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P68530 (COX2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Alternative name(s):
Cytochrome c oxidase polypeptide II
Gene names
Name:MT-CO2
Synonyms:COII, COXII, MTCO2
Encoded onMitochondrion
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length227 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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.

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

Chain1 – 227227Cytochrome c oxidase subunit 2
PRO_0000183517

Regions

Topological domain1 – 1414Mitochondrial intermembrane
Transmembrane15 – 4531Helical; Name=I
Topological domain46 – 5914Mitochondrial matrix
Transmembrane60 – 8728Helical; Name=II
Topological domain88 – 227140Mitochondrial intermembrane

Sites

Metal binding1611Copper A1
Metal binding1961Copper A1
Metal binding1961Copper A2
Metal binding1981Copper A2; via carbonyl oxygen
Metal binding1981Magnesium; shared with chain I
Metal binding2001Copper A1
Metal binding2001Copper A2
Metal binding2041Copper A2
Metal binding2071Copper A1

Amino acid modifications

Modified residue11N-formylmethionine

Experimental info

Sequence conflict581A → P in AAA31644. Ref.3
Sequence conflict1181F → L in AAA31644. Ref.3

Secondary structure

...................................... 227
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P68530 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: C562D5B39FA9771A

FASTA22726,021
        10         20         30         40         50         60 
MAYPMQLGFQ DATSPIMEEL LHFHDHTLMI VFLISSLVLY IISLMLTTKL THTSTMDAQE 

        70         80         90        100        110        120 
VETIWTILPA IILILIALPS LRILYMMDEI NNPSLTVKTM GHQWYWSYEY TDYEDLSFDS 

       130        140        150        160        170        180 
YMIPTSELKP GELRLLEVDN RVVLPMEMTI RMLVSSEDVL HSWAVPSLGL KTDAIPGRLN 

       190        200        210        220 
QTTLMSSRPG LYYGQCSEIC GSNHSFMPIV LELVPLKYFE KWSASML 

« Hide

References

[1]"Studies on cytochrome c oxidase, IV[1-3]. Primary structure and function of subunit II."
Steffens G.J., Buse G.
Hoppe-Seyler's Z. Physiol. Chem. 360:613-619(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Heart.
[2]"Complete sequence of bovine mitochondrial DNA. Conserved features of the mammalian mitochondrial genome."
Anderson S., de Bruijn M.H.L., Coulson A.R., Eperon I.C., Sanger F., Young I.G.
J. Mol. Biol. 156:683-717(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Heart.
[3]"The genetic code in bovine mitochondria: sequence of genes for the cytochrome oxidase subunit II and two tRNAs."
Young I.G., Anderson S.
Gene 12:257-265(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Bos taurus mitochondrial protein coding regions."
Wettstein P.J.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 65, 66, D and F.
[5]"The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A."
Tsukihara T., Aoyama H., Yamashita E., Tomizaki T., Yamaguchi H., Shinzawa-Itoh K., Nakashima R., Yaono R., Yoshikawa S.
Science 272:1136-1144(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[6]"Structure analysis of bovine heart cytochrome c oxidase at 2.8 A resolution."
Tomizaki T., Yamashita E., Yamaguchi H., Aoyama H., Tsukihara T., Shinzawa-Itoh K., Nakashima R., Yaono R., Yoshikawa S.
Acta Crystallogr. D 55:31-45(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
Tissue: Heart.
[7]"X-ray structure of azide-bound fully oxidized cytochrome c oxidase from bovine heart at 2.9 A resolution."
Fei M.J., Yamashita E., Inoue N., Yao M., Yamaguchi H., Tsukihara T., Shinzawa-Itoh K., Nakashima R., Yoshikawa S.
Acta Crystallogr. D 56:529-535(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
Tissue: Heart.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V00654 Genomic DNA. Translation: CAA24000.1.
M10544 Genomic DNA. Translation: AAA31644.1.
AF490528 Genomic DNA. Translation: AAM08331.1.
AF490529 Genomic DNA. Translation: AAM08344.1.
AF493541 Genomic DNA. Translation: AAM12792.1.
AF493542 Genomic DNA. Translation: AAM12805.1.
PIROBBO2. B00152.
RefSeqYP_209208.1. NC_006853.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OCCX-ray2.80B/O1-227[»]
1OCOX-ray2.80B/O1-227[»]
1OCRX-ray2.35B/O1-227[»]
1OCZX-ray2.90B/O1-227[»]
1V54X-ray1.80B/O1-227[»]
1V55X-ray1.90B/O1-227[»]
2DYRX-ray1.80B/O1-227[»]
2DYSX-ray2.20B/O1-227[»]
2EIJX-ray1.90B/O1-227[»]
2EIKX-ray2.10B/O1-227[»]
2EILX-ray2.10B/O1-227[»]
2EIMX-ray2.60B/O1-227[»]
2EINX-ray2.70B/O1-227[»]
2OCCX-ray2.30B/O1-227[»]
2Y69X-ray1.95B/O1-227[»]
2YBBelectron microscopy19.00M1-227[»]
2ZXWX-ray2.50B/O1-227[»]
3ABKX-ray2.00B/O1-227[»]
3ABLX-ray2.10B/O1-227[»]
3ABMX-ray1.95B/O1-227[»]
3AG1X-ray2.20B/O1-227[»]
3AG2X-ray1.80B/O1-227[»]
3AG3X-ray1.80B/O1-227[»]
3AG4X-ray2.05B/O1-227[»]
3ASNX-ray3.00B/O1-227[»]
3ASOX-ray2.30B/O1-227[»]
ProteinModelPortalP68530.
SMRP68530. Positions 1-227.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP68530. 1 interaction.

Protein family/group databases

TCDB3.D.4.7.1. the proton-translocating cytochrome oxidase (cox) superfamily.

Proteomic databases

PaxDbP68530.
PRIDEP68530.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000060549; ENSBTAP00000053151; ENSBTAG00000043556.
GeneID3283880.
KEGGbta:3283880.

Organism-specific databases

CTD4513.

Phylogenomic databases

eggNOGCOG1622.
HOGENOMHOG000264988.
HOVERGENHBG012727.
InParanoidP68530.
KOK02261.
OMAEDVLHSW.
OrthoDBEOG7TJ3JX.
ProtClustDBMTH00098.
TreeFamTF344269.

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...

Other

EvolutionaryTraceP68530.
NextBio20810187.

Entry information

Entry nameCOX2_BOVIN
AccessionPrimary (citable) accession number: P68530
Secondary accession number(s): P00404
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: March 19, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references