Cytochrome c oxidase subunit 2 - Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)

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P00411 (COX2_NEUCR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 96. History...

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

Documents (1) |

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 2
EC=1.9.3.1

Alternative name(s):
Cytochrome c oxidase polypeptide II

Gene names

Name:	cox-2
Synonyms:	cox2, oxi1
ORF Names:	NCM018, NCU16028

Encoded on

Mitochondrion

Organism

Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) [Reference proteome]

Taxonomic identifier

367110 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora ›

Protein attributes

Sequence length	250 AA.
Sequence status	Complete.
Protein existence	Inferred 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. Subunit 2 transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit 1.
Catalytic activity	4 ferrocytochrome c + O₂ + 4 H⁺ = 4 ferricytochrome c + 2 H₂O.
Cofactor	Copper A.
Subcellular location	Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the cytochrome c oxidase subunit 2 family.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transmembrane Transmembrane helix
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW
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	copper ion binding Inferred from electronic annotation. Source: InterPro cytochrome-c oxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 250

250

Cytochrome c oxidase subunit 2

PRO_0000183638

Regions

Topological domain

1 – 39

Mitochondrial intermembrane Potential

Transmembrane

40 – 59

Helical; Potential

Topological domain

60 – 76

Mitochondrial matrix Potential

Transmembrane

77 – 97

Helical; Potential

Topological domain

98 – 250

153

Mitochondrial intermembrane Potential

Sites

Metal binding

185

Copper A Probable

Metal binding

220

Copper A Probable

Metal binding

224

Copper A Probable

Metal binding

228

Copper A Probable

Experimental info

Sequence conflict

G → V in AAA31959. Ref.1

Sequence conflict

G → V in CAA32813. Ref.4

Sequence conflict

186

S → D in AAA31959. Ref.1

Sequence conflict

201

G → R in AAA31959. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P00411 [UniParc].

Last modified December 14, 2011. Version 2.
Checksum: 7F8C8642EFAAB013
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FASTA

250

28,555

        10         20         30         40         50         60 
MGLLFNNLIM NFDAPSPWGI YFQDSATPQM EGLVELHDNI MYYLVVILFG VGWILLSIIR 

        70         80         90        100        110        120 
NYISTKSPIS HKYLNHGTLI ELIWTITPAV ILILIAFPSF KLLYLMDEVS DPSMSVLAEG 

       130        140        150        160        170        180 
HQWYWSYQYP DFLDSNDEFI EFDSYIVPES DLEEGALRML EVDNRVILPE LTHVRFIITA 

       190        200        210        220        230        240 
GDVIHSFAVP SLGVKCDAYP GRLNQVSVFI NREGVFYGQC SEICGILHSS MPIVIESVSL 

       250 
EKFLTWLEEQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cytochrome oxidase subunit 2 gene in Neurospora crassa mitochondria." Macino G., Morelli G. J. Biol. Chem. 258:13230-13235(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[2]	"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. 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.
[3]	"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.
[4]	"Molecular characterization of the mitochondrial DNA of a new stopper mutant ER-3 of Neurospora crassa." Almasan A., Mishra N.C. Genetics 120:935-945(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-65. Strain: RL3-8A.
[5]	"The mitochondrially made subunit 2 of Neurospora crassa cytochrome aa3 is synthesized as a precursor protein." van den Boogaart P., van Dijk S., Agsteribbe E. FEBS Lett. 147:97-100(1982) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-54. Strain: ANT-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	K00825 Genomic DNA. Translation: AAA31959.2. X14681 Genomic DNA. Translation: CAA32813.1. J01429 Genomic DNA. No translation available.
PIR	OBNC2. A00479.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
OrthoDB	EOG4ZW8M5.
Family and domain databases
Gene3D	1.10.287.90. 1 hit. 2.60.40.420. 1 hit.
InterPro	IPR001505. Copper_CuA. IPR008972. Cupredoxin. IPR014222. Cyt_c_oxidase_su2. IPR002429. Cyt_c_oxidase_su2_C. IPR011759. Cyt_c_oxidase_su2_TM_dom. [Graphical view]
Pfam	PF00116. COX2. 1 hit. PF02790. COX2_TM. 1 hit. [Graphical view]
SUPFAM	SSF49503. Cupredoxin. 1 hit. SSF81464. Cyt_c_oxidase_II-like_TM. 1 hit.
TIGRFAMs	TIGR02866. CoxB. 1 hit.
PROSITE	PS00078. COX2. False negative. PS50857. COX2_CUA. False negative. PS50999. COX2_TM. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

COX2_NEUCR

Accession

Primary (citable) accession number: P00411

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	December 14, 2011
Last modified:	May 1, 2013
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

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

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents