Reviewed, UniProtKB/Swiss-Prot P48887 (COX1_ALBCO)

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

Albinaria coerulea (Land snail)

Taxonomic identifier

42349 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Mollusca › Gastropoda › Pulmonata › Stylommatophora › Sigmurethra › Clausilioidea › Clausiliidae › Alopiinae › Albinaria

Protein attributes

Sequence length	509 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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
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 transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-KW respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 509	509	Cytochrome c oxidase subunit 1		PRO_0000183277
Regions
	Transmembrane	14 – 34	21	Potential
	Transmembrane	52 – 72	21	Potential
	Transmembrane	98 – 118	21	Potential
	Transmembrane	141 – 161	21	Potential
	Transmembrane	179 – 199	21	Potential
	Transmembrane	230 – 250	21	Potential
	Transmembrane	263 – 283	21	Potential
	Transmembrane	302 – 322	21	Potential
	Transmembrane	333 – 353	21	Potential
	Transmembrane	380 – 400	21	Potential
	Transmembrane	409 – 429	21	Potential
	Transmembrane	452 – 472	21	Potential
Sites
	Metal binding	57	1	Iron (heme A axial ligand) Probable
	Metal binding	236	1	Copper B Probable
	Metal binding	240	1	Copper B Probable
	Metal binding	285	1	Copper B Probable
	Metal binding	286	1	Copper B Probable
	Metal binding	371	1	Iron (heme A3 axial ligand) Probable
	Metal binding	373	1	Iron (heme A axial ligand) Probable
Amino acid modifications
	Cross-link	236 ↔ 240		1'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P48887-1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 07236D1343151A6B	FASTA	509	57,034
	10 20 30 40 50 60 MRWFYSTNHK DIGTLYMLFG IWCGMVGTGL SLLIRLELGT SGTLTDDHFY NVIVTAHAFV 70 80 90 100 110 120 MIFFMVMPIM IGGFGNWMVP LLIGAPDMSF PRMNNMSFWL LPPAFILLIC SSMVEGGAGT 130 140 150 160 170 180 GWTVYPPLSS SLAHSGASVD LAIFSLHLAG MSSILGAINF ITTIFNMRSP GMTMERVSLF 190 200 210 220 230 240 VWSILVTVFL LLLSLPVLAG AITMLLTDRN FNTSFFDPAG GGDPILYQHL FWFFGHPEVY 250 260 270 280 290 300 ILILPGFGMI SHILGNSAMK QPFGTLGMIY AMISIGILGF IVWAHHMFTV GMDVDTRAYF 310 320 330 340 350 360 TAATMIIAIP TGIKVFSWLM TIYGSKVQYT ASMYWVLGFI FLFTLGGLTG IVLSNSSLDI 370 380 390 400 410 420 MLHDTYYVVA HFHYVLSMGA VFAIFAGFNF WFPVMTGLIL HERLAKAQFV VMFIAVNMTF 430 440 450 460 470 480 FPQHFLGLAG MPRRYSDYPD SYFMWNQLSS YGSLMSVFAV LLFVLIVWEA FLSQRSLLFV 490 500 DATLYSREWS DGYFPPDFHS NIYQSYITI

References

[1]	"Complete sequence and gene organization of the mitochondrial genome of the land snail Albinaria coerulea." Hatzoglou E., Rodakis G.C., Lecanidou R. Genetics 140:1353-1366(1995) [PubMed: 7498775] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	X83390 Genomic DNA. Translation: CAA58307.1.
PIR	S59154.
RefSeq	NP_007340.1.
3D structure databases
HSSP	HSSP built from PDB template 2OCC based on UniProtKB P00396.
ModBase	Search...
Genome annotation databases
GeneID	807999.
Organism-specific databases
CTD	807999.
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...

Entry information

Entry name

COX1_ALBCO

Accession

Primary (citable) accession number: P48887

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	October 13, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)