[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=AX3; DOI=10.1007/s002940050179; PubMed=9000384 [NCBI, ExPASy, EBI, Israel, Japan] Ogawa S., Matsuo K., Angata K., Yanagisawa K., Tanaka Y.; "Group-I introns in the cytochrome c oxidase genes of Dictyostelium discoideum: two related ORFs in one loop of a group-I intron, a cox1/2 hybrid gene and an unusually large cox3 gene."; Curr. Genet. 31:80-88(1997).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=AX3; DOI=10.1007/s004380051196; PubMed=10821186 [NCBI, ExPASy, EBI, Israel, Japan] Ogawa S., Yoshino R., Angata K., Iwamoto M., Pi M., Kuroe K., Matsuo K., Morio T., Urushihara H., Yanagisawa K., Tanaka Y.; "The mitochondrial DNA of Dictyostelium discoideum: complete sequence, gene content and genome organization."; Mol. Gen. Genet. 263:514-519(2000).
[3]	NUCLEOTIDE SEQUENCE [MRNA] OF 83-205. STRAIN=AX3; Mueller-Taubenberger A.; "Dictyostelium discoideum Ddmco gene sequence."; Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 259-764. STRAIN=AX3; DOI=10.1016/S0005-2728(97)00010-8; PubMed=9186775 [NCBI, ExPASy, EBI, Israel, Japan] Pellizzari R., Anjard C., Bisson R.; "Subunits I and II of Dictyostelium cytochrome c oxidase are specified by a single open reading frame transcribed into a large polycistronic RNA."; Biochim. Biophys. Acta 1320:1-7(1997).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 259-341. STRAIN=AX2; Anjard C., Reymond C.D.; Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.

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 (By similarity).
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.
SIMILARITY: In the N-terminal section; belongs to the heme-copper respiratory oxidase family.
SIMILARITY: In the C-terminal section; belongs to the cytochrome c oxidase subunit 2 family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D50297; BAA21123.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB000109; BAA78055.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U87391; AAB42021.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X81884; CAA57467.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X95896; CAA65139.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T43751; T43751.

RefSeq

NP_050073.1; -.

3D structure databases

HSSP

P98002; 1AR1. [HSSP ENTRY / PDB]

ModBase

O21042.

Organism-specific databases

dictyBase

DDB_G0294088; cox1/2.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from InterPro).
GO:0005746;	Cellular component: mitochondrial respiratory chain (inferred from electronic annotation from UniProtKB-KW).
GO:0005507;	Molecular function: copper ion binding (inferred from electronic annotation from InterPro).
GO:0004129;	Molecular function: cytochrome-c oxidase activity (inferred from electronic annotation from InterPro).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from dictyBase).
GO:0009060;	Biological process: aerobic respiration (inferred from electronic annotation from InterPro).
GO:0022904;	Biological process: respiratory electron transport chain (inferred from electronic annotation from InterPro).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001505; Copper_CuA.
IPR000883; COX1.
IPR014222; COX2.
IPR002429; COX2_C.
IPR008972; Cupredoxin.
IPR011759; Cyt_c_oxidase_II_TM.
Graphical view of domain structure.

Gene3D

G3DSA:1.20.210.10; COX1; 1.
G3DSA:1.10.287.90; COX2_TM; 1.
G3DSA:2.60.40.420; Cupredoxin; 1.

PANTHER

PTHR10422; COX1; 1.

Pfam

PF00115; COX1; 1.
PF00116; COX2; 1.
PF02790; COX2_TM; 1.
Pfam graphical view of domain structure.

PRINTS

PR01165; CYCOXIDASEI.
PR01166; CYCOXIDASEII.

ProDom

PD000131; Copper_CuA; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR02866; CoxB; 1.

PROSITE

PS50855; COX1; 1.
PS00077; COX1_CUB; 1.
PS00078; COX2; 1.
PS50857; COX2_CUA; 1.
PS50999; COX2_TM; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

2193894; -.

Other

ProtoNet

O21042.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Copper; Electron transport; Heme; Iron; Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; Respiratory chain; Transmembrane; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 764`	`764`	`Cytochrome c oxidase subunit 1+2.`	`PRO_0000312383`
`TRANSMEM`	`36 56`	`21`	`Potential.`
`TRANSMEM`	`82 102`	`21`	`Potential.`
`TRANSMEM`	`121 141`	`21`	`Potential.`
`TRANSMEM`	`164 184`	`21`	`Potential.`
`TRANSMEM`	`202 222`	`21`	`Potential.`
`TRANSMEM`	`253 273`	`21`	`Potential.`
`TRANSMEM`	`285 305`	`21`	`Potential.`
`TRANSMEM`	`329 349`	`21`	`Potential.`
`TRANSMEM`	`356 376`	`21`	`Potential.`
`TRANSMEM`	`390 410`	`21`	`Potential.`
`TRANSMEM`	`438 458`	`21`	`Potential.`
`TRANSMEM`	`477 497`	`21`	`Potential.`
`TRANSMEM`	`545 565`	`21`	`Potential.`
`TRANSMEM`	`594 614`	`21`	`Potential.`
`REGION`	`1 485`	`485`	`COX1.`
`REGION`	`486 764`	`279`	`COX2.`
`METAL`	`80 80`		`Iron (heme A axial ligand) (By similarity).`
`METAL`	`259 259`		`Copper B (By similarity).`
`METAL`	`263 263`		`Copper B (By similarity).`
`METAL`	`308 308`		`Copper B (By similarity).`
`METAL`	`309 309`		`Copper B (By similarity).`
`METAL`	`394 394`		`Iron (heme A3 axial ligand) (By similarity).`
`METAL`	`396 396`		`Iron (heme A axial ligand) (By similarity).`
`METAL`	`699 699`		`Copper A (By similarity).`
`METAL`	`734 734`		`Copper A (By similarity).`
`METAL`	`738 738`		`Copper A (By similarity).`
`METAL`	`742 742`		`Copper A (By similarity).`
`CROSSLNK`	`259 263`		`1'-histidyl-3'-tyrosine (His-Tyr) (By similarity).`
`CONFLICT`	`83 89`		`IMIFFVV -> MKVFMNC (in Ref. 3; AAB42021).`
`CONFLICT`	`104 104`		`I -> II (in Ref. 3; AAB42021).`
`CONFLICT`	`198 198`		`S -> P (in Ref. 3; AAB42021).`
`CONFLICT`	`259 259`		`H -> D (in Ref. 5; CAA65139).`

Sequence information

Length: 764 AA [This is the length of the unprocessed precursor]

Molecular weight: 85501 Da [This is the MW of the unprocessed precursor]

CRC64: BF363A039A0BA912 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKILEIYDKQ IAEKEGNIFI FISKWIISVD HKNIGTMYTN FSILAGIVGT LLSLVIRMEL 

        70         80         90        100        110        120 
STGNMLDGDG QQYNVIVTAH GLIMIFFVVM PAMLGGFANW FIPIMVGSPD VAFPRLNNIS 

       130        140        150        160        170        180 
LWLIIVSFFL LLTSSCVGIG VGTGWTVYPP LSTMEYHPGH AVDVGILSLH IAGASSLLGA 

       190        200        210        220        230        240 
INFLTTVFNM KIAGLSWSKV SLFVWSILIT AVLLVLSLPV LAGGLTMLIT DRNFETTFFD 

       250        260        270        280        290        300 
PIGGGDPILY QHLFWFFGHP EVYILILPGF GLVSIILSKY SNKGIFGVKG MISAMSAIGF 

       310        320        330        340        350        360 
LGFLVWAHHM YTVGLDVDTR AYFTAATMII AIPTGIKIFS WLATLWGGVI KITTPMLFVI 

       370        380        390        400        410        420 
GFLVLFTIGG LTGVVLANGG LDISLHDTYY VVAHFHYVLS MGAIFAIFAG YYYYYSIMNS 

       430        440        450        460        470        480 
TRLFGVVRYN EQLGRIHFWT MFIGVNVTFF PMHFLGLAGM PRRIGDYPDA YIGWNLIASY 

       490        500        510        520        530        540 
GSLITAFGLL FFVVNIFTPY IRRSVNIKNG AIILMGLDFA RDWQIGFQDP ATPIMEGIID 

       550        560        570        580        590        600 
LHNYIFFYLI VVAVFIGWVM GRILWRFSYK WSYPTIGDIE IFKNFTAYNQ IIHGTVIEIV 

       610        620        630        640        650        660 
WTLIPTVILY LIAIPSFTLL YAMDEIINPT VTIKIIGHQW YWSYEYGDNA SNLIEFDSYM 

       670        680        690        700        710        720 
VYERDLAEGQ LRLLEVDNAM VVPVKTHIRL IITSGDVLHS WAIPSFGIKV DAVPGRLNQI 

       730        740        750        760 
GLYVKREGTF YGQCSELCGV DHGFMPIKVQ AVKLGEYFSK LNEK

O21042 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools