Cytochrome c oxidase subunit 1 - Rattus norvegicus (Rat)

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P05503 (COX1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 108. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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:	Mtco1
Synonyms:	Coi, mt-Co1

Encoded on

Mitochondrion

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	514 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

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
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aerobic respiration Inferred from electronic annotation. Source: InterPro aging Inferred from expression pattern PubMed 9701770. Source: RGD cerebellum development Inferred from expression pattern PubMed 2465379. Source: RGD electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW oxidative phosphorylation Inferred from electronic annotation. Source: UniProtKB-UniPathway response to copper ion Inferred from expression pattern PubMed 18567746. Source: RGD response to electrical stimulus Inferred from expression pattern PubMed 14519661. Source: RGD response to oxidative stress Inferred from direct assay PubMed 17870132. Source: RGD
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay PubMed 18567746. Source: RGD 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 – 514

514

Cytochrome c oxidase subunit 1

PRO_0000183406

Regions

Transmembrane

17 – 37

Helical; Potential

Transmembrane

56 – 76

Helical; Potential

Transmembrane

102 – 122

Helical; Potential

Transmembrane

145 – 165

Helical; Potential

Transmembrane

183 – 203

Helical; Potential

Transmembrane

234 – 254

Helical; Potential

Transmembrane

268 – 288

Helical; Potential

Transmembrane

310 – 330

Helical; Potential

Transmembrane

338 – 358

Helical; Potential

Transmembrane

380 – 400

Helical; Potential

Transmembrane

414 – 434

Helical; Potential

Transmembrane

456 – 476

Helical; Potential

Sites

Metal binding

Iron (heme A axial ligand) Probable

Metal binding

240

Copper B Probable

Metal binding

244

Copper B Probable

Metal binding

290

Copper B Probable

Metal binding

291

Copper B Probable

Metal binding

376

Iron (heme A3 axial ligand) Probable

Metal binding

378

Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link

240 ↔ 244

1'-histidyl-3'-tyrosine (His-Tyr) By similarity

Experimental info

Sequence conflict

R → G in AAD15016. Ref.2

Sequence conflict

H → P in AAD15016. Ref.2

Sequence conflict

P → L in AAD15016. Ref.2

Sequence conflict

I → L in AAD15016. Ref.2

Sequence conflict

216 – 218

NTT → EFP in AAB21298. Ref.4

Sequence conflict

227

D → G in AAD15016. Ref.2

Sequence conflict

249

P → L in AAD15016. Ref.2

Sequence conflict

252

G → E in AAD15016. Ref.2

Sequence conflict

276

T → A in AAB21298. Ref.4

Sequence conflict

392

G → C in AAD15016. Ref.2

Sequence conflict

392

G → C in AAB21298. Ref.4

Sequence conflict

413

H → L in AAD15016. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P05503 [UniParc].

Last modified October 1, 1989. Version 2.
Checksum: 20BCE1C7857ED6FD
Show »

FASTA

514

56,937

        10         20         30         40         50         60 
MFVNRWLFST NHKDIGTLYL LFGAWAGMVG TALSILIRAE LGQPGALLGD DQIYNVIVTA 

        70         80         90        100        110        120 
HAFVMIFFMV MPMMIGGFGN WLVPLMIGAP DMAFPRMNNM SFWLLPPSFL LLLASSMVEA 

       130        140        150        160        170        180 
GAGTGWTVYP PLAGNLAHAG VSVDLTIFSL HLAGVSSILG AINFITTIIN MKPPAMTQYQ 

       190        200        210        220        230        240 
TPLFVWSVLI TAVLLLLSLP VLAAGITMLL TDRNLNTTFF DPAGGGDPIL YQHLFWFFGH 

       250        260        270        280        290        300 
PEVYILILPG FGIISHVVTY YSGKKEPFGY MGMVWTMMSI GFLGFIVWAH HMFTVGLDVD 

       310        320        330        340        350        360 
TRAYFTSATM IIAIPTGVKV FSWLATLHGG NIKWSPAMLW ALGFIFLFTV GGLTGIVLSN 

       370        380        390        400        410        420 
SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM AGFVHWFPLF SGYTLNDTWA KAHFAIMFVG 

       430        440        450        460        470        480 
VNMTFFPQHF LGLAGMPRRY SDYPDAYTTW NTVSSMGSFI SLTAVLVMIF MIWEAFASKR 

       490        500        510 
EVLSISYSST NLEWLHGCPP PYHTFEEPSY VKVK

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References

[1]	"The complete nucleotide sequence of the Rattus norvegicus mitochondrial genome: cryptic signals revealed by comparative analysis between vertebrates." Gadaleta G., Pepe G., de Candia G., Quagliariello C., Sbisa E., Saccone C. J. Mol. Evol. 28:497-516(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Wistar.
[2]	"Analysis of a DNA segment from rat liver mitochondria containing the genes for the cytochrome oxidase subunits I, II, II, ATPase subunit 6, and several tRNA genes." Grosskopf R., Feldmann H. Curr. Genet. 4:151-158(1981) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Sprague-Dawley. Tissue: Liver.
[3]	"Tumor-associated mutations of rat mitochondrial transfer RNA genes." Taira M., Yoshida E., Kobayashi M., Yaginuma K., Koike K. Nucleic Acids Res. 11:1635-1643(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
[4]	"Hormonal regulation of cytochrome oxidase subunit messenger RNAs in rat Sertoli cells." Ku C.Y., Lu Q., Ussuf K.K., Weinstock G.M., Sanborn B.M. Mol. Endocrinol. 5:1669-1676(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 216-514. Tissue: Sertoli cell.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X14848 Genomic DNA. Translation: CAA32956.1. J01435 Genomic DNA. Translation: AAD15016.1. V00676 Genomic DNA. Translation: CAA24046.1. V00678 Genomic DNA. Translation: CAA24050.1. S79304 mRNA. Translation: AAB21298.2.
IPI	IPI00200472.
PIR	S04749.
RefSeq	AP_004894.1. AC_000022.2.
3D structure databases
ProteinModelPortal	P05503.
SMR	P05503. Positions 1-514.
ModBase	Search...
Proteomic databases
PaxDb	P05503.
PRIDE	P05503.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
RGD	621871. mt-Co1.
Phylogenomic databases
eggNOG	COG0843.
HOGENOM	HOG000085274.
HOVERGEN	HBG003841.
InParanoid	P05503.
OrthoDB	EOG4BG8VW.
Enzyme and pathway databases
UniPathway	UPA00705.
Gene expression databases
ArrayExpress	P05503.
Genevestigator	P05503.
GermOnline	ENSRNOG00000034234. Rattus norvegicus.
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...
Other
ChEMBL	CHEMBL2436.
NextBio	35584672.

Entry information

Entry name

COX1_RAT

Accession

Primary (citable) accession number: P05503

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	October 1, 1989
Last modified:	April 3, 2013
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents