Cytochrome c oxidase subunit 1 - Physarum polycephalum (Slime mold)

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Q07434 (COX1_PHYPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 80. 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:

COX1

Encoded on

Mitochondrion

Organism

Physarum polycephalum (Slime mold)

Taxonomic identifier

5791 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Myxogastria › Myxogastromycetidae › Physariida › Physaraceae › Physarum

Protein attributes

Sequence length	594 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.
RNA editing	Modified position: not applicable. Some positions are modified by RNA editing via nucleotide insertion and conversion. Ref.1

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Coding sequence diversity	RNA editing
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 – 594

594

Cytochrome c oxidase subunit 1

PRO_0000183390

Regions

Transmembrane

41 – 61

Helical; Potential

Transmembrane

89 – 109

Helical; Potential

Transmembrane

126 – 146

Helical; Potential

Transmembrane

171 – 191

Helical; Potential

Transmembrane

209 – 229

Helical; Potential

Transmembrane

260 – 280

Helical; Potential

Transmembrane

292 – 312

Helical; Potential

Transmembrane

333 – 353

Helical; Potential

Transmembrane

363 – 383

Helical; Potential

Transmembrane

405 – 425

Helical; Potential

Transmembrane

467 – 487

Helical; Potential

Transmembrane

508 – 528

Helical; Potential

Sites

Metal binding

Iron (heme A axial ligand) Probable

Metal binding

266

Copper B Probable

Metal binding

270

Copper B Probable

Metal binding

315

Copper B Probable

Metal binding

316

Copper B Probable

Metal binding

401

Iron (heme A3 axial ligand) Probable

Metal binding

403

Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link

266 ↔ 270

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

Sequences

Sequence

Length

Mass (Da)

Tools

Q07434 [UniParc].

Last modified August 14, 2001. Version 2.
Checksum: 8D8A60C44620D5FF
Show »

FASTA

594

66,514

        10         20         30         40         50         60 
MSSIPFDQKT ISLLGMKMDT SDFYTFADRW LFSTNHKYIG TLYLLFSIGA GLAGLALSVI 

        70         80         90        100        110        120 
MRMELASCGD LILNSNYQLY NTIVTAHALI MIFFFVMPAL IGGFGNWFVP LLMGAPDMAF 

       130        140        150        160        170        180 
PRLNNISLWL LPSSLILLLL SSYVEIGAGT GWTVYPPLSS ITGHSGPSVD LAIFSLHLAG 

       190        200        210        220        230        240 
VSSMLGAINF ICTIKNMRLK GLTGERLSLF VWAVLVTVIL LLLSLPVLAG AITMLLTDRN 

       250        260        270        280        290        300 
FNTSFFDATG GGDPILYQHL FWFFGHPEVY ILILPGFGIV SIIIQAYANK AIFGYLGMVY 

       310        320        330        340        350        360 
AMLSIGILGF MVWAHHMYTV GLDVDTRAYF TAATMIIAVP TGIKIFSWLA TLFGSYLKLR 

       370        380        390        400        410        420 
TPLLFILGFL ILFTLGGLSG VVLANSGLDI AFHDTYYVVA HFHYVLSMGA VFAAFAAFYH 

       430        440        450        460        470        480 
WFSIIKSFTT YEPHEWEFVY NPFELRKKIP YRRTDFSYLE TAGILHFITT FIGVNLTFFP 

       490        500        510        520        530        540 
MHLLGLAGMP RRIPDYPDAY LHFNLISSYG SFVTLVSTIM FFMFGVVFNY NLFINGFPSM 

       550        560        570        580        590 
FYIIKPLIKI TFFRIKQIIQ GNNECLNSIS KELTILILHV KRLSKLSVNN WSIA

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References

[1]	"Substitutional and insertional RNA editing of the cytochrome c oxidase subunit 1 mRNA of Physarum polycephalum." Gott J.M., Visomirski L.M., Hunter J.L. J. Biol. Chem. 268:25483-25486(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], RNA EDITING. Strain: M3C.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L14769 mRNA. Translation: AAA71993.1.
3D structure databases
ProteinModelPortal	Q07434.
SMR	Q07434. Positions 26-520.
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. IPR023615. Cyt_c_Oxase_su1_BS. IPR023616. Cyt_c_Oxase_su1_dom. [Graphical view]
PANTHER	PTHR10422. PTHR10422. 1 hit.
Pfam	PF00115. COX1. 2 hits. [Graphical view]
PRINTS	PR01165. CYCOXIDASEI.
SUPFAM	SSF81442. COX1. 1 hit.
PROSITE	PS50855. COX1. 1 hit. PS00077. COX1_CUB. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

COX1_PHYPO

Accession

Primary (citable) accession number: Q07434

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	August 14, 2001
Last modified:	April 3, 2013
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

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

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents