Q8WEW3 (COX1_SEPOF) 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

Sepia officinalis (Common cuttlefish)

Taxonomic identifier

6610 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Lophotrochozoa › Mollusca › Cephalopoda › Coleoidea › Neocoleoidea › Decapodiformes › Sepiida › Sepiina › Sepiidae › Sepia

Protein attributes

Sequence length	223 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 – ›223	›223	Cytochrome c oxidase subunit 1		PRO_0000183416
Regions
	Topological domain	‹1 – 4	›4	Mitochondrial matrix Potential
	Transmembrane	5 – 27	23	Helical; Name=1; Potential
	Topological domain	28 – 46	19	Mitochondrial intermembrane Potential
	Transmembrane	47 – 69	23	Helical; Name=2; Potential
	Topological domain	70 – 88	19	Mitochondrial matrix Potential
	Transmembrane	89 – 111	23	Helical; Name=3; Potential
	Topological domain	112 – 130	19	Mitochondrial intermembrane Potential
	Transmembrane	131 – 153	23	Helical; Name=4; Potential
	Topological domain	154 – 173	20	Mitochondrial matrix Potential
	Transmembrane	174 – 196	23	Helical; Name=5; Potential
	Topological domain	197 – 223	27	Mitochondrial intermembrane Potential
Sites
	Metal binding	47	1	Iron (heme A axial ligand) Probable
Experimental info
	Sequence conflict	25	1	T → S in AAC95107. Ref.2
	Sequence conflict	32	1	S → T in AAC95107. Ref.2
	Sequence conflict	50	1	V → I in AAC95107. Ref.2
	Sequence conflict	100	1	A → S in AAC95107. Ref.2
	Sequence conflict	122	1	I → L in AAC95107. Ref.2
	Sequence conflict	155	1	M → L in AAC95107. Ref.2
	Sequence conflict	171	1	V → A in AAC95107. Ref.2
	Non-terminal residue	1	1
	Non-terminal residue	223	1

Sequences

	Sequence		Length	Mass (Da)
	Q8WEW3 [UniParc]. Last modified July 19, 2003. Version 2. Checksum: 2C48081196B6CDF4	FASTA	223	24,364
	10 20 30 40 50 60 IGTLYFIFGI WSGLLGTSLS LMIRTELGKP GSLLNDDQLY NVVVTAHGFV MIFFLVMPIM 70 80 90 100 110 120 IGGFGNWLVP LMLGAPDMAF PRMNNMSFWL LPPSLTLLLA SSAVESGAGT GWTVYPPLSS 130 140 150 160 170 180 NISHAGPSVD LAIFSLHLAG VSSILGAINF ITTIMNMRWE GLQMERLPLF VWSVFITAIL 190 200 210 220 LLLSLPVLAG AITMLLTDRN FNTTFFDPSG GGDPILYQHL FWF

References

[1]	"On bivalve phylogeny: a high-level phylogeny of the mollusk class Bivalvia based on a combined analysis of morphology and DNA sequence data." Giribet G., Wheeler W.C. Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"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] OF 3-221.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF120630 Genomic DNA. Translation: AAL55480.1. AF000062 Genomic DNA. Translation: AAC95107.1.
3D structure databases
ProteinModelPortal	Q8WEW3.
SMR	Q8WEW3. Positions 1-223.
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_SEPOF

Accession

Primary (citable) accession number: Q8WEW3
Secondary accession number(s): Q9ZYY9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2003
Last sequence update:	July 19, 2003
Last modified:	March 6, 2013
This is version 54 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)