Reviewed, UniProtKB/Swiss-Prot Q33375 (COX1_CANSI)

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:	MT-CO1
Synonyms:	COI, COXI, MTCO1

Encoded on

Mitochondrion

Organism

Canis simensis (Ethiopian wolf)

Taxonomic identifier

32534 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis

Protein attributes

Sequence length	196 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
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. 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
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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – ›196	›196	Cytochrome c oxidase subunit 1		PRO_0000183301
Regions
	Transmembrane	9 – 29	21	Potential
	Transmembrane	34 – 54	21	Potential
	Transmembrane	76 – 96	21	Potential
	Transmembrane	104 – 124	21	Potential
	Transmembrane	146 – 166	21	Potential
	Transmembrane	176 – 196	21	Potential
Sites
	Metal binding	6	1	Copper B Probable
	Metal binding	10	1	Copper B Probable
	Metal binding	56	1	Copper B Probable
	Metal binding	57	1	Copper B Probable
	Metal binding	142	1	Iron (heme A3 axial ligand) Probable
	Metal binding	144	1	Iron (heme A axial ligand) Probable
Amino acid modifications
	Cross-link	6 ↔ 10		1'-histidyl-3'-tyrosine (His-Tyr) By similarity
Experimental info
	Non-terminal residue	1	1
	Non-terminal residue	196	1

Sequences

	Sequence		Length	Mass (Da)
	Q33375-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 8C5CE47EC8CE515C	FASTA	196	22,107
	10 20 30 40 50 60 XWFFGHPEVY ILILPGFGMI SHIVTYYSGK KEPFGYMGMV WAMMSIGFLG FIVWAHHMFT 70 80 90 100 110 120 VGMDVDTRAY FTSATMIIAI PTGVKVFSWL ATLHGGNIKW SPAMLWALGF IFLFTVGGLT 130 140 150 160 170 180 GIVLANSSLD IVLHDTYYVV AHFHYVLSMG AVFAIMGGFA HWFPLFSGYT LNDTWAKIHF 190 TIMFVGVNMT FFPQHF

References

[1]

"Molecular genetics of the most endangered canid: the Ethiopian wolf Canis simensis." Gottelli D., Sillero-Zubiri C., Applebaum G.D., Roy M.S., Girman D.J., Garcia-Moreno J., Ostrander E.A., Wayne R.K. Mol. Ecol. 3:301-312(1994) [PubMed: 7921357] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	L29413 Genomic DNA. Translation: AAA53663.2. Sequence problems.
3D structure databases
SMR	Q33375. Positions 2-196.
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q33375.
Enzyme and pathway databases
BRENDA	1.9.3.1. 301264.
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...

Entry information

Entry name

COX1_CANSI

Accession

Primary (citable) accession number: Q33375

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	October 13, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)