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

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Q34388 (COX1_DROSI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 84. History...

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

Documents (3) |

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:CoI
Synonyms:	CoI

Encoded on

Mitochondrion

Organism

Drosophila simulans (Fruit fly) [Complete proteome]

Taxonomic identifier

7240 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	511 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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.
Sequence similarities	Belongs to the heme-copper respiratory oxidase family.
Caution	There is no mitochondrial-type translation initiation codon present in frame in the sequence. In Ref.6, the authors suggest the presence of a novel start codon coding for either Pro or Ser in Drosophila CoI transcripts.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Coding sequence diversity	Polymorphism
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 electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW oxidative phosphorylation Inferred from electronic annotation. Source: UniProtKB-UniPathway
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	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 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 – 511

511

Cytochrome c oxidase subunit 1

PRO_0000183328

Regions

Transmembrane

15 – 35

Helical; Potential

Transmembrane

54 – 74

Helical; Potential

Transmembrane

100 – 120

Helical; Potential

Transmembrane

143 – 163

Helical; Potential

Transmembrane

181 – 201

Helical; Potential

Transmembrane

232 – 252

Helical; Potential

Transmembrane

266 – 286

Helical; Potential

Transmembrane

303 – 323

Helical; Potential

Transmembrane

336 – 356

Helical; Potential

Transmembrane

378 – 398

Helical; Potential

Transmembrane

412 – 432

Helical; Potential

Transmembrane

450 – 470

Helical; Potential

Sites

Metal binding

Iron (heme A axial ligand) Probable

Metal binding

238

Copper B Probable

Metal binding

242

Copper B Probable

Metal binding

288

Copper B Probable

Metal binding

289

Copper B Probable

Metal binding

374

Iron (heme A3 axial ligand) Probable

Metal binding

376

Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link

238 ↔ 242

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

Natural variations

Natural variant

450

V → I in strain: Hawaii, New Caledonia and Tahiti. Ref.1 Ref.4

Natural variant

468

Y → F in strain: Hawaii, New Caledonia and Tahiti. Ref.1 Ref.4

Experimental info

Sequence conflict

V → I in AAF77453. Ref.1

Sequence conflict

V → I in AAF77427. Ref.1

Sequence conflict

V → I in AAF77413. Ref.1

Sequence conflict

V → I in AFC97648. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

Q34388 [UniParc].

Last modified November 28, 2012. Version 3.
Checksum: 918CEE06A60210DC
Show »

FASTA

511

56,375

        10         20         30         40         50         60 
PRQWLFSTNH KDIGTLYFIF GAWAGMVGTS LSILIRAELG HPGALIGDDQ IYNVIVTAHA 

        70         80         90        100        110        120 
FIMIFFMVMP IMIGGFGNWL VPLMLGAPDM AFPRMNNMSF WLLPPALSLL LVSSMVENGA 

       130        140        150        160        170        180 
GTGWTVYPPL SAGIAHGGAS VDLAIFSLHL AGISSILGAV NFITTVINMR STGISLDRMP 

       190        200        210        220        230        240 
LFVWSVVITA LLLLLSLPVL AGAITMLLTD RNLNTSFFDP AGGGDPILYQ HLFWFFGHPE 

       250        260        270        280        290        300 
VYILILPGFG MISHIISQES GKKETFGSLG MIYAMLAIGL LGFIVWAHHM FTVGMDVDTR 

       310        320        330        340        350        360 
AYFTSATMII AVPTGIKIFS WLATLHGTQL SYSPAILWAL GFVFLFTVGG LTGVVLANSS 

       370        380        390        400        410        420 
VDIILHDTYY VVAHFHYVLS MGAVFAIMAG FIHWYPLFTG LTLNNKWLKS QFIIMFIGVN 

       430        440        450        460        470        480 
LTFFPQHFLG LAGMPRRYSD YPDAYTTWNV VSTIGSTISL LGILFFFYII WESLVSQRQV 

