Q9ZZ08 (COX1_HAPMA) 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

Hapalochlaena maculosa (Blue-ringed octopus) (Octopus maculosus)

Taxonomic identifier

61716 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Lophotrochozoa › Mollusca › Cephalopoda › Coleoidea › Neocoleoidea › Octopodiformes › Octopoda › Incirrata › Octopodidae › Hapalochlaena

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 electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW oxidative phosphorylation Inferred from electronic annotation. Source: UniProtKB-UniPathway
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	cytochrome-c oxidase activity Inferred from electronic annotation. Source: EC 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_0000183342
Regions
	Topological domain	‹1	›1	Mitochondrial matrix Potential
	Transmembrane	2 – 22	21	Helical; Name=1; Potential
	Topological domain	23 – 39	17	Mitochondrial intermembrane Potential
	Transmembrane	40 – 60	21	Helical; Name=2; Potential
	Topological domain	61 – 85	25	Mitochondrial matrix Potential
	Transmembrane	86 – 106	21	Helical; Name=3; Potential
	Topological domain	107 – 128	22	Mitochondrial intermembrane Potential
	Transmembrane	129 – 149	21	Helical; Name=4; Potential
	Topological domain	150 – 166	17	Mitochondrial matrix Potential
	Transmembrane	167 – 187	21	Helical; Name=5; Potential
	Topological domain	188 – 219	32	Mitochondrial intermembrane Potential
Sites
	Metal binding	45	1	Iron (heme A axial ligand) Probable
Experimental info
	Non-terminal residue	1	1
	Non-terminal residue	219	1

Sequences

	Sequence		Length	Mass (Da)
	Q9ZZ08 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 0D9D1CF45F2584D9	FASTA	219	23,945
	10 20 30 40 50 60 TLYFIFGIWS GLLGTSLSLM IRTELGQPGS LLNDDQLYNV IVTAHAFVMI FFLVMPVMIG 70 80 90 100 110 120 GFGNWLVPLM LGAPDMAFPR MNNMSFWLLP PSLTLLLSSA PVESGAGTGW TVYPPLSSNL 130 140 150 160 170 180 AHMGPSVDLA IFSLHLAGIS SIPGAINFIT TIINMRWEGM MMERLPLFVW SVFITAILLL 190 200 210 LSLPVLAGAI TMLLTDRNFN TTFFDPSGGG DPILYQHLF

References

[1]	"Phylogenetic analysis of cytochrome c oxidase I sequences to determine higher-level relationships within the coleoid cephalopods." Carlini D.B., Graves J.E. Bull. Mar. Sci. 64:57-76(1999) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF000043 Genomic DNA. Translation: AAC95088.1.
3D structure databases
ProteinModelPortal	Q9ZZ08.
SMR	Q9ZZ08. 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. 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. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

COX1_HAPMA

Accession

Primary (citable) accession number: Q9ZZ08

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2003
Last sequence update:	May 1, 1999
Last modified:	March 6, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)