Reviewed, UniProtKB/Swiss-Prot Q34391 (COX1_DROSE)

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 sechellia (Fruit fly)

Taxonomic identifier

7238 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	499 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
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
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...

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_0000183327
Regions
	Transmembrane	16 – 36	21	Potential
	Transmembrane	55 – 75	21	Potential
	Transmembrane	101 – 121	21	Potential
	Transmembrane	144 – 164	21	Potential
	Transmembrane	182 – 202	21	Potential
	Transmembrane	233 – 253	21	Potential
	Transmembrane	267 – 287	21	Potential
	Transmembrane	304 – 324	21	Potential
	Transmembrane	337 – 357	21	Potential
	Transmembrane	379 – 399	21	Potential
	Transmembrane	413 – 433	21	Potential
	Transmembrane	451 – 471	21	Potential
Sites
	Metal binding	60	1	Iron (heme A axial ligand) Probable
	Metal binding	239	1	Copper B Probable
	Metal binding	243	1	Copper B Probable
	Metal binding	289	1	Copper B Probable
	Metal binding	290	1	Copper B Probable
	Metal binding	375	1	Iron (heme A3 axial ligand) Probable
	Metal binding	377	1	Iron (heme A axial ligand) Probable
Amino acid modifications
	Cross-link	239 ↔ 243		1'-histidyl-3'-tyrosine (His-Tyr) By similarity
Experimental info
	Non-terminal residue	499	1

Sequences

	Sequence		Length	Mass (Da)
	Q34391-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 31AFD754D30F12F3	FASTA	499	55,037
	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 SQFITMFIGV 430 440 450 460 470 480 NLTFFPQHFL GLAGMPRRYS DYPDAYTTWN IVSTIGSTIS LLGILFFFFI IWESLVSQRQ 490 VIYPIQLNSS IEWYQNTPP

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: SS78.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M57908 Genomic DNA. Translation: AAB02286.1.
3D structure databases
HSSP	HSSP built from PDB template 2OCC based on UniProtKB P00396.
SMR	Q34391. Positions 4-499.
ModBase	Search...
Organism-specific databases
FlyBase	FBgn0012794. Dsec\mt:CoI.
Enzyme and pathway databases
BRENDA	1.9.3.1. 300118.
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_DROSE

Accession

Primary (citable) accession number: Q34391

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 15, 2002
Last sequence update:	November 1, 1996
Last modified:	October 13, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project