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P03945 (COX1_NEUCR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 101. 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
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:cox-1
Synonyms:coi, cox1
ORF Names:NCM025, NCU16016
Encoded onMitochondrion
OrganismNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) [Reference proteome]
Taxonomic identifier367110 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora ›

Protein attributes

Sequence length557 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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.

Post-translational modification

The amino end of the mature protein may be Ser-3.

Sequence similarities

Belongs to the heme-copper respiratory oxidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 557557Cytochrome c oxidase subunit 1
PRO_0000183366

Regions

Transmembrane22 – 4221Helical; Potential
Transmembrane69 – 8921Helical; Potential
Transmembrane106 – 12621Helical; Potential
Transmembrane151 – 17121Helical; Potential
Transmembrane187 – 20721Helical; Potential
Transmembrane240 – 26021Helical; Potential
Transmembrane272 – 29221Helical; Potential
Transmembrane310 – 33021Helical; Potential
Transmembrane343 – 36321Helical; Potential
Transmembrane378 – 39821Helical; Potential
Transmembrane418 – 43821Helical; Potential
Transmembrane457 – 47721Helical; Potential

Sites

Metal binding671Iron (heme A axial ligand) Probable
Metal binding2461Copper B Probable
Metal binding2501Copper B Probable
Metal binding2951Copper B Probable
Metal binding2961Copper B Probable
Metal binding3811Iron (heme A3 axial ligand) Probable
Metal binding3831Iron (heme A axial ligand) Probable

Amino acid modifications

Lipidation3241N6-myristoyl lysine Ref.7
Cross-link246 ↔ 2501'-histidyl-3'-tyrosine (His-Tyr) By similarity

Experimental info

Sequence conflict5271V → A in CAA25976. Ref.1
Sequence conflict5271V → A in CAA28195. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P03945 [UniParc].

Last modified December 14, 2011. Version 2.
Checksum: 8AC9618704E5C91D

FASTA55761,522
        10         20         30         40         50         60 
MSSISIWTER WFLSTNAKDI GVLYLIFALF SGLLGTAFSV LIRMELSGPG VQYIADNQLY 

        70         80         90        100        110        120 
NAIITAHAIL MIFFMVMPAL IGGFGNFLLP LLVGGPDMAF PRLNNISFWL LPPSLLLLVF 

       130        140        150        160        170        180 
SACIEGGAGT GWTIYPPLSG VQSHSGPSVD LAIFALHLSG VSSLLGSINF ITTIVNMRTP 

       190        200        210        220        230        240 
GIRLHKLALF GWAVVITAVL LLLSLPVLAG AITMLLTDRN FNTSFFETAG GGDPILFQHL 

       250        260        270        280        290        300 
FWFFGHPEVY ILIIPGFGII STTISAYSNK SVFGYIGMVY AMMSIGILGF IVWSHHMYTV 

       310        320        330        340        350        360 
GLDVDTRAYF TAATLIIAVP TGIKIFSWLA TCYGGSIRLT PSMLFALGFV FMFTIGGLSG 

       370        380        390        400        410        420 
VVLANASLDI AFHDTYYVVA HFHYVLSMGA VFAMFSGWYH WVPKILGLNY NMVLSKAQFW 

       430        440        450        460        470        480 
LLFIGVNLTF FPQHFLGLQG MPRRISDYPD AFSGWNLISS FGSIVSVVAS WLFLYIVYIQ 

       490        500        510        520        530        540 
LVQGEYAGRY PWSIPQFYTD SLRALLNRSY PSLEWSISSP PKPHSFVSLP LQSSSFFLSF 

       550 
FRLSSYGEQK EISGRQN

« Hide

References

« Hide 'large scale' references
[1]"Subunit 1 of cytochrome oxidase from Neurospora crassa: nucleotide sequence of the coding gene and partial amino acid sequence of the protein."
Burger G., Scriven C., Machleidt W., Werner S.
EMBO J. 1:1385-1391(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 3-99; 234-285; 346-354; 443-489 AND 494-521.
[2]"The structure of the gene for subunit I of cytochrome c oxidase in Neurospora crassa mitochondria."
de Jonge J.C., de Vries H.
Curr. Genet. 7:21-28(1983)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"A group II intron in the Neurospora mitochondrial coI gene: nucleotide sequence and implications for splicing and molecular evolution."
Field D.J., Sommerfield A., Saville B.J., Collins R.A.
Nucleic Acids Res. 17:9087-9099(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Adiopodoume / FGSC 430.
[4]"The genome sequence of the filamentous fungus Neurospora crassa."
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. expand/collapse author list , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[5]"Mitochondrial genetics of Neurospora."
Kennell J.C., Collins R.A., Griffiths A.J.F., Nargang F.E.
(In) Kueck U. (eds.); The Mycota II, Genetics and Biotechnology (2nd edition), pp.95-112, Springer-Verlag, Berlin-Heidelberg (2004)
Cited for: GENOME REANNOTATION.
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[6]"Mitochondrial gene URFN of Neurospora crassa codes for a long polypeptide with highly repetitive structure."
Burger G., Werner S.
J. Mol. Biol. 191:589-599(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 519-557.
[7]"Cytochrome c oxidase in Neurospora crassa contains myristic acid covalently linked to subunit 1."
Vassilev A.O., Plesofsky-Vig N., Brambl R.
Proc. Natl. Acad. Sci. U.S.A. 92:8680-8684(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: MYRISTOYLATION AT LYS-324.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X01850 Genomic DNA. Translation: CAA25976.1.
M36958 Genomic DNA. No translation available.
X14669 Genomic DNA. Translation: CAA32799.1.
X04512 Genomic DNA. Translation: CAA28195.1.
PIRODNC1. A00469.

3D structure databases

ProteinModelPortalP03945.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

OrthoDBEOG4BK8C4.

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. COX1. 1 hit.
PROSITEPS50855. COX1. False negative.
PS00077. COX1_CUB. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX1_NEUCR
AccessionPrimary (citable) accession number: P03945
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 1986
Last sequence update: December 14, 2011
Last modified: April 3, 2013
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents