P68530 (COX2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

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)

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	respiratory electron transport chain Inferred from electronic annotation. Source: InterPro
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 electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding 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

14

Mitochondrial intermembrane

Transmembrane

15 – 45

31

Helical; Name=I

Topological domain

46 – 59

14

Mitochondrial matrix

Transmembrane

60 – 87

28

Helical; Name=II

Topological domain

88 – 227

140

Mitochondrial intermembrane

Sites

Metal binding

161

1

Copper A1

Metal binding

196

1

Copper A1

Metal binding

196

1

Copper A2

Metal binding

198

1

Copper A2; via carbonyl oxygen

Metal binding

198

1

Magnesium; shared with chain I

Metal binding

200

1

Copper A1

Metal binding

200

1

Copper A2

Metal binding

204

1

Copper A2

Metal binding

207

1

Copper A1

Amino acid modifications

Modified residue

1

1

N-formylmethionine

Experimental info

Sequence conflict

58

1

A → P in AAA31644. Ref.3

Sequence conflict

118

1

F → L in AAA31644. Ref.3

Secondary structure

1

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227

Helix Strand Turn

Details...

Helix

15 – 45

31

Helix

59 – 62

4

Helix

64 – 86

23

Beta strand

94 – 102

9

Beta strand

105 – 110

6

Beta strand

112 – 114

3

Beta strand

116 – 120

5

Helix

125 – 127

3

Turn

134 – 136

3

Beta strand

138 – 140

3

Beta strand

142 – 145

4

Beta strand

148 – 159

12

Beta strand

161 – 165

5

Helix

166 – 168

3

Beta strand

170 – 174

5

Beta strand

180 – 185

6

Beta strand

190 – 194

5

Turn

202 – 205

4

Beta strand

209 – 214

6

Helix

216 – 225

10

Sequences

	Sequence		Length	Mass (Da)
	P68530 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: C562D5B39FA9771A	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

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: 220175] [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: 7120390] [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: 6265319] [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: 8638158] [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: 10089392] [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: 10771420] [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.

STRING

P68530.

Protein family/group databases

TCDB

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

Proteomic databases

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

maNOG12393.

HOVERGEN

HBG012727.

InParanoid

P68530.

OrthoDB

EOG4BZN3N.

PhylomeDB

P68530.

ProtClustDB

MTH00098.

Family and domain databases

InterPro

IPR001505. Copper_CuA.
IPR008972. Cupredoxin.
IPR014222. Cyt_c_oxidase_su2.
IPR015964. Cyt_c_oxidase_su2-like_TM_dom.
IPR002429. Cyt_c_oxidase_su2_C.
IPR011759. Cyt_c_oxidase_su2_TM_dom.
[Graphical view]

Gene3D

G3DSA:1.10.287.90. COX2_TM. 1 hit.
G3DSA:2.60.40.420. Cupredoxin. 1 hit.

KO

K02261.

Pfam

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

PRINTS

PR01166. CYCOXIDASEII.

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...

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:	December 14, 2011
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program