Cytochrome c oxidase subunit 1 - Drosophila mauritiana (Fruit fly)

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Reviewed, UniProtKB/Swiss-Prot Q34345 (COX1_DROMA)

Last modified October 13, 2009. Version 63. 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:CoI
Synonyms:	CoI

Encoded on

Mitochondrion

Organism

Drosophila mauritiana (Fruit fly)

Taxonomic identifier

7226 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

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Protein attributes

Sequence length	499 AA.
Sequence status	Fragment.
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
Coding sequence diversity	Polymorphism
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-SubCell mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-KW 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 – ›499

›499

Cytochrome c oxidase subunit 1

PRO_0000183324

Regions

Transmembrane

16 – 36

Potential

Transmembrane

55 – 75

Potential

Transmembrane

101 – 121

Potential

Transmembrane

144 – 164

Potential

Transmembrane

182 – 202

Potential

Transmembrane

233 – 253

Potential

Transmembrane

267 – 287

Potential

Transmembrane

304 – 324

Potential

Transmembrane

337 – 357

Potential

Transmembrane

379 – 399

Potential

Transmembrane

413 – 433

Potential

Transmembrane

451 – 471

Potential

Sites

Metal binding

Iron (heme A axial ligand) Probable

Metal binding

239

Copper B Probable

Metal binding

243

Copper B Probable

Metal binding

289

Copper B Probable

Metal binding

290

Copper B Probable

Metal binding

375

Iron (heme A3 axial ligand) Probable

Metal binding

377

Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link

239 ↔ 243

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

Natural variations

Natural variant

412

H → Q in strain: G52.

Experimental info

Non-terminal residue

499

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Sequences

Sequence

Length

Mass (Da)

Tools

Q34345-1 [UniParc].

Last modified August 1, 1999. Version 2.
Checksum: F930E67C0E49E635
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FASTA

499

55,060

        10         20         30         40         50         60 
MPRQWLFSTN HKDIGTLYFI FGAWAGMVGT SLSILIRAEL GHPGALIGDD QIYNVIVTAH 

        70         80         90        100        110        120 
AFIMIFFMVM PIMIGGFGNW LVPLMLGAPD MAFPRMNNMS FWLLPPALSL LLVSSMVENG 

       130        140        150        160        170        180 
AGTGWTVYPP LSAGIAHGGA SVDLAIFSLH LAGISSILGA VNFITTVINM RSTGISLDRM 

       190        200        210        220        230        240 
PLFVWSVVIT ALLLLLSLPV LAGAITMLLT DRNLNTSFFD PAGGGDPILY QHLFWFFGHP 

       250        260        270        280        290        300 
EVYILILPGF GMISHIISQE SGKKETFGSL GMIYAMLAIG LLGFIVWAHH MFTVGMDVDT 

       310        320        330        340        350        360 
RAYFTSATMI IAVPTGIKIF SWLATLHGTQ LSYSPAILWA LGFVFLFTVG GLTGVVLANS 

       370        380        390        400        410        420 
SVDIILHDTY YVVAHFHYVL SMGAVFAIMA GFIHWYPLFT GLTLNNKWLK SHFIIMFIGV 

       430        440        450        460        470        480 
NLTFFPQHFL GLAGMPRRYS DYPDAYTTWN VVSTIGSTIS LLGILFFFYI IWESLVSQRQ 

       490 
VIYPIQLNSS IEWYQNTPP

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References

[1]	"Evolution of Drosophila mitochondrial DNA and the history of the melanogaster subgroup." Satta Y., Takahata N. Proc. Natl. Acad. Sci. U.S.A. 87:9558-9562(1990) [PubMed: 2124697] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: G52 and Mauritius island.
[2]	"Analysis of nucleotide substitutions of mitochondrial DNAs in Drosophila melanogaster and its sibling species." Satta Y., Ishiwa H., Chigusa S.I. Mol. Biol. Evol. 4:638-650(1987) [PubMed: 2832697] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-102. Strain: Mauritius island.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	M18073 Genomic DNA. Translation: AAA69804.2. M57907 Genomic DNA. Translation: AAB02280.1. M57912 Genomic DNA. Translation: AAA99051.1.
3D structure databases
HSSP	HSSP built from PDB template 2OCC based on UniProtKB P00396.
SMR	Q34345. Positions 4-499.
ModBase	Search...
Organism-specific databases
FlyBase	FBgn0012510. Dmau\mt:CoI.
Enzyme and pathway databases
BRENDA	1.9.3.1. 294628.
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_DROMA

Accession

Primary (citable) accession number: Q34345
Secondary accession number(s): Q34346, Q34350

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 15, 2002
Last sequence update:	August 1, 1999
Last modified:	October 13, 2009
This is version 63 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project

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Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

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

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Organism-specific databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents