[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=7498775 [NCBI, ExPASy, EBI, Israel, Japan] Hatzoglou E., Rodakis G.C., Lecanidou R.; "Complete sequence and gene organization of the mitochondrial genome of the land snail Albinaria coerulea."; Genetics 140:1353-1366(1995).

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.
SIMILARITY: Belongs to the heme-copper respiratory oxidase 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

X83390; CAA58307.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S59154; S59154.

RefSeq

NP_007340.1; -.

3D structure databases

HSSP

P00396; 2OCC. [HSSP ENTRY / PDB]

ModBase

P48887.

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 UniProtKB-KW).
GO:0004129;	Molecular function: cytochrome-c oxidase activity (inferred from electronic annotation from EC).
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:0009060;	Biological process: aerobic respiration (inferred from electronic annotation from InterPro).
GO:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000883; COX1.
Graphical view of domain structure.

Gene3D

G3DSA:1.20.210.10; COX1; 1.

PANTHER

PTHR10422; COX1; 1.

Pfam

PF00115; COX1; 1.
Pfam graphical view of domain structure.

PRINTS

PR01165; CYCOXIDASEI.

PROSITE

PS50855; COX1; 1.
PS00077; COX1_CUB; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P48887.

Genome annotation databases

GeneID

807999; -.

Other

UniRef

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

Keywords

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`	`1 509`	`509`	`Cytochrome c oxidase subunit 1.`	`PRO_0000183277`
`TRANSMEM`	`14 34`	`21`	`Potential.`
`TRANSMEM`	`52 72`	`21`	`Potential.`
`TRANSMEM`	`98 118`	`21`	`Potential.`
`TRANSMEM`	`141 161`	`21`	`Potential.`
`TRANSMEM`	`179 199`	`21`	`Potential.`
`TRANSMEM`	`230 250`	`21`	`Potential.`
`TRANSMEM`	`263 283`	`21`	`Potential.`
`TRANSMEM`	`302 322`	`21`	`Potential.`
`TRANSMEM`	`333 353`	`21`	`Potential.`
`TRANSMEM`	`380 400`	`21`	`Potential.`
`TRANSMEM`	`409 429`	`21`	`Potential.`
`TRANSMEM`	`452 472`	`21`	`Potential.`
`METAL`	`57 57`		`Iron (heme A axial ligand) (Probable).`
`METAL`	`236 236`		`Copper B (Probable).`
`METAL`	`240 240`		`Copper B (Probable).`
`METAL`	`285 285`		`Copper B (Probable).`
`METAL`	`286 286`		`Copper B (Probable).`
`METAL`	`371 371`		`Iron (heme A3 axial ligand) (Probable).`
`METAL`	`373 373`		`Iron (heme A axial ligand) (Probable).`
`CROSSLNK`	`236 240`		`1'-histidyl-3'-tyrosine (His-Tyr) (By similarity).`

Sequence information

Length: 509 AA [This is the length of the unprocessed precursor]

Molecular weight: 57034 Da [This is the MW of the unprocessed precursor]

CRC64: 07236D1343151A6B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRWFYSTNHK DIGTLYMLFG IWCGMVGTGL SLLIRLELGT SGTLTDDHFY NVIVTAHAFV 

        70         80         90        100        110        120 
MIFFMVMPIM IGGFGNWMVP LLIGAPDMSF PRMNNMSFWL LPPAFILLIC SSMVEGGAGT 

       130        140        150        160        170        180 
GWTVYPPLSS SLAHSGASVD LAIFSLHLAG MSSILGAINF ITTIFNMRSP GMTMERVSLF 

       190        200        210        220        230        240 
VWSILVTVFL LLLSLPVLAG AITMLLTDRN FNTSFFDPAG GGDPILYQHL FWFFGHPEVY 

       250        260        270        280        290        300 
ILILPGFGMI SHILGNSAMK QPFGTLGMIY AMISIGILGF IVWAHHMFTV GMDVDTRAYF 

       310        320        330        340        350        360 
TAATMIIAIP TGIKVFSWLM TIYGSKVQYT ASMYWVLGFI FLFTLGGLTG IVLSNSSLDI 

       370        380        390        400        410        420 
MLHDTYYVVA HFHYVLSMGA VFAIFAGFNF WFPVMTGLIL HERLAKAQFV VMFIAVNMTF 

       430        440        450        460        470        480 
FPQHFLGLAG MPRRYSDYPD SYFMWNQLSS YGSLMSVFAV LLFVLIVWEA FLSQRSLLFV 

       490        500 
DATLYSREWS DGYFPPDFHS NIYQSYITI

P48887 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