[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-154. STRAIN=Isolate JJG237; DOI=10.1016/S1055-7903(03)00256-2; PubMed=12967617 [NCBI, ExPASy, EBI, Israel, Japan] Gillespie J.J., Kjer K.M., Duckett C.N., Tallamy D.W.; "Convergent evolution of cucurbitacin feeding in spatially isolated rootworm taxa (Coleoptera: Chrysomelidae; Galerucinae, Luperini)."; Mol. Phylogenet. Evol. 29:161-175(2003).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-219. DOI=10.1073/pnas.061034598; PubMed=11259651 [NCBI, ExPASy, EBI, Israel, Japan] Termonia A., Hsiao T.H., Pasteels J.M., Milinkovitch M.C.; "Feeding specialization and host-derived chemical defense in Chrysomeline leaf beetles did not lead to an evolutionary dead end."; Proc. Natl. Acad. Sci. U.S.A. 98:3909-3914(2001).

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

AY242402; AAP13120.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY027627; AAK16643.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

SMR

Q9B229; 1-219.

ModBase

Q9B229.

Ontologies

GO:0016021;	Cellular component: integral to membrane (non-traceable author statement from UniProtKB).
GO:0005751;	Cellular component: mitochondrial respiratory chain complex IV (non-traceable author statement from UniProtKB).
GO:0005507;	Molecular function: copper ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004129;	Molecular function: cytochrome-c oxidase activity (non-traceable author statement from UniProtKB).
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:0006123;	Biological process: mitochondrial electron transport, cytochrome c to oxygen (non-traceable author statement from UniProtKB).
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).

Other

ProtoNet

Q9B229.

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 >219`	`>219`	`Cytochrome c oxidase subunit 1.`	`PRO_0000183314`
`TOPO_DOM`	`<1 1`	`>1`	`Mitochondrial matrix (By similarity).`
`TRANSMEM`	`2 24`	`23`	`III (By similarity).`
`TOPO_DOM`	`25 47`	`23`	`Mitochondrial intermembrane (By similarity).`
`TRANSMEM`	`48 77`	`30`	`IV (By similarity).`
`TOPO_DOM`	`78 89`	`12`	`Mitochondrial matrix (By similarity).`
`TRANSMEM`	`90 119`	`30`	`V (By similarity).`
`TOPO_DOM`	`120 134`	`15`	`Mitochondrial intermembrane (By similarity).`
`TRANSMEM`	`135 168`	`34`	`VI (By similarity).`
`TOPO_DOM`	`169 176`	`8`	`Mitochondrial matrix (By similarity).`
`TRANSMEM`	`177 193`	`17`	`VII (By similarity).`
`TOPO_DOM`	`194 205`	`12`	`Mitochondrial intermembrane (By similarity).`
`TRANSMEM`	`206 >219`	`>14`	`VIII (By similarity).`
`METAL`	`147 147`		`Copper B (Probable).`
`METAL`	`151 151`		`Copper B (Probable).`
`METAL`	`197 197`		`Copper B (Probable).`
`METAL`	`198 198`		`Copper B (Probable).`
`CROSSLNK`	`147 151`		`1'-histidyl-3'-tyrosine (His-Tyr) (By similarity).`
`CONFLICT`	`20 20`		`I -> L (in Ref. 2; AAK16643).`
`CONFLICT`	`41 46`		`SNIAHG -> ANTAHS (in Ref. 2; AAK16643).`
`CONFLICT`	`81 88`		`MGMKLDRM -> EGMNFEQT (in Ref. 2; AAK16643).`
`CONFLICT`	`96 96`		`V -> L (in Ref. 2; AAK16643).`
`NON_TER`	`1 1`
`NON_TER`	`219 219`

Sequence information

Length: 219 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 24021 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 93BD81BF4358C92D [This is a checksum on the sequence]

        10         20         30         40         50         60 
FPRMNNMSFW LLPPSLFLLI MSSIVENGAG TGWTVYPPLS SNIAHGGSSV DLAIFSLHLA 

        70         80         90        100        110        120 
GISSILGAIN FITTVINMRP MGMKLDRMPL FVWAVVITAI LLLLSLPVLA GAITMLLTDR 

       130        140        150        160        170        180 
NLNTSFFDPA GGGDPILYQH LFWFFGHPEV YILILPGFGM ISHIISQESS KKEVFGTLGM 

       190        200        210 
IYAMMAIGLL GFIVWAHHMF TVGMDVDTQT YFTSATMII

Q9B229 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