P14573 (COX2_LOCMI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytochrome c oxidase subunit 2
EC=1.9.3.1

Alternative name(s):
Cytochrome c oxidase polypeptide II

Gene names

Name:

COII

Encoded on

Mitochondrion

Organism

Locusta migratoria (Migratory locust)

Taxonomic identifier

7004 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Orthopteroidea › Orthoptera › Caelifera › Acridomorpha › Acridoidea › Acrididae › Oedipodinae › Locusta

Protein attributes

Sequence length	227 AA.
Sequence status	Complete.
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. Subunit 2 transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit 1.
Catalytic activity	4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O.
Cofactor	Copper A.
Subcellular location	Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the cytochrome c oxidase subunit 2 family.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transmembrane Transmembrane helix
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	copper ion binding Inferred from electronic annotation. Source: InterPro cytochrome-c oxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 227	227	Cytochrome c oxidase subunit 2		PRO_0000183621
Regions
	Topological domain	1 – 26	26	Mitochondrial intermembrane Potential
	Transmembrane	27 – 48	22	Helical; Potential
	Topological domain	49 – 62	14	Mitochondrial matrix Potential
	Transmembrane	63 – 82	20	Helical; Potential
	Topological domain	83 – 227	145	Mitochondrial intermembrane Potential
Sites
	Metal binding	161	1	Copper A Probable
	Metal binding	196	1	Copper A Probable
	Metal binding	200	1	Copper A Probable
	Metal binding	204	1	Copper A Probable

Sequences

	Sequence		Length	Mass (Da)
	P14573 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: D458468CD36FF10B	FASTA	227	26,035
	10 20 30 40 50 60 MATWSNLSLQ DGASPLMEQL SFFHDHTMID LLLITMIVGY SLSYMLLTKY TNRNMLHGHL 70 80 90 100 110 120 IETIWTALPA ITLIFIALPS LRLLYLLDDS SDAMITIKTI GRQWYWSYEY SDFINVEFDT 130 140 150 160 170 180 YMTPENELNT DEFRLLEVDN RTTLPMNTEV RVLTSASDVL HSWAVPALVL KIDATPGRLN 190 200 210 220 QGMFMINRPG LFFGQCSEIC GANHSFMPIV IESTSIKLFI KWLSNMM

References

[1]	"Different mitochondrial gene orders among insects: exchanged tRNA gene positions in the COII/COIII region between an orthopteran and a dipteran species." Haucke H.R., Gellissen G. Curr. Genet. 14:471-476(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The sequence, organization, and evolution of the Locusta migratoria mitochondrial genome." Flook P.K., Rowell C.H.F., Gellissen G. J. Mol. Evol. 41:928-941(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	X13975 Genomic DNA. Translation: CAA32153.1. X80245 Genomic DNA. Translation: CAA56539.1.
PIR	T11479.
RefSeq	NP_007292.1. NC_001712.1.
3D structure databases
ProteinModelPortal	P14573.
SMR	P14573. Positions 1-227.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	807963.
Organism-specific databases
CTD	4513.
Phylogenomic databases
ProtClustDB	MTH00154.
Family and domain databases
Gene3D	1.10.287.90. 1 hit. 2.60.40.420. 1 hit.
InterPro	IPR001505. Copper_CuA. IPR008972. Cupredoxin. IPR002429. Cyt_c_oxidase_su2_C. IPR011759. Cyt_c_oxidase_su2_TM_dom. [Graphical view]
Pfam	PF00116. COX2. 1 hit. PF02790. COX2_TM. 1 hit. [Graphical view]
SUPFAM	SSF49503. Cupredoxin. 1 hit. SSF81464. Cyt_c_oxidase_II-like_TM. 1 hit.
PROSITE	PS00078. COX2. 1 hit. PS50857. COX2_CUA. 1 hit. PS50999. COX2_TM. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

COX2_LOCMI

Accession

Primary (citable) accession number: P14573

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	May 1, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)