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Protein

Cytochrome c oxidase subunit 2

Gene

Mtco2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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.

Cofactori

Cu cationNote: Binds a copper A center.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi161Copper ACurated1
Metal bindingi196Copper ACurated1
Metal bindingi200Copper ACurated1
Metal bindingi204Copper ACurated1

GO - Molecular functioni

GO - Biological processi

  • ATP synthesis coupled electron transport Source: GO_Central
  • lactation Source: RGD
  • response to cold Source: RGD
Complete GO annotation...

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome c oxidase subunit 2
Alternative name(s):
Cytochrome c oxidase polypeptide II
Gene namesi
Name:Mtco2
Synonyms:Coii, mt-Co2
Encoded oniMitochondrion
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Mitochondrion

Organism-specific databases

RGDi621872. mt-Co2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 26Mitochondrial intermembraneSequence analysisAdd BLAST26
Transmembranei27 – 48HelicalSequence analysisAdd BLAST22
Topological domaini49 – 62Mitochondrial matrixSequence analysisAdd BLAST14
Transmembranei63 – 82HelicalSequence analysisAdd BLAST20
Topological domaini83 – 227Mitochondrial intermembraneSequence analysisAdd BLAST145

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001836771 – 227Cytochrome c oxidase subunit 2Add BLAST227

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei218PhosphotyrosineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP00406.
PRIDEiP00406.

PTM databases

iPTMnetiP00406.

Expressioni

Gene expression databases

ExpressionAtlasiP00406. differential.
GenevisibleiP00406. RN.

Interactioni

Protein-protein interaction databases

MINTiMINT-4996308.
STRINGi10116.ENSRNOP00000046414.

Structurei

3D structure databases

ProteinModelPortaliP00406.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4767. Eukaryota.
COG1622. LUCA.
GeneTreeiENSGT00390000017410.
HOGENOMiHOG000264988.
HOVERGENiHBG012727.
InParanoidiP00406.
KOiK02261.
OMAiVVLPMEM.
OrthoDBiEOG091G0IO9.

Family and domain databases

Gene3Di1.10.287.90. 1 hit.
2.60.40.420. 1 hit.
InterProiIPR001505. Copper_CuA.
IPR008972. Cupredoxin.
IPR014222. Cyt_c_oxidase_su2.
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.
TIGRFAMsiTIGR02866. CoxB. 1 hit.
PROSITEiPS00078. COX2. 1 hit.
PS50857. COX2_CUA. 1 hit.
PS50999. COX2_TM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00406-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAYPFQLGLQ DATSPIMEEL TNFHDHTLMI VFLISSLVLY IISLMLTTKL
60 70 80 90 100
THTSTMDAQE VETIWTILPA VILILIALPS LRILYMMDEI NNPVLTVKTM
110 120 130 140 150
GHQWYWSYEY TDYEDLCFDS YMIPTNDLKP GELRLLEVDN RVVLPMELPI
160 170 180 190 200
RMLISSEDVL HSWAVPSLGL KTDAIPGRLN QATVTSNRPG LFYGQCSEIC
210 220
GSNHSFMPIV LEMVPLKYFE NWSASMI
Length:227
Mass (Da):25,928
Last modified:April 1, 2015 - v3
Checksum:i9EA986B08B629664
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti17M → I in AAP31514 (PubMed:7981121).Curated1
Sequence conflicti21T → M in AAA67374 (PubMed:6285344).Curated1
Sequence conflicti29M → I in AAP31514 (PubMed:7981121).Curated1
Sequence conflicti45M → I in AAP31514 (PubMed:7981121).Curated1
Sequence conflicti56M → I in AAP31514 (PubMed:7981121).Curated1
Sequence conflicti59Q → H in AAA67314 (PubMed:1848093).Curated1
Sequence conflicti130P → L no nucleotide entry (Ref. 4) Curated1
Sequence conflicti130P → L in AAA67314 (PubMed:1848093).Curated1
Sequence conflicti164A → P no nucleotide entry (Ref. 4) Curated1
Sequence conflicti164A → P in AAA67314 (PubMed:1848093).Curated1
Sequence conflicti165V → I in AAB00992 (PubMed:6091655).Curated1
Sequence conflicti165V → I in CAA32957 (PubMed:2504926).Curated1
Sequence conflicti165V → I in AAA67314 (PubMed:1848093).Curated1
Sequence conflicti179L → P in AAA67314 (PubMed:1848093).Curated1
Sequence conflicti189P → L no nucleotide entry (Ref. 4) Curated1
Sequence conflicti189P → L in AAA67314 (PubMed:1848093).Curated1
Sequence conflicti208P → L no nucleotide entry (Ref. 4) Curated1
Sequence conflicti208P → L in AAA67314 (PubMed:1848093).Curated1
Sequence conflicti218Y → H in AAA67374 (PubMed:6285344).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01434 Genomic DNA. Translation: AAA67374.1.
M27315 Genomic DNA. Translation: AAB00992.1.
X14848 Genomic DNA. Translation: CAA32957.1.
M64496 Genomic DNA. Translation: AAA67314.1.
AY172581 Genomic DNA. Translation: AAN77597.1.
S74342 mRNA. Translation: AAP31514.1.
PIRiA93914. OBRT2.
B93914. OBRT2B.
RefSeqiAP_004895.1. AC_000022.2.
YP_665632.1. NC_001665.2.

Genome annotation databases

EnsembliENSRNOT00000043693; ENSRNOP00000046414; ENSRNOG00000030371.
GeneIDi26198.
KEGGirno:26198.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01434 Genomic DNA. Translation: AAA67374.1.
M27315 Genomic DNA. Translation: AAB00992.1.
X14848 Genomic DNA. Translation: CAA32957.1.
M64496 Genomic DNA. Translation: AAA67314.1.
AY172581 Genomic DNA. Translation: AAN77597.1.
S74342 mRNA. Translation: AAP31514.1.
PIRiA93914. OBRT2.
B93914. OBRT2B.
RefSeqiAP_004895.1. AC_000022.2.
YP_665632.1. NC_001665.2.

3D structure databases

ProteinModelPortaliP00406.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4996308.
STRINGi10116.ENSRNOP00000046414.

PTM databases

iPTMnetiP00406.

Proteomic databases

PaxDbiP00406.
PRIDEiP00406.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000043693; ENSRNOP00000046414; ENSRNOG00000030371.
GeneIDi26198.
KEGGirno:26198.

Organism-specific databases

CTDi4513.
RGDi621872. mt-Co2.

Phylogenomic databases

eggNOGiKOG4767. Eukaryota.
COG1622. LUCA.
GeneTreeiENSGT00390000017410.
HOGENOMiHOG000264988.
HOVERGENiHBG012727.
InParanoidiP00406.
KOiK02261.
OMAiVVLPMEM.
OrthoDBiEOG091G0IO9.

Miscellaneous databases

PROiP00406.

Gene expression databases

ExpressionAtlasiP00406. differential.
GenevisibleiP00406. RN.

Family and domain databases

Gene3Di1.10.287.90. 1 hit.
2.60.40.420. 1 hit.
InterProiIPR001505. Copper_CuA.
IPR008972. Cupredoxin.
IPR014222. Cyt_c_oxidase_su2.
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.
TIGRFAMsiTIGR02866. CoxB. 1 hit.
PROSITEiPS00078. COX2. 1 hit.
PS50857. COX2_CUA. 1 hit.
PS50999. COX2_TM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCOX2_RAT
AccessioniPrimary (citable) accession number: P00406
Secondary accession number(s): Q37738, Q80WI7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 2015
Last modified: November 30, 2016
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.