Q9B229 (COX1_CHRKN) Reviewed, UniProtKB/Swiss-Prot

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

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Coleoptera › Polyphaga › Cucujiformia › Chrysomeloidea › Chrysomelidae › Chrysomelinae › Chrysomelini › Chrysomela

Protein attributes

Sequence length	219 AA.
Sequence status	Fragment.
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 Transmembrane helix
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
Cellular_component	integral to membrane Non-traceable author statement. Source: UniProtKB mitochondrial respiratory chain complex IV Non-traceable author statement. Source: UniProtKB
Molecular_function	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 iron ion 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 – ›219	›219	Cytochrome c oxidase subunit 1		PRO_0000183314
Regions
	Topological domain	‹1	›1	Mitochondrial matrix By similarity UniProtKB P00396
	Transmembrane	2 – 24	23	Helical; Name=III; By similarity UniProtKB P00396
	Topological domain	25 – 47	23	Mitochondrial intermembrane By similarity UniProtKB P00396
	Transmembrane	48 – 77	30	Helical; Name=IV; By similarity UniProtKB P00396
	Topological domain	78 – 89	12	Mitochondrial matrix By similarity UniProtKB P00396
	Transmembrane	90 – 119	30	Helical; Name=V; By similarity UniProtKB P00396
	Topological domain	120 – 134	15	Mitochondrial intermembrane By similarity UniProtKB P00396
	Transmembrane	135 – 168	34	Helical; Name=VI; By similarity UniProtKB P00396
	Topological domain	169 – 176	8	Mitochondrial matrix By similarity UniProtKB P00396
	Transmembrane	177 – 193	17	Helical; Name=VII; By similarity UniProtKB P00396
	Topological domain	194 – 205	12	Mitochondrial intermembrane By similarity UniProtKB P00396
	Transmembrane	206 – ›219	›14	Helical; Name=VIII; By similarity UniProtKB P00396
Sites
	Metal binding	147	1	Copper B Probable UniProtKB P00396
	Metal binding	151	1	Copper B Probable UniProtKB P98002
	Metal binding	197	1	Copper B Probable UniProtKB P00396
	Metal binding	198	1	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	20	1	I → L in AAK16643. Ref.2
	Sequence conflict	41 – 46	6	SNIAHG → ANTAHS in AAK16643. Ref.2
	Sequence conflict	81 – 88	8	MGMKLDRM → EGMNFEQT in AAK16643. Ref.2
	Sequence conflict	96	1	V → L in AAK16643. Ref.2
	Non-terminal residue	1	1
	Non-terminal residue	219	1

Sequences

	Sequence		Length	Mass (Da)
	Q9B229 [UniParc]. Last modified August 16, 2004. Version 2. Checksum: 93BD81BF4358C92D	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

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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-219.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY242402 Genomic DNA. Translation: AAP13120.1. AY027627 Genomic DNA. Translation: AAK16643.1.
3D structure databases
ProteinModelPortal	Q9B229.
SMR	Q9B229. Positions 1-219.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00705.
Family and domain databases
Gene3D	1.20.210.10. 1 hit.
InterPro	IPR000883. Cyt_c_Oxase_su1. IPR023615. Cyt_c_Oxase_su1_BS. IPR023616. Cyt_c_Oxase_su1_dom. [Graphical view]
PANTHER	PTHR10422. PTHR10422. 1 hit.
Pfam	PF00115. COX1. 1 hit. [Graphical view]
PRINTS	PR01165. CYCOXIDASEI.
SUPFAM	SSF81442. COX1. 1 hit.
PROSITE	PS50855. COX1. 1 hit. PS00077. COX1_CUB. 1 hit. [Graphical view]
ProtoNet	Search...

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:	April 3, 2013
This is version 55 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)