Cytochrome c oxidase subunit 1 - MT-CO1 - Anas platyrhynchos (Domestic duck)

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P50656 (COX1_ANAPL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 78. 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 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

Anas platyrhynchos (Domestic duck) (Anas boschas) [Complete proteome]

Taxonomic identifier

8839 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Testudines + Archosauria group › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Anseriformes › Anatidae › Anas

Protein attributes

Sequence length	102 AA.
Sequence status	Fragment.
Protein existence	Inferred from homology

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.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transmembrane Transmembrane helix
Ligand	Copper Heme Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	aerobic respiration Inferred from electronic annotation. Source: InterPro oxidative phosphorylation Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	integral component of membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell respiratory chain complex IV Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	cytochrome-c oxidase activity Inferred from electronic annotation. Source: UniProtKB-EC electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion 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 – ›102

›102

Cytochrome c oxidase subunit 1

PRO_0000183281

Regions

Transmembrane

18 – 38

Helical; Potential

Transmembrane

64 – 84

Helical; Potential

Sites

Metal binding

Iron (heme A axial ligand) Probable

Experimental info

Sequence conflict

47 – 50

TLLG → PPGL in CAA39146. Ref.2

Sequence conflict

V → D in CAA39146. Ref.2

Non-terminal residue

102

Sequences

Sequence

Length

Mass (Da)

Tools

P50656 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 5E1B143E869F8115
Show »

FASTA

102

11,414

        10         20         30         40         50         60 
MTFINRWLFS TNHKDIGTLY LIFGAWAGMI GTALSLLIRA ELGQPGTLLG DDQIYNVIVT 

        70         80         90        100 
RHAFVMIFFM VMPIMIGGFG NWLVPLMIGA PDMAFPRMNN MS

« Hide

References

[1]	"Molecular characterization and evolution of a duck mitochondrial genome." Ramirez V., Savoie P., Morais R. J. Mol. Evol. 37:296-310(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: Pekin breed. Tissue: Liver.
[2]	"Gene organization of the Peking duck mitochondrial genome." Desjardins P., Ramirez V., Morais R. Curr. Genet. 17:515-518(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-59. Strain: Pekin breed. Tissue: Liver.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L22480 Unassigned DNA. Translation: AAA16541.1. X55529 Genomic DNA. Translation: CAA39146.1.
3D structure databases
ProteinModelPortal	P50656.
SMR	P50656. Positions 3-102.
ModBase	Search...
MobiDB	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00705.
Family and domain databases
Gene3D	1.20.210.10. 1 hit.
InterPro	IPR000883. Cyt_c_Oxase_su1. IPR023616. Cyt_c_Oxase_su1_dom. [Graphical view]
PANTHER	PTHR10422. PTHR10422. 1 hit.
Pfam	PF00115. COX1. 1 hit. [Graphical view]
PRINTS	PR01165. CYCOXIDASEI.
SUPFAM	SSF81442. SSF81442. 1 hit.
PROSITE	PS50855. COX1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

COX1_ANAPL

Accession

Primary (citable) accession number: P50656

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	April 16, 2014
This is version 78 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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

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

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