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P20681 (COX1_PODAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytochrome c oxidase subunit 1

EC=1.9.3.1
Alternative name(s):
Cytochrome c oxidase polypeptide I
Gene names
Name:COI
Synonyms:CO1
Encoded onMitochondrion
OrganismPodospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina) [Complete proteome]
Taxonomic identifier515849 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesLasiosphaeriaceaePodospora

Protein attributes

Sequence length541 AA.
Sequence statusComplete.
Protein existenceInferred 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 541541Cytochrome c oxidase subunit 1
PRO_0000183397

Regions

Transmembrane23 – 4321Helical; Potential
Transmembrane70 – 9021Helical; Potential
Transmembrane107 – 12721Helical; Potential
Transmembrane152 – 17221Helical; Potential
Transmembrane188 – 20821Helical; Potential
Transmembrane241 – 26121Helical; Potential
Transmembrane273 – 29321Helical; Potential
Transmembrane311 – 33121Helical; Potential
Transmembrane344 – 36421Helical; Potential
Transmembrane383 – 40321Helical; Potential
Transmembrane418 – 43821Helical; Potential
Transmembrane458 – 47821Helical; Potential

Sites

Metal binding681Iron (heme A axial ligand) Probable
Metal binding2471Copper B Probable
Metal binding2511Copper B Probable
Metal binding2961Copper B Probable
Metal binding2971Copper B Probable
Metal binding3821Iron (heme A3 axial ligand) Probable
Metal binding3841Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link247 ↔ 2511'-histidyl-3'-tyrosine (His-Tyr) By similarity

Experimental info

Sequence conflict231N → T no nucleotide entry Ref.2
Sequence conflict231N → T in CAA30131. Ref.4
Sequence conflict511S → G no nucleotide entry Ref.2
Sequence conflict511S → G in CAA30131. Ref.4
Sequence conflict4141T → I in AAA32001. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P20681 [UniParc].

Last modified July 1, 1993. Version 2.
Checksum: 06AF3D497D03DAF2

FASTA54159,737
        10         20         30         40         50         60 
MSGGVSLWIE RWMLSTNAKD IGNLYLIFAL FSGLLGTAFS VLIRMELSGP SVQYIADNQL 

        70         80         90        100        110        120 
YNSIITAHAL LMIFFMVMPA LIGGFGNFLL PLLVGGPDMA FPRLNNISFW LLPPSLILLV 

       130        140        150        160        170        180 
FSACIEGGAG TGWTIYPPLS GVQSHSGPSV DLAIFALHLS GVSSLLGAMN FITTIMNMRT 

       190        200        210        220        230        240 
PSIRLHKLAL FGWAVIITAV LLLLSLPVLA GAITMLLTDR NFNTSFFETA GGGDPILFQH 

       250        260        270        280        290        300 
LFWFFGHPEV YILIIPAFGI ISTTISAYSN KSVFGYIGMV YAMMSIGILG FIVWSHHMYT 

       310        320        330        340        350        360 
VGLDVDTRAY FTAATLIIAV PTGIKIFSWL ATCYGGSIRL TPSMLFALGF VFMFTIGGLS 

       370        380        390        400        410        420 
GVVLANASLD IAFHDTYYVV AHFHYVLSMG AVFAMFSGWY FWIPKMLGLN YNMTLSKVQF 

       430        440        450        460        470        480 
WILFIGVNVT FFPQHFLGLQ GMPRRISDYP DAFAGWNLIS SFGSIISVVA AWLFLYIVYL 

       490        500        510        520        530        540 
QLVEGEYAGR FPWLNPQFYT DTLQALLNRS YPSLEWALSS PPKPHAFVSL PLQSNILRSL 


F 

« Hide

References

« Hide 'large scale' references
[1]"DNA sequence analysis of the 24.5 kilobase pair cytochrome oxidase subunit I mitochondrial gene from Podospora anserina: a gene with sixteen introns."
Cummings D.J., Michel F., McNally K.L.
Curr. Genet. 16:381-406(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete DNA sequence of the mitochondrial genome of Podospora anserina."
Cummings D.J., McNally K.L., Domenico J.M., Matsuura E.T.
Curr. Genet. 17:375-402(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: s.
[3]"Senescence in Podospora anserina: a possible role for nucleic acid interacting proteins suggested by the sequence analysis of a mitochondrial DNA region specifically amplified in senescent cultures."
Vierny-Jamet C.
Gene 74:387-398(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 376-541.
Strain: s.
[4]"The onset of senescence is affected by DNA rearrangements of a discontinuous mitochondrial gene in Podospora anserina."
Kueck U., Osiewacz H.D., Schmidt U., Kappelhoff B., Schulte E., Stahl U., Esser K.
Curr. Genet. 9:373-382(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-86 AND 212-242.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X55026 Genomic DNA. Translation: CAA38777.1.
M28703 Genomic DNA. Translation: AAA32001.2.
X07119, X07120 Genomic DNA. Translation: CAA30131.1.
X07121 Genomic DNA. Translation: CAA30132.1.
PIRA48327.
RefSeqNP_074924.1. NC_001329.3.

3D structure databases

ProteinModelPortalP20681.
SMRP20681. Positions 7-527.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID802462.
KEGGpan:PoanfMp17.

Phylogenomic databases

KOK02256.

Enzyme and pathway databases

UniPathwayUPA00705.

Family and domain databases

Gene3D1.20.210.10. 1 hit.
InterProIPR000883. Cyt_c_Oxase_su1.
IPR023615. Cyt_c_Oxase_su1_BS.
IPR023616. Cyt_c_Oxase_su1_dom.
[Graphical view]
PANTHERPTHR10422. PTHR10422. 1 hit.
PfamPF00115. COX1. 1 hit.
[Graphical view]
PRINTSPR01165. CYCOXIDASEI.
SUPFAMSSF81442. SSF81442. 1 hit.
PROSITEPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX1_PODAN
AccessionPrimary (citable) accession number: P20681
Secondary accession number(s): O21208, Q35363
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 1, 1993
Last modified: April 16, 2014
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways