Reviewed, UniProtKB/Swiss-Prot O03521 (COX1_CASBE)

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

Casuarius bennetti (Dwarf cassowary)

Taxonomic identifier

30463 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Palaeognathae › Casuariiformes › Casuariidae › Casuarius

Protein attributes

Sequence length	337 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-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: 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 – ›337	›337	Cytochrome c oxidase subunit 1		PRO_0000183304
Regions
	Transmembrane	18 – 38	21	Potential
	Transmembrane	57 – 77	21	Potential
	Transmembrane	103 – 123	21	Potential
	Transmembrane	146 – 166	21	Potential
	Transmembrane	184 – 204	21	Potential
	Transmembrane	235 – 255	21	Potential
	Transmembrane	269 – 289	21	Potential
	Transmembrane	311 – 331	21	Potential
Sites
	Metal binding	62	1	Iron (heme A axial ligand) Probable
	Metal binding	241	1	Copper B Probable
	Metal binding	245	1	Copper B Probable
	Metal binding	291	1	Copper B Probable
	Metal binding	292	1	Copper B Probable
Amino acid modifications
	Cross-link	241 ↔ 245		1'-histidyl-3'-tyrosine (His-Tyr) By similarity
Experimental info
	Non-terminal residue	337	1

Sequences

	Sequence		Length	Mass (Da)
	O03521-1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 92A8EBB2E2264C02	FASTA	337	36,766
	10 20 30 40 50 60 MTFITRWLFS TNHKDIGTLY LIFGAWAGMV GTALSLLIRA ELGQPGTLLG DDQIYNVIVT 70 80 90 100 110 120 AHAFVMIFFM VMPVMIGGFG NWLVPLMIGA PDMAFPRMNN MSFWLLPPSF LLLLASSTVE 130 140 150 160 170 180 AGAGTGWTVY PPLAGNLAHA GASVDLAIFS LHLAGVSSIL GAINFITTAI NMKPPALTQY 190 200 210 220 230 240 QTPLFVWSVL ITAILLLLSL PVLAAGITML LTDRNLNTTF FDPAGGGDPV LYQHLFWFFG 250 260 270 280 290 300 HPEVYILILP GFGMISHVVT YYAGKKEPFG YMGMVWAMLS IGFLGFIVWA HHMFTVGMDV 310 320 330 DTRAYFTSAT MIIAIPTGIK VFSWLATLHG GTIKWDP

References

[1]

"Phylogenetic relationships of the ratite birds: resolving conflicts between molecular and morphological data sets." Lee K., Feinstein J., Cracraft J. (In) Mindell D.P. (eds.); Avian molecular evolution and systematics, pp.1-1, Academic Press, New York (1997) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	U76058 Genomic DNA. Translation: AAB61316.1.
3D structure databases
HSSP	HSSP built from PDB template 1FFT based on UniProtKB P18401.
SMR	O03521. Positions 3-337.
ModBase	Search...
Phylogenomic databases
HOVERGEN	O03521.
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_CASBE

Accession

Primary (citable) accession number: O03521

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	July 1, 1997
Last modified:	June 16, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)