Cytochrome c oxidase subunit 2 - Bos taurus (Bovine)

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P68530 (COX2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 77. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Cytochrome c oxidase subunit 2

Alternative name(s):
Cytochrome c oxidase polypeptide II

Gene names

Name:	MT-CO2
Synonyms:	COII, COXII, MTCO2

Encoded on

Mitochondrion

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	227 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transmembrane Transmembrane helix
Ligand	Copper Metal-binding
PTM	Formylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	copper ion binding Inferred from electronic annotation. Source: InterPro cytochrome-c oxidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 227

227

Cytochrome c oxidase subunit 2

PRO_0000183517

Regions

Topological domain

1 – 14

Mitochondrial intermembrane

Transmembrane

15 – 45

Helical; Name=I

Topological domain

46 – 59

Mitochondrial matrix

Transmembrane

60 – 87

Helical; Name=II

Topological domain

88 – 227

140

Mitochondrial intermembrane

Sites

Metal binding

161

Copper A1

Metal binding

196

Copper A1

Metal binding

196

Copper A2

Metal binding

198

Copper A2; via carbonyl oxygen

Metal binding

198

Magnesium; shared with chain I

Metal binding

200

Copper A1

Metal binding

200

Copper A2

Metal binding

204

Copper A2

Metal binding

207

Copper A1

Amino acid modifications

Modified residue

N-formylmethionine

Experimental info

Sequence conflict

A → P in AAA31644. Ref.3

Sequence conflict

118

F → L in AAA31644. Ref.3

Secondary structure

227

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P68530 [UniParc].

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

FASTA

227

26,021

        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.

IPI

IPI00708779.

PIR

OBBO2. B00152.

RefSeq

YP_209208.1. NC_006853.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OCC	X-ray	2.80	B/O	1-227	[»]
1OCO	X-ray	2.80	B/O	1-227	[»]
1OCR	X-ray	2.35	B/O	1-227	[»]
1OCZ	X-ray	2.90	B/O	1-227	[»]
1V54	X-ray	1.80	B/O	1-227	[»]
1V55	X-ray	1.90	B/O	1-227	[»]
2DYR	X-ray	1.80	B/O	1-227	[»]
2DYS	X-ray	2.20	B/O	1-227	[»]
2EIJ	X-ray	1.90	B/O	1-227	[»]
2EIK	X-ray	2.10	B/O	1-227	[»]
2EIL	X-ray	2.10	B/O	1-227	[»]
2EIM	X-ray	2.60	B/O	1-227	[»]
2EIN	X-ray	2.70	B/O	1-227	[»]
2OCC	X-ray	2.30	B/O	1-227	[»]
2Y69	X-ray	1.95	B/O	1-227	[»]
2YBB	electron microscopy	19.00	M	1-227	[»]
2ZXW	X-ray	2.50	B/O	1-227	[»]
3ABK	X-ray	2.00	B/O	1-227	[»]
3ABL	X-ray	2.10	B/O	1-227	[»]
3ABM	X-ray	1.95	B/O	1-227	[»]
3AG1	X-ray	2.20	B/O	1-227	[»]
3AG2	X-ray	1.80	B/O	1-227	[»]
3AG3	X-ray	1.80	B/O	1-227	[»]
3AG4	X-ray	2.05	B/O	1-227	[»]
3ASN	X-ray	3.00	B/O	1-227	[»]
3ASO	X-ray	2.30	B/O	1-227	[»]

ProteinModelPortal

P68530.

SMR

P68530. Positions 1-227.

ModBase

Search...

Protein-protein interaction databases

IntAct

P68530. 1 interaction.

Protein family/group databases

TCDB

3.D.4.7.1. proton-translocating cytochrome oxidase (COX) superfamily.

Proteomic databases

PaxDb

P68530.

PRIDE

P68530.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000060549; ENSBTAP00000053151; ENSBTAG00000043556.

GeneID

3283880.

KEGG

bta:3283880.

Organism-specific databases

CTD

4513.

Phylogenomic databases

eggNOG

COG1622.

HOGENOM

HOG000264988.

HOVERGEN

HBG012727.

InParanoid

P68530.

K02261.

OrthoDB

EOG4BZN3N.

ProtClustDB

MTH00098.

Family and domain databases

Gene3D

1.10.287.90. 1 hit.
2.60.40.420. 1 hit.

InterPro

IPR001505. Copper_CuA.
IPR008972. Cupredoxin.
IPR014222. Cyt_c_oxidase_su2.
IPR002429. Cyt_c_oxidase_su2_C.
IPR011759. Cyt_c_oxidase_su2_TM_dom.
[Graphical view]

Pfam

PF00116. COX2. 1 hit.
PF02790. COX2_TM. 1 hit.
[Graphical view]

SUPFAM

SSF49503. Cupredoxin. 1 hit.
SSF81464. Cyt_c_oxidase_II-like_TM. 1 hit.

TIGRFAMs

TIGR02866. CoxB. 1 hit.

PROSITE

PS00078. COX2. 1 hit.
PS50857. COX2_CUA. 1 hit.
PS50999. COX2_TM. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P68530.

NextBio

20810187.

Entry information

Entry name

COX2_BOVIN

Accession

Primary (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:	May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents