Reviewed, UniProtKB/Swiss-Prot P00396 (COX1_BOVIN)

Names and origin

Protein names

Recommended name:
    Cytochrome c oxidase subunit 1
    EC=1.9.3.1
Alternative name(s):
    Cytochrome c oxidase polypeptide I

Gene names

Name:	MT-CO1
Synonyms:	COI, COXI, MTCO1

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	514 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.
Catalytic activity	4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O.
Pathway	Energy metabolism; oxidative phosphorylation.
Subcellular location	Mitochondrion inner membrane; Multi-pass membrane protein.
Post-translational modification	His-240 and Tyr-244 are involved in the formation of a copper-coordinated covalent cross-link at the active site of the catalytic subunit I.
Sequence similarities	Belongs to the heme-copper respiratory oxidase family.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transmembrane
Ligand	Copper Heme Iron Metal-binding
Molecular function	Oxidoreductase
PTM	Formylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	aerobic respiration Inferred from electronic annotation. Source: InterPro electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport 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: UniProtKB-KW cytochrome-c oxidase activity Inferred from electronic annotation. Source: EC 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 – 514

514

Cytochrome c oxidase subunit 1

PRO_0000183294

Regions

Topological domain

1 – 11

11

Mitochondrial matrix Ref.2

Transmembrane

12 – 40

29

I Ref.2

Topological domain

41 – 50

10

Mitochondrial intermembrane Ref.5

Transmembrane

51 – 86

36

II

Topological domain

87 – 94

8

Mitochondrial matrix Ref.2

Transmembrane

95 – 117

23

III

Topological domain

118 – 140

23

Mitochondrial intermembrane Ref.2

Transmembrane

141 – 170

30

IV Ref.2

Topological domain

171 – 182

12

Mitochondrial matrix Ref.2

Transmembrane

183 – 212

30

V Ref.2

Topological domain

213 – 227

15

Mitochondrial intermembrane Ref.2

Transmembrane

228 – 261

34

VI Ref.2

Topological domain

262 – 269

8

Mitochondrial matrix Ref.2

Transmembrane

270 – 286

17

VII

Topological domain

287 – 298

12

Mitochondrial intermembrane Ref.2

Transmembrane

299 – 327

29

VIII

Topological domain

328 – 335

8

Mitochondrial matrix

Transmembrane

336 – 357

22

IX

Topological domain

358 – 370

13

Mitochondrial intermembrane

Transmembrane

371 – 400

30

X

Topological domain

401 – 406

6

Mitochondrial matrix Ref.2

Transmembrane

407 – 433

27

XI

Topological domain

434 – 446

13

Mitochondrial intermembrane

Transmembrane

447 – 478

32

XII Ref.2

Topological domain

479 – 514

36

Mitochondrial matrix Ref.2

Sites

Metal binding

61

1

Iron (heme A axial ligand) Ref.2

Metal binding

240

1

Copper B Ref.2

Metal binding

290

1

Copper B Ref.2

Metal binding

291

1

Copper B Ref.2

Metal binding

368

1

Magnesium; shared with chain II

Metal binding

376

1

Iron (heme A3 axial ligand) Ref.2

Metal binding

378

1

Iron (heme A axial ligand) Ref.2

Binding site

244

1

Oxygen Probable

Amino acid modifications

Modified residue

1

1

N-formylmethionine Ref.2

Cross-link

240 ↔ 244

1'-histidyl-3'-tyrosine (His-Tyr) Ref.4

Secondary structure

1

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514

Helix Strand Turn

Details...

Helix

2 – 6

5

Helix

12 – 41

30

Beta strand

43 – 45

3

Beta strand

47 – 50

4

Helix

51 – 67

17

Helix

70 – 74

5

Helix

77 – 86

10

Helix

95 – 103

9

Helix

105 – 115

11

Turn

125 – 128

4

Turn

130 – 133

4

Turn

135 – 138

4

Helix

141 – 170

30

Helix

178 – 180

3

Helix

183 – 214

32

Helix

222 – 224

3

Helix

228 – 245

18

Helix

248 – 260

13

Turn

261 – 263

3

Helix

270 – 283

14

Helix

288 – 291

4

Helix

299 – 311

13

Helix

313 – 327

15

Helix

336 – 357

22

Helix

361 – 367

7

Helix

371 – 382

12

Helix

385 – 401

17

Helix

407 – 425

19

Helix

428 – 433

6

Beta strand

437 – 439

3

Helix

445 – 447

3

Helix

448 – 478

31

Helix

488 – 490

3

Helix

492 – 494

3

Sequences

	Sequence		Length	Mass (Da)
	P00396-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 0D7C807D7FA3996C	FASTA	514	57,032
	10 20 30 40 50 60 MFINRWLFST NHKDIGTLYL LFGAWAGMVG TALSLLIRAE LGQPGTLLGD DQIYNVVVTA 70 80 90 100 110 120 HAFVMIFFMV MPIMIGGFGN WLVPLMIGAP DMAFPRMNNM SFWLLPPSFL LLLASSMVEA 130 140 150 160 170 180 GAGTGWTVYP PLAGNLAHAG ASVDLTIFSL HLAGVSSILG AINFITTIIN MKPPAMSQYQ 190 200 210 220 230 240 TPLFVWSVMI TAVLLLLSLP VLAAGITMLL TDRNLNTTFF DPAGGGDPIL YQHLFWFFGH 250 260 270 280 290 300 PEVYILILPG FGMISHIVTY YSGKKEPFGY MGMVWAMMSI GFLGFIVWAH HMFTVGMDVD 310 320 330 340 350 360 TRAYFTSATM IIAIPTGVKV FSWLATLHGG NIKWSPAMMW ALGFIFLFTV GGLTGIVLAN 370 380 390 400 410 420 SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM GGFVHWFPLF SGYTLNDTWA KIHFAIMFVG 430 440 450 460 470 480 VNMTFFPQHF LGLSGMPRRY SDYPDAYTMW NTISSMGSFI SLTAVMLMVF IIWEAFASKR 490 500 510 EVLTVDLTTT NLEWLNGCPP PYHTFEEPTY VNLK

References

[1]	"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.
[2]	"Studies on cytochrome-c oxidase, XIV. The amino-acid sequence of subunit I -- proteinchemical methods for the analysis of a large hydrophobic membrane protein." Hensel S., Buse G. Biol. Chem. Hoppe-Seyler 371:411-422(1990) [PubMed: 2165784] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Heart.
[3]	"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.
[4]	"Evidence for a copper-coordinated histidine-tyrosine cross-link in the active site of cytochrome oxidase." Buse G., Soulimane T., Dewor M., Meyer H.E., Blueggel M. Protein Sci. 8:985-990(1999) [PubMed: 10338009] [Abstract] Cited for: COVALENT BOND.
[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

EMBLGenBankDDBJ

V00654 Genomic DNA. Translation: CAA23999.1.
AF490528 Genomic DNA. Translation: AAM08330.1.
AF490529 Genomic DNA. Translation: AAM08343.1.
AF493541 Genomic DNA. Translation: AAM12791.1.
AF493542 Genomic DNA. Translation: AAM12804.1.

IPI

IPI00709295.

PIR

ODBO1. A00464.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OCC	X-ray	2.80	A/N	1-514	[»]
1OCO	X-ray	2.80	A/N	1-514	[»]
1OCR	X-ray	2.35	A/N	1-514	[»]
1OCZ	X-ray	2.90	A/N	1-514	[»]
1V54	X-ray	1.80	A/N	1-514	[»]
1V55	X-ray	1.90	A/N	1-514	[»]
2DYR	X-ray	1.80	A/N	1-514	[»]
2DYS	X-ray	2.20	A/N	1-514	[»]
2EIJ	X-ray	1.90	A/N	1-514	[»]
2EIK	X-ray	2.10	A/N	1-514	[»]
2EIL	X-ray	2.10	A/N	1-514	[»]
2EIM	X-ray	2.60	A/N	1-514	[»]
2EIN	X-ray	2.70	A/N	1-514	[»]
2OCC	X-ray	2.30	A/N	1-514	[»]
2ZXW	X-ray	2.50	A/N	1-514	[»]

ModBase

Search...

Protein family/group databases

TCDB

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

Genome annotation databases

Ensembl

ENSBTAG00000043561. Bos taurus. [Contig view]

Phylogenomic databases

HOVERGEN

P00396.

Enzyme and pathway databases

BRENDA

1.9.3.1. 251.

Family and domain databases

InterPro

IPR000883. Cyt_c_oxidase_su1.
[Graphical view]

Gene3D

G3DSA:1.20.210.10. COX1. 1 hit.

PANTHER

PTHR10422. COX1. 1 hit.

Pfam

PF00115. COX1. 1 hit.
[Graphical view]

PRINTS

PR01165. CYCOXIDASEI.

PROSITE

PS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

COX1_BOVIN

Accession

Primary (citable) accession number: P00396

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	June 16, 2009
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)