Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q00227

- COX2_MYTED

UniProt

Q00227 - COX2_MYTED

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Cytochrome c oxidase subunit 2

Gene

COII

Organism
Mytilus edulis (Blue mussel)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

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. Subunit 2 transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit 1.

Catalytic activityi

4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O.

Cofactori

Copper A.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi176 – 1761Copper ACurated
Metal bindingi211 – 2111Copper ACurated
Metal bindingi215 – 2151Copper ACurated
Metal bindingi219 – 2191Copper ACurated

GO - Molecular functioni

  1. copper ion binding Source: InterPro
  2. cytochrome-c oxidase activity Source: UniProtKB-EC

GO - Biological processi

  1. electron transport chain Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome c oxidase subunit 2 (EC:1.9.3.1)
Alternative name(s):
Cytochrome c oxidase polypeptide II
Gene namesi
Name:COII
Encoded oniMitochondrion
OrganismiMytilus edulis (Blue mussel)
Taxonomic identifieri6550 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaBivalviaPteriomorphiaMytiloidaMytiloideaMytilidaeMytilinaeMytilus

Subcellular locationi

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. mitochondrial inner membrane Source: UniProtKB-KW
  3. respiratory chain Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 242242Cytochrome c oxidase subunit 2PRO_0000183636Add
BLAST

Proteomic databases

PRIDEiQ00227.

Structurei

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3030Mitochondrial intermembraneSequence AnalysisAdd
BLAST
Topological domaini48 – 6619Mitochondrial matrixSequence AnalysisAdd
BLAST
Topological domaini84 – 242159Mitochondrial intermembraneSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei31 – 4717HelicalSequence AnalysisAdd
BLAST
Transmembranei67 – 8317HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di1.10.287.90. 1 hit.
2.60.40.420. 1 hit.
InterProiIPR001505. Copper_CuA.
IPR008972. Cupredoxin.
IPR002429. Cyt_c_oxidase_su2_C.
IPR011759. Cyt_c_oxidase_su2_TM_dom.
[Graphical view]
PfamiPF00116. COX2. 1 hit.
PF02790. COX2_TM. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 1 hit.
SSF81464. SSF81464. 1 hit.
PROSITEiPS00078. COX2. 1 hit.
PS50857. COX2_CUA. 1 hit.
PS50999. COX2_TM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q00227 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSFYGSRYFG DIVHGELGKD LFRYHGFVMM VAVAVLVFVM YMGCVILFTK
60 70 80 90 100
FSYRHFLNRQ RLEFWWTIVP MLMLVGLWXP SMINLYYMEE VKRPRWNFKA
110 120 130 140 150
IGKQWYWSYE FCRNLDTPSS SESAESISCY TIDSYMEDQQ ETFSKGGYRL
160 170 180 190 200
LDVDNRMVAP ADVQMTAFVS SSDVLHSFAL PKLLIKVDAI PGRINRLPMK
210 220 230 240
ASQCSIIYGQ CSEICGVNHS FMPIVIEFIP EKYFVMWLEA LN
Length:242
Mass (Da):28,273
Last modified:July 5, 2005 - v2
Checksum:iFC3FE2D3D15E4D56
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY484747 Genomic DNA. Translation: AAT98406.1.
PIRiS28747.
RefSeqiYP_073337.1. NC_006161.1.

Genome annotation databases

GeneIDi2960254.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY484747 Genomic DNA. Translation: AAT98406.1 .
PIRi S28747.
RefSeqi YP_073337.1. NC_006161.1.

3D structure databases

ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q00227.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 2960254.

Organism-specific databases

CTDi 4513.

Family and domain databases

Gene3Di 1.10.287.90. 1 hit.
2.60.40.420. 1 hit.
InterProi IPR001505. Copper_CuA.
IPR008972. Cupredoxin.
IPR002429. Cyt_c_oxidase_su2_C.
IPR011759. Cyt_c_oxidase_su2_TM_dom.
[Graphical view ]
Pfami PF00116. COX2. 1 hit.
PF02790. COX2_TM. 1 hit.
[Graphical view ]
SUPFAMi SSF49503. SSF49503. 1 hit.
SSF81464. SSF81464. 1 hit.
PROSITEi PS00078. COX2. 1 hit.
PS50857. COX2_CUA. 1 hit.
PS50999. COX2_TM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Complete sequences of the highly rearranged molluscan mitochondrial genomes of the scaphopod Graptacme eborea and the bivalve Mytilus edulis."
    Boore J.L., Medina M., Rosenberg L.A.
    Mol. Biol. Evol. 21:1492-1503(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "A novel mitochondrial genome organization for the blue mussel, Mytilus edulis."
    Hoffmann R.J., Boore J.L., Brown W.M.
    Genetics 131:397-412(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-112 AND 162-242.

Entry informationi

Entry nameiCOX2_MYTED
AccessioniPrimary (citable) accession number: Q00227
Secondary accession number(s): Q68SR6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 5, 2005
Last modified: October 29, 2014
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3