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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi161 – 1611Copper ACurated
Metal bindingi196 – 1961Copper ACurated
Metal bindingi200 – 2001Copper ACurated
Metal bindingi204 – 2041Copper ACurated

GO - Molecular functioni

GO - Biological processi

  • electron transport chain Source: InterPro
  • 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)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2626Mitochondrial intermembraneSequence analysisAdd
BLAST
Transmembranei27 – 4822HelicalSequence analysisAdd
BLAST
Topological domaini49 – 6214Mitochondrial matrixSequence analysisAdd
BLAST
Transmembranei63 – 8220HelicalSequence analysisAdd
BLAST
Topological domaini83 – 227145Mitochondrial intermembraneSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 227227Cytochrome c oxidase subunit 2PRO_0000183677Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei218 – 2181PhosphotyrosineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP00406.
PRIDEiP00406.

PTM databases

iPTMnetiP00406.

Expressioni

Gene expression databases

ExpressionAtlasiP00406. baseline.
GenevisibleiP00406. RN.

Interactioni

Protein-protein interaction databases

MINTiMINT-4996308.
STRINGi10116.ENSRNOP00000046414.

Structurei

3D structure databases

ProteinModelPortaliP00406.
SMRiP00406. Positions 1-227.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4767. Eukaryota.
COG1622. LUCA.
HOGENOMiHOG000264988.
HOVERGENiHBG012727.
InParanoidiP00406.
KOiK02261.
OMAiMDEINNP.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171M → I in AAP31514 (PubMed:7981121).Curated
Sequence conflicti21 – 211T → M in AAA67374 (PubMed:6285344).Curated
Sequence conflicti29 – 291M → I in AAP31514 (PubMed:7981121).Curated
Sequence conflicti45 – 451M → I in AAP31514 (PubMed:7981121).Curated
Sequence conflicti56 – 561M → I in AAP31514 (PubMed:7981121).Curated
Sequence conflicti59 – 591Q → H in AAA67314 (PubMed:1848093).Curated
Sequence conflicti130 – 1301P → L no nucleotide entry (Ref. 4) Curated
Sequence conflicti130 – 1301P → L in AAA67314 (PubMed:1848093).Curated
Sequence conflicti164 – 1641A → P no nucleotide entry (Ref. 4) Curated
Sequence conflicti164 – 1641A → P in AAA67314 (PubMed:1848093).Curated
Sequence conflicti165 – 1651V → I in AAB00992 (PubMed:6091655).Curated
Sequence