       490        500        510 
IYPIQLNSSI EWYQNTPPAE HSYSELPLLT N

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Comparative genomics of mitochondrial DNA in Drosophila simulans." Ballard J.W. J. Mol. Evol. 51:64-75(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS ILE-450 AND PHE-468. Strain: California, Hawaii, Kenya, Madagascar, New Caledonia, Reunion, Seychelles and Tahiti.
[2]	"Sequential evolution of a symbiont inferred from the host: Wolbachia and Drosophila simulans." Ballard J.W.O. Mol. Biol. Evol. 21:428-442(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Australia and Kenya.
[3]	"Paternal transmission of mitochondrial DNA as an integral part of mitochondrial inheritance in metapopulations of Drosophila simulans." Wolff J.N., Nafisinia M., Sutovsky P., Ballard J.W. Heredity 110:57-62(2013) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Kenya.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-498, VARIANTS ILE-450 AND PHE-468. Strain: Hawaii and Sl3.
[5]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-101. Strain: Nairobi.
[6]	"Comparative genomics of Drosophila mtDNA: Novel features of conservation and change across functional domains and lineages." Montooth K.L., Abt D.N., Hofmann J.W., Rand D.M. J. Mol. Evol. 69:94-114(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-10, IDENTIFICATION OF PROBABLE INITIATION SITE.
[7]	"Evolution of the mitochondrial ATPase 6 gene in Drosophila: unusually high level of polymorphism in D. melanogaster." Kaneko M., Satta Y., Matsuura E.T., Chigusa S.I. Genet. Res. 61:195-204(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 500-510.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF200833 Genomic DNA. Translation: AAF77296.1. AF200834 Genomic DNA. Translation: AAF77310.1. AF200835 Genomic DNA. Translation: AAF77324.1. AF200836 Genomic DNA. Translation: AAF77336.1. AF200837 Genomic DNA. Translation: AAF77349.1. AF200838 Genomic DNA. Translation: AAF77368.1. AF200839 Genomic DNA. Translation: AAF77376.1. AF200840 Genomic DNA. Translation: AAF77393.1. AF200841 Genomic DNA. Translation: AAF77401.1. AF200842 Genomic DNA. Translation: AAF77413.1. AF200843 Genomic DNA. Translation: AAF77427.1. AF200844 Genomic DNA. Translation: AAF77440.1. AF200845 Genomic DNA. Translation: AAF77453.1. AF200846 Genomic DNA. Translation: AAF77466.1. AF200847 Genomic DNA. Translation: AAF77478.1. AF200848 Genomic DNA. Translation: AAF77492.1. AF200849 Genomic DNA. Translation: AAF77506.1. AF200850 Genomic DNA. Translation: AAF77518.1. AF200851 Genomic DNA. Translation: AAF77532.1. AF200852 Genomic DNA. Translation: AAF77544.1. AF200853 Genomic DNA. Translation: AAF77557.1. AF200854 Genomic DNA. Translation: AAF77570.1. AY518670 Genomic DNA. Translation: AAR91400.1. AY518671 Genomic DNA. Translation: AAR91402.1. AY518672 Genomic DNA. Translation: AAR91415.1. AY518673 Genomic DNA. Translation: AAR91428.1. AY518674 Genomic DNA. Translation: AAR91441.1. JQ691660 Genomic DNA. Translation: AFC97648.1. JQ691661 Genomic DNA. Translation: AFC97661.1. M57909 Genomic DNA. Translation: AAB02284.1. M57911 Genomic DNA. Translation: AAA66247.2. M18072 Genomic DNA. Translation: AAA65482.2. S64977 Genomic DNA. Translation: AAD13955.1.
RefSeq	NP_982323.2. NC_005781.1.
3D structure databases
ProteinModelPortal	Q34388.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2760962.
KEGG	dsi:COX1.
Organism-specific databases
CTD	4512.
FlyBase	FBgn0012877. Dsim\mt:CoI.
Phylogenomic databases
KO	K02256.
ProtClustDB	MTH00153.
Enzyme and pathway databases
UniPathway	UPA00705.
Family and domain databases
Gene3D	1.20.210.10. 1 hit.
InterPro	IPR000883. Cyt_c_Oxase_su1. IPR023615. Cyt_c_Oxase_su1_BS. 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. COX1. 1 hit.
PROSITE	PS50855. COX1. 1 hit. PS00077. COX1_CUB. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

COX1_DROSI

Accession

Primary (citable) accession number: Q34388
Secondary accession number(s): H9EAT7

Q9ME63

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 15, 2002
Last sequence update:	November 28, 2012
Last modified:	May 1, 2013
This is version 84 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project

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

Preferred order of sections

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

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents