Cytochrome c oxidase subunit 1 - Apis mellifera ligustica (Common honeybee)

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Reviewed, UniProtKB/Swiss-Prot P20374 (COX1_APILI)

Last modified October 13, 2009. Version 69. History...

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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:

COI

Encoded on

Mitochondrion

Organism

Apis mellifera ligustica (Common honeybee)

Taxonomic identifier

7469 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Hymenoptera › Apocrita › Aculeata › Apoidea › Apidae › Apis

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Protein attributes

Sequence length	521 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
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 – 521

521

Cytochrome c oxidase subunit 1

PRO_0000183284

Regions

Transmembrane

15 – 35

Potential

Transmembrane

61 – 81

Potential

Transmembrane

98 – 118

Potential

Transmembrane

143 – 163

Potential

Transmembrane

184 – 204

Potential

Transmembrane

232 – 252

Potential

Transmembrane

265 – 285

Potential

Transmembrane

303 – 323

Potential

Transmembrane

336 – 356

Potential

Transmembrane

383 – 403

Potential

Transmembrane

412 – 432

Potential

Transmembrane

451 – 471

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

108

F → L in strain: Isolate ligus8.

Natural variant

270

S → G in strain: Isolate ligus8.

Natural variant

271

M → I in strain: Isolate ligus2.

Natural variant

437

R → P in strain: Isolate ligus7.

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Sequences

Sequence

Length

Mass (Da)

Tools

P20374-1 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 2149417AC981CE64
Show »

FASTA

521

59,294

        10         20         30         40         50         60 
MMKWFMSTNH KNIGILYIIL ALWSGMLGSS MSLIIRMELS SPGSWISNDQ IYNTIVTSHA 

        70         80         90        100        110        120 
FLMIFFMVMP FLIGGFGNWL IPLMLGSPDM AFPRMNNISF WLLPPSLFML LLSNLFYPSP 

       130        140        150        160        170        180 
GTGWTVYPPL SAYLYHSSPS VDFAIFSLHM SGISSIMGSL NLMVTIMMMK NFSMNYDQIS 

       190        200        210        220        230        240 
LFPWSVFITA ILLIMSLPVL AGAITMLLFD RNFNTSFFDP MGGGDPILYQ HLFWFFGHPE 

       250        260        270        280        290        300 
VYILILPGFG LISHIVMNES GKKEIFGNLS MIYAMLGIGF LGFIVWAHHM FTVGLDVDTR 

       310        320        330        340        350        360 
AYFTSATMII AVPTGIKVFS WLATYHGSKL KLNISILWSL GFIMLFTIGG LTGIMLSNSS 

       370        380        390        400        410        420 
IDIILHDTYY VVGHFHYVLS MGAVFAIISS FIHWYPLITG LLLNIKWLKI QFIMMFIGVN 

       430        440        450        460        470        480 
LTFFPQHFLG LMSMPRRYSD YPDSYYCWNS ISSMGSMISL NSMIFLIFII LESLISKRML 

       490        500        510        520 
LFKFNQSSLE WLNFLPPLDH SHLEIPLLIK NLNLKSILIK F

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References

[1]	"The CO-I and CO-II region of honeybee mitochondrial DNA: evidence for variation in insect mitochondrial evolutionary rates." Crozier R.H., Crozier Y.C., Mackinlay A.G. Mol. Biol. Evol. 6:399-411(1989) [PubMed: 2559293] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Thorax.
[2]	"The mitochondrial genome of the honeybee Apis mellifera: complete sequence and genome organization." Crozier R.H., Crozier Y.C. Genetics 133:97-117(1993) [PubMed: 8417993] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Thorax.
[3]	"ND2 and CO1 mitochondrial genes in Apis mellifera L.: a molecular approach to Mediterranean populations monitoring." Marino A., Mantovani B., Carpana E., Sabatini A.G., Lodesani M. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 93-507. Strain: Isolate ligus2, Isolate ligus3, Isolate ligus4, Isolate ligus5, Isolate ligus6, Isolate ligus7, Isolate ligus8 and Isolate ligus9.
[4]	"Putative origin and function of the intergenic region between COI and COII of Apis mellifera L. mitochondrial DNA." Cornuet J.-M., Garnery L., Solignac M. Genetics 128:393-403(1991) [PubMed: 1649072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 338-521.

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Cross-references

Sequence databases
	M23409 Genomic DNA. Translation: AAA18476.1. L06178 Genomic DNA. Translation: AAB96799.1. AY114452 Genomic DNA. Translation: AAM76437.1. AY114453 Genomic DNA. Translation: AAM76438.1. AY114454 Genomic DNA. Translation: AAM76439.1. AY114455 Genomic DNA. Translation: AAM76440.1. AY114456 Genomic DNA. Translation: AAM76441.1. AY114457 Genomic DNA. Translation: AAM76442.1. AY114458 Genomic DNA. Translation: AAM76443.1. AY114460 Genomic DNA. Translation: AAM76445.1.
PIR	A32431.
RefSeq	NP_008083.1.
3D structure databases
HSSP	HSSP built from PDB template 2OCC based on UniProtKB P00396.
ModBase	Search...
Genome annotation databases
GeneID	807695.
Organism-specific databases
CTD	807695.
Enzyme and pathway databases
BRENDA	1.9.3.1. 303239.
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_APILI

Accession

Primary (citable) accession number: P20374
Secondary accession number(s): Q8LUG0

Q8LXP7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	October 13, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

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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

Natural variations

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents