Cytochrome c oxidase subunit 1 - Chrysomela knabi (Leaf beetle)

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Reviewed, UniProtKB/Swiss-Prot Q9B229 (COX1_CHRKN)

Last modified March 24, 2009. Version 42. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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

Chrysomela knabi (Leaf beetle)

Taxonomic identifier

153783 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Coleoptera › Polyphaga › Cucujiformia › Chrysomeloidea › Chrysomelidae › Chrysomelinae › Chrysomelini › Chrysomela

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Protein attributes

Sequence length	219 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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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.

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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 mitochondrial electron transport, cytochrome c to oxygen Non-traceable author statement. Source: UniProtKB transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Non-traceable author statement. Source: UniProtKB mitochondrial respiratory chain complex IV Non-traceable author statement. Source: UniProtKB
Molecular function	copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW cytochrome-c oxidase activity Non-traceable author statement. Source: UniProtKB electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

‹1 – ›219

›219

Cytochrome c oxidase subunit 1

PRO_0000183314

Regions

Topological domain

‹1

›1

Mitochondrial matrix By similarity UniProtKB P00396

Transmembrane

2 – 24

III By similarity UniProtKB P00396

Topological domain

25 – 47

Mitochondrial intermembrane By similarity UniProtKB P00396

Transmembrane

48 – 77

IV By similarity UniProtKB P00396

Topological domain

78 – 89

Mitochondrial matrix By similarity UniProtKB P00396

Transmembrane

90 – 119

V By similarity UniProtKB P00396

Topological domain

120 – 134

Mitochondrial intermembrane By similarity UniProtKB P00396

Transmembrane

135 – 168

VI By similarity UniProtKB P00396

Topological domain

169 – 176

Mitochondrial matrix By similarity UniProtKB P00396

Transmembrane

177 – 193

VII By similarity UniProtKB P00396

Topological domain

194 – 205

Mitochondrial intermembrane By similarity UniProtKB P00396

Transmembrane

206 – ›219

›14

VIII By similarity UniProtKB P00396

Sites

Metal binding

147

Copper B Probable UniProtKB P00396

Metal binding

151

Copper B Probable UniProtKB P98002

Metal binding

197

Copper B Probable UniProtKB P00396

Metal binding

198

Copper B Probable UniProtKB P00396

Amino acid modifications

Cross-link

147 ↔ 151

1'-histidyl-3'-tyrosine (His-Tyr) By similarity UniProtKB P00396

Experimental info

Sequence conflict

I → L in AAK16643. Ref.2

Sequence conflict

41 – 46

SNIAHG → ANTAHS in AAK16643. Ref.2

Sequence conflict

81 – 88

MGMKLDRM → EGMNFEQT in AAK16643. Ref.2

Sequence conflict

V → L in AAK16643. Ref.2

Non-terminal residue

219

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Sequences

Sequence

Length

Mass (Da)

Tools

Q9B229-1 [UniParc].

Last modified August 16, 2004. Version 2.
Checksum: 93BD81BF4358C92D
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FASTA

219

24,021

        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

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References

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

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Cross-references

Sequence databases
	AY242402 Genomic DNA. Translation: AAP13120.1. AY027627 Genomic DNA. Translation: AAK16643.1.
3D structure databases
SMR	Q9B229. Positions 1-219.
ModBase	Search...
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...

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Entry information

Entry name

COX1_CHRKN

Accession

Primary (citable) accession number: Q9B229
Secondary accession number(s): Q85KD6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	August 16, 2004
Last modified:	March 24, 2009
This is version 42 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Family and domain databases

Entry information

Relevant documents