Reviewed, UniProtKB/Swiss-Prot P98003 (COX1_CRION)

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:

COI

Encoded on

Mitochondrion

Organism

Crithidia oncopelti

Taxonomic identifier

5657 [NCBI]

Taxonomic lineage

Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Crithidia

Protein attributes

Sequence length	340 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 – ›340	›340	Cytochrome c oxidase subunit 1		PRO_0000183317
Regions
	Transmembrane	18 – 38	21	Potential
	Transmembrane	42 – 62	21	Potential
	Transmembrane	66 – 86	21	Potential
	Transmembrane	100 – 120	21	Potential
	Transmembrane	148 – 168	21	Potential
	Transmembrane	186 – 206	21	Potential
	Transmembrane	237 – 257	21	Potential
	Transmembrane	279 – 299	21	Potential
	Transmembrane	305 – 325	21	Potential
Sites
	Metal binding	64	1	Iron (heme A axial ligand) Probable
	Metal binding	243	1	Copper B Probable
	Metal binding	247	1	Copper B Probable
	Metal binding	292	1	Copper B Probable
	Metal binding	293	1	Copper B Probable
Amino acid modifications
	Cross-link	243 ↔ 247		1'-histidyl-3'-tyrosine (His-Tyr) By similarity
Experimental info
	Non-terminal residue	340	1

Sequences

	Sequence		Length	Mass (Da)
	P98003-1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 65D78B06AFD07B54	FASTA	340	38,174
	10 20 30 40 50 60 MFWISLVCLS VSHKMIGMCY LLVAILCGFL GYIYSLFIRL ELSIIGCGVL FGDYQYYNVL 70 80 90 100 110 120 VTTHGLVMVF AFIMPVMMGG LVNYFVPVLS GFPDMVFPRL NNMSFWMFMG GFGALVSGLL 130 140 150 160 170 180 TEEGMGIGWT MYPTLICVDF HSSLACDFTV FAVHLLGVSS ILNSINLLGT LFCCRRKFFS 190 200 210 220 230 240 FLNWTLFIWG SLITALLLII TLPVLAGGVT LVLCDRNFNT SFYDVVGGGD LLLFQHLFWF 250 260 270 280 290 300 FGHPEVYIII IPVFGLISTM VEVLGFRCVF SSVAMIYSMI LIAILGFFVW AHHMFVVGMD 310 320 330 340 VDTRAYFGSV TVLIGLPTCI KLFNWTYSFL YTDFIIAFEA

References

[1]	Maslov D.A., Horvath A., Gwang K. II, Kolesnikov A.A. Submitted (OCT-1990) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: S-068.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X56015 Genomic DNA. Translation: CAA39490.1.
PIR	S34958.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.9.3.1. 257162.
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_CRION

Accession

Primary (citable) accession number: P98003

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	October 13, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)