Q33375 (COX1_CANSI) Reviewed, UniProtKB/Swiss-Prot

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) (Simenia simensis)

Taxonomic identifier

32534 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis

Protein attributes

Sequence length	196 AA.
Sequence status	Fragment.
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 Transmembrane helix
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 oxidative phosphorylation Inferred from electronic annotation. Source: UniProtKB-UniPathway
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	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 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 – ›196	›196	Cytochrome c oxidase subunit 1		PRO_0000183301
Regions
	Transmembrane	9 – 29	21	Helical; Potential
	Transmembrane	34 – 54	21	Helical; Potential
	Transmembrane	76 – 96	21	Helical; Potential
	Transmembrane	104 – 124	21	Helical; Potential
	Transmembrane	146 – 166	21	Helical; Potential
	Transmembrane	176 – 196	21	Helical; 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 [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	L29413 Genomic DNA. Translation: AAA53663.2. Sequence problems.
3D structure databases
ProteinModelPortal	Q33375.
SMR	Q33375. Positions 2-196.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00705.
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...

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:	April 3, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program