Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9B229 (COX1_CHRKN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
OrganismChrysomela knabi (Leaf beetle)
Taxonomic identifier153783 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaColeopteraPolyphagaCucujiformiaChrysomeloideaChrysomelidaeChrysomelinaeChrysomeliniChrysomela

Protein attributes

Sequence length219 AA.
Sequence statusFragment.
Protein existenceInferred 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›219›219Cytochrome c oxidase subunit 1
PRO_0000183314

Regions

Topological domain‹1›1Mitochondrial matrix By similarity UniProtKB P00396
Transmembrane2 – 2423Helical; Name=III; By similarity UniProtKB P00396
Topological domain25 – 4723Mitochondrial intermembrane By similarity UniProtKB P00396
Transmembrane48 – 7730Helical; Name=IV; By similarity UniProtKB P00396
Topological domain78 – 8912Mitochondrial matrix By similarity UniProtKB P00396
Transmembrane90 – 11930Helical; Name=V; By similarity UniProtKB P00396
Topological domain120 – 13415Mitochondrial intermembrane By similarity UniProtKB P00396
Transmembrane135 – 16834Helical; Name=VI; By similarity UniProtKB P00396
Topological domain169 – 1768Mitochondrial matrix By similarity UniProtKB P00396
Transmembrane177 – 19317Helical; Name=VII; By similarity UniProtKB P00396
Topological domain194 – 20512Mitochondrial intermembrane By similarity UniProtKB P00396
Transmembrane206 – ›219›14Helical; Name=VIII; By similarity UniProtKB P00396

Sites

Metal binding1471Copper B Probable UniProtKB P00396
Metal binding1511Copper B Probable UniProtKB P98002
Metal binding1971Copper B Probable UniProtKB P00396
Metal binding1981Copper B Probable UniProtKB P00396

Amino acid modifications

Cross-link147 ↔ 1511'-histidyl-3'-tyrosine (His-Tyr) By similarity UniProtKB P00396

Experimental info

Sequence conflict201I → L in AAK16643. Ref.2
Sequence conflict41 – 466SNIAHG → ANTAHS in AAK16643. Ref.2
Sequence conflict81 – 888MGMKLDRM → EGMNFEQT in AAK16643. Ref.2
Sequence conflict961V → L in AAK16643. Ref.2
Non-terminal residue11
Non-terminal residue2191

Sequences

Sequence LengthMass (Da)Tools
Q9B229 [UniParc].

Last modified August 16, 2004. Version 2.
Checksum: 93BD81BF4358C92D

FASTA21924,021
        10         20         30         40         50         60 
FPRMNNMSFW LLPPSLFLLI MSSIVENGAG TGWTVYPPLS SNIAHGGSSV DLAIFSLHLA 

        70         80         90        100        110        120 
GISSILGAIN FITTVINMRP MGMKLDRMPL FVWAVVITAI LLLLSLPVLA GAITMLLTDR 

       130        140        150        160        170        180 
NLNTSFFDPA GGGDPILYQH LFWFFGHPEV YILILPGFGM ISHIISQESS KKEVFGTLGM 

       190        200        210 
IYAMMAIGLL GFIVWAHHMF TVGMDVDTQT YFTSATMII 

« Hide

References

[1]"Convergent evolution of cucurbitacin feeding in spatially isolated rootworm taxa (Coleoptera: Chrysomelidae; Galerucinae, Luperini)."
Gillespie J.J., Kjer K.M., Duckett C.N., Tallamy D.W.
Mol. Phylogenet. Evol. 29:161-175(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-154.
Strain: Isolate JJG237.
[2]"Feeding specialization and host-derived chemical defense in Chrysomeline leaf beetles did not lead to an evolutionary dead end."
Termonia A., Hsiao T.H., Pasteels J.M., Milinkovitch M.C.
Proc. Natl. Acad. Sci. U.S.A. 98:3909-3914(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-219.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY242402 Genomic DNA. Translation: AAP13120.1.
AY027627 Genomic DNA. Translation: AAK16643.1.

3D structure databases

ProteinModelPortalQ9B229.
SMRQ9B229. Positions 1-219.
ModBaseSearch...
MobiDBSearch...

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. SSF81442. 1 hit.
PROSITEPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX1_CHRKN
AccessionPrimary (citable) accession number: Q9B229
Secondary accession number(s): Q85KD6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: May 14, 2014
This is version 60 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways