCDAPE PWQLGFQDAA TPIMQGIMDL HHDIFFFLVQ ILVFVLWVLS 

       190        200        210        220        230        240 
RALWCFRSKI SPIPQRIVHG TTIEILWTIL PSIILMFIAI PSFTLLYSMD DVVVDPAITI 

       250        260        270        280        290        300 
KAIGHQWYWS YEYSDYNNSD EQSLAFDSYM VPEDDLELGQ LRLLEVDNRV VVPAKTHLRV 

       310        320        330        340        350        360 
LITSADVLHS WAVPSLGVKC DAVPGRLNQI STFIQREGVY YGQCSEICGT NHAFMPIVVE 

       370 
AVSTKDYGSW VSNQIQ 

« Hide

References

[1]Adams K.L.
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"RNA-mediated transfer of the gene coxII from the mitochondrion to the nucleus during flowering plant evolution."
Nugent J.M., Palmer J.D.
Cell 66:473-481(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 64-376.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF211254 mRNA. Translation: AAF19523.1.
PIRA39653.

3D structure databases

ProteinModelPortalP32646.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.287.90. 1 hit.
2.60.40.420. 1 hit.
InterProIPR001505. Copper_CuA.
IPR008972. Cupredoxin.
IPR014222. Cyt_c_oxidase_su2.
IPR002429. Cyt_c_oxidase_su2_C.
IPR011759. Cyt_c_oxidase_su2_TM_dom.
[Graphical view]
PfamPF00116. COX2. 1 hit.
PF02790. COX2_TM. 1 hit.
[Graphical view]
SUPFAMSSF49503. SSF49503. 1 hit.
SSF81464. SSF81464. 1 hit.
TIGRFAMsTIGR02866. CoxB. 1 hit.
PROSITEPS00078. COX2. 1 hit.
PS50857. COX2_CUA. 1 hit.
PS50999. COX2_TM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX2_VIGUN
AccessionPrimary (citable) accession number: P32646
Secondary accession number(s): Q9LD17
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: July 25, 2003
Last modified: April 16, 2014
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families