Cytochrome c oxidase subunit 1 - Caenorhabditis elegans

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P24893 (COX1_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 101. 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:	cox-1
Synonyms:	coI
ORF Names:	MTCE.26

Encoded on

Mitochondrion

Organism

Caenorhabditis elegans [Reference proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Ecdysozoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	525 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.

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 Reference proteome
Gene Ontology (GO)
Biological_process	aerobic respiration Inferred from electronic annotation. Source: InterPro mitochondrial electron transport, cytochrome c to oxygen Non-traceable author statement Ref.2. Source: UniProtKB
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial inner membrane Non-traceable author statement Ref.2. Source: UniProtKB respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	cytochrome-c oxidase activity Non-traceable author statement Ref.2. Source: UniProtKB 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 – 525

525

Cytochrome c oxidase subunit 1

PRO_0000183298

Regions

Transmembrane

25 – 45

Helical; Potential

Transmembrane

71 – 91

Helical; Potential

Transmembrane

108 – 128

Helical; Potential

Transmembrane

152 – 172

Helical; Potential

Transmembrane

190 – 210

Helical; Potential

Transmembrane

241 – 261

Helical; Potential

Transmembrane

274 – 294

Helical; Potential

Transmembrane

317 – 337

Helical; Potential

Transmembrane

344 – 364

Helical; Potential

Transmembrane

387 – 407

Helical; Potential

Transmembrane

420 – 440

Helical; Potential

Transmembrane

459 – 479

Helical; Potential

Sites

Metal binding

Iron (heme A axial ligand) Probable

Metal binding

247

Copper B Probable

Metal binding

251

Copper B Probable

Metal binding

297

Copper B Probable

Metal binding

298

Copper B Probable

Metal binding

383

Iron (heme A3 axial ligand) Probable

Metal binding

385

Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link

247 ↔ 251

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

Natural variations

Natural variant

A → S in strain: CB4856 and CB4857. Ref.1

Natural variant

466

I → M in strain: AB1, AB2, CB4852, CB4853, CB4855, CB4857, CB4858, KR314 and PB306. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P24893 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: E3D051208B09396F
Show »

FASTA

525

58,464

        10         20         30         40         50         60 
MNLYKKYQGG LAVWLESSNH KDIGTLYFIF GLWSGMVGTS FSLLIRLELA KPGFFLSNGQ 

        70         80         90        100        110        120 
LYNSVITAHA ILMIFFMVMP TMIGGFGNWL LPLMLGAPDM SFPRLNNLSF WLLPTSMLLI 

       130        140        150        160        170        180 
LDACFVDMGC GTSWTVYPPL STMGHPGSSV DLAIFSLHAA GLSSILGGIN FMCTTKNLRS 

       190        200        210        220        230        240 
SSISLEHMTL FVWTVFVTVF LLVLSLPVLA GAITMLLTDR NLNTSFFDPS TGGNPLIYQH 

       250        260        270        280        290        300 
LFWFFGHPEV YILILPAFGI VSQSTLYLTG KKEVFGALGM VYAILSIGLI GCVVWAHHMY 

       310        320        330        340        350        360 
TVGMDLDSRA YFSAATMVIA VPTGVKVFSW LATLFGMKMV FNPLLLWVLG FIFLFTLGGL 

       370        380        390        400        410        420 
TGVVLSNSSL DIILHDTYYV VSHFHYVLSL GAVFGIFTGV TLWWSFITGY VLDKLMMSAV 

       430        440        450        460        470        480 
FILLFIGVNL TFFPLHFAGL HGFPRKYLDY PDVYSVWNII ASYGSIISTA GLFLFIYVLL 

       490        500        510        520 
ESFFSYRLVI SDYYSNSSPE YCMSNYVFGH SYQSEIYFST TSLKN

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Phylogenetics in Caenorhabditis elegans: an analysis of divergence and outcrossing." Denver D.R., Morris K., Thomas W.K. Mol. Biol. Evol. 20:393-400(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-12 AND MET-466. Strain: AB1, AB2, Bristol N2, CB4852, CB4853, CB4854, CB4855, CB4856, CB4857, CB4858, KR314, PB303, PB306, RW7000 and TR403.
[2]	"The mitochondrial genomes of two nematodes, Caenorhabditis elegans and Ascaris suum." Okimoto R., Macfarlane J.L., Clary D.O., Wolstenholme D.R. Genetics 130:471-498(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[3]	"Evidence for the frequent use of TTG as the translation initiation codon of mitochondrial protein genes in the nematodes, Ascaris suum and Caenorhabditis elegans." Okimoto R., Macfarlane J.L., Wolstenholme D.R. Nucleic Acids Res. 18:6113-6118(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY171193 Genomic DNA. Translation: AAO16252.1. AY171194 Genomic DNA. Translation: AAO16256.1. AY171195 Genomic DNA. Translation: AAO16260.1. AY171196 Genomic DNA. Translation: AAO16264.1. AY171197 Genomic DNA. Translation: AAO16268.1. AY171198 Genomic DNA. Translation: AAO16272.1. AY171199 Genomic DNA. Translation: AAO16276.1. AY171200 Genomic DNA. Translation: AAO16280.1. AY171201 Genomic DNA. Translation: AAO16284.1. AY171202 Genomic DNA. Translation: AAO16288.1. AY171203 Genomic DNA. Translation: AAO16292.1. AY171204 Genomic DNA. Translation: AAO16296.1. AY171205 Genomic DNA. Translation: AAO16300.1. AY171206 Genomic DNA. Translation: AAO16304.1. AY171207 Genomic DNA. Translation: AAO16308.1. X54252 Genomic DNA. Translation: CAA38159.1.
PIR	S26034.
RefSeq	NP_006961.1. NC_001328.1.
3D structure databases
ProteinModelPortal	P24893.
SMR	P24893. Positions 14-501.
ModBase	Search...
Protein-protein interaction databases
IntAct	P24893. 1 interaction.
STRING	6239.MTCE.26.
Proteomic databases
PaxDb	P24893.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2565700.
KEGG	cel:COX1.
Organism-specific databases
CTD	4512.
Phylogenomic databases
eggNOG	COG0843.
HOGENOM	HOG000085274.
KO	K02256.
ProtClustDB	MTH00079.
Enzyme and pathway databases
UniPathway	UPA00705.
Gene expression databases
ArrayExpress	P24893.
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...
Other
NextBio	953875.

Entry information

Entry name

COX1_CAEEL

Accession

Primary (citable) accession number: P24893

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	November 1, 1995
Last modified:	April 3, 2013
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase

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

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents