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Q36724 (COX1_BLAGE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Cytochrome c oxidase subunit 1
EC=1.9.3.1
Alternative name(s):
Cytochrome c oxidase polypeptide I
Gene names
Name:COI
Encoded onMitochondrion
OrganismBlattella germanica (German cockroach) (Blatta germanica)
Taxonomic identifier6973 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Orthopteroidea › Dictyoptera › Blattodea › Blaberoidea › Ectobiidae › Blattellinae › Blattella

Protein attributes

Sequence length508 AA.
Sequence statusFragment.
Protein existenceEvidence 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.

Tissue specificity

Expressed in all tissues examined. Highest levels in gut and fat body, lower levels in ovary and collateral glands. Ref.1

Developmental stage

Levels increase 3-fold during embryo development with the highest level in 17 day old embryos. Relatively low levels in larvae and adults. Ref.1

Sequence similarities

Belongs to the heme-copper respiratory oxidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 508›508Cytochrome c oxidase subunit 1
PRO_0000183295

Regions

Topological domain‹1 – 6›6Mitochondrial matrix By similarity UniProtKB P00396
Transmembrane7 – 3529Helical; Name=I; By similarity UniProtKB P00396
Topological domain36 – 4510Mitochondrial intermembrane By similarity UniProtKB P00396
Transmembrane46 – 8136Helical; Name=II; By similarity UniProtKB P00396
Topological domain82 – 898Mitochondrial matrix By similarity UniProtKB P00396
Transmembrane90 – 11223Helical; Name=III; By similarity UniProtKB P00396
Topological domain113 – 13523Mitochondrial intermembrane By similarity UniProtKB P00396
Transmembrane136 – 16530Helical; Name=IV; By similarity UniProtKB P00396
Topological domain166 – 17712Mitochondrial matrix By similarity UniProtKB P00396
Transmembrane178 – 20730Helical; Name=V; By similarity UniProtKB P00396
Topological domain208 – 22215Mitochondrial intermembrane By similarity UniProtKB P00396
Transmembrane223 – 25634Helical; Name=VI; By similarity UniProtKB P00396
Topological domain257 – 2648Mitochondrial matrix By similarity UniProtKB P00396
Transmembrane265 – 28117Helical; Name=VII; By similarity UniProtKB P00396
Topological domain282 – 29312Mitochondrial intermembrane By similarity UniProtKB P00396
Transmembrane294 – 32229Helical; Name=VIII; By similarity UniProtKB P00396
Topological domain323 – 3308Mitochondrial matrix By similarity UniProtKB P00396
Transmembrane331 – 35222Helical; Name=IX; By similarity UniProtKB P00396
Topological domain353 – 36513Mitochondrial intermembrane By similarity UniProtKB P00396
Transmembrane366 – 39530Helical; Name=X; By similarity UniProtKB P00396
Topological domain396 – 4016Mitochondrial matrix By similarity UniProtKB P00396
Transmembrane402 – 42827Helical; Name=XI; By similarity UniProtKB P00396
Topological domain429 – 44113Mitochondrial intermembrane By similarity UniProtKB P00396
Transmembrane442 – 47332Helical; Name=XII; By similarity UniProtKB P00396
Topological domain474 – 50835Mitochondrial matrix By similarity UniProtKB P00396

Sites

Metal binding561Iron (heme A axial ligand) Probable UniProtKB P00396
Metal binding2351Copper B Probable UniProtKB P00396
Metal binding2391Copper B Probable UniProtKB P00396
Metal binding2851Copper B Probable UniProtKB P00396
Metal binding2861Copper B Probable UniProtKB P00396
Metal binding3711Iron (heme A3 axial ligand) Probable UniProtKB P00396
Metal binding3731Iron (heme A axial ligand) Probable UniProtKB P00396

Amino acid modifications

Cross-link235 ↔ 2391'-histidyl-3'-tyrosine (His-Tyr) By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
Q36724 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 48B5BE46771C10DD

FASTA50856,001
        10         20         30         40         50         60 
WLFSTNHKDI GTLYFIFGAW SGMVGMSLSM LIRAELNQPG SLIGDDQIYN VIVTAHAFVM 

        70         80         90        100        110        120 
IFFMVMPILI GGFGNWLVPL MLGAPDMAFP RMNNMSFWFL PPSLSLLLAS SLVESGAGTG 

       130        140        150        160        170        180 
WTLYPPLASG IAHAGASVDL AIFSLHLAGV SSILGAVNFI STIINMKPIN MSPERIPLFV 

       190        200        210        220        230        240 
WSVGITALLL LLSLPVLAGA ITMLLTDRNL NTSFFDPAGG GDPILYQHLF WFFGHPEVYI 

       250        260        270        280        290        300 
LILPGFGMIS HIICHESGKK EAFGNLGMIF AMLAIGLLGF VVWAHHMFTV GMDVDTRAYF 

       310        320        330        340        350        360 
TSATMIIAVP TGIKIFSWLA TMYGSQLTYS APCLWALGFV FLFTVGGLTG VVLANSSIDI 

       370        380        390        400        410        420 
VLHDTYYVVA HFHYVLSMGA VFAIMAGFIQ WYPLFTGLSL NPKWLKIQFS IMFLGVNLTF 

       430        440        450        460        470        480 
FPQHFLGLAG MPRRYSDYPD AYTAWNVISS IGSMISFVAV LMFIFIMWES MSSNRQVLFP 

       490        500 
TQTSNSIEWF QNIPPAEHSY AELPTISY

« Hide

References

[1]"Cytochrome c oxidase subunit I from the cockroach Blattella germanica: cloning, developmental pattern and tissue expression."
Martinez-Gonzalez J., Hegardt F.G.
Insect Biochem. Mol. Biol. 24:619-626(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		S72627 mRNA. Translation: AAB31450.2.

3D structure databases

ProteinModelPortalQ36724.
SMRQ36724. Positions 1-502.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00705.

Family and domain databases

Gene3D1.20.210.10. 1 hit.
InterProIPR000883. Cyt_c_Oxase_su1.
IPR023615. Cyt_c_Oxase_su1_BS.
IPR023616. Cyt_c_Oxase_su1_dom.
[Graphical view]
PANTHERPTHR10422. PTHR10422. 1 hit.
PfamPF00115. COX1. 1 hit.
[Graphical view]
PRINTSPR01165. CYCOXIDASEI.
SUPFAMSSF81442. COX1. 1 hit.
PROSITEPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX1_BLAGE
AccessionPrimary (citable) accession number: Q36724
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: November 1, 1996
Last modified: April 3, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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