Cytochrome c oxidase subunit 1 - Bos mutus grunniens (Wild yak)

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Reviewed, UniProtKB/Swiss-Prot Q5Y4Q8 (COX1_BOSMU)

Last modified June 16, 2009. Version 28. History...

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

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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 mutus grunniens (Wild yak) (Bos grunniens)

Taxonomic identifier

30521 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	514 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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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.
Sequence similarities	Belongs to the heme-copper respiratory oxidase family.

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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
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...

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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_0000253786

Regions

Topological domain

1 – 11

Mitochondrial matrix By similarity

Transmembrane

12 – 40

I By similarity

Topological domain

41 – 50

Mitochondrial intermembrane By similarity

Transmembrane

51 – 86

II By similarity

Topological domain

87 – 94

Mitochondrial matrix By similarity

Transmembrane

95 – 117

III By similarity

Topological domain

118 – 140

Mitochondrial intermembrane By similarity

Transmembrane

141 – 170

IV By similarity

Topological domain

171 – 182

Mitochondrial matrix By similarity

Transmembrane

183 – 212

V By similarity

Topological domain

213 – 227

Mitochondrial intermembrane By similarity

Transmembrane

228 – 261

VI By similarity

Topological domain

262 – 269

Mitochondrial matrix By similarity

Transmembrane

270 – 286

VII By similarity

Topological domain

287 – 298

Mitochondrial intermembrane By similarity

Transmembrane

299 – 327

VIII By similarity

Topological domain

328 – 335

Mitochondrial matrix By similarity

Transmembrane

336 – 357

IX By similarity

Topological domain

358 – 370

Mitochondrial intermembrane By similarity

Transmembrane

371 – 400

X By similarity

Topological domain

401 – 406

Mitochondrial matrix By similarity

Transmembrane

407 – 433

XI By similarity

Topological domain

434 – 446

Mitochondrial intermembrane By similarity

Transmembrane

447 – 478

XII By similarity

Topological domain

479 – 514

Mitochondrial matrix By similarity

Sites

Metal binding

Iron (heme A axial ligand) Probable

Metal binding

244

Copper B Probable

Metal binding

290

Copper B Probable

Metal binding

291

Copper B Probable

Metal binding

376

Iron (heme A3 axial ligand) Probable

Metal binding

378

Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link

240 ↔ 244

1'-histidyl-3'-tyrosine (His-Tyr) By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

Q5Y4Q8-1 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 9D7FD418DE78EDC0
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FASTA

514

56,918

        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 LGLSGMPRRS PDYPDAYTMW NTVSSMGSFI SLTAVMLMVF IIWEALASKR 

       490        500        510 
EVLTVDLTTT NLEWLNGCPP PYHTFEEPTY VNLK

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References

[1]	"Complete sequence of the Yak (Bos grunniens.) mitochondrial genome and its genetic relationship with related species." Gu Z., Zhao X., Li N., Wu C. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

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Cross-references

Sequence databases
	AY684273 Genomic DNA. Translation: AAU89108.1.
3D structure databases
SMR	Q5Y4Q8. Positions 1-514.
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q5Y4Q8.
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...

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Entry information

Entry name

COX1_BOSMU

Accession

Primary (citable) accession number: Q5Y4Q8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 17, 2006
Last sequence update:	November 23, 2004
Last modified:	June 16, 2009
This is version 28 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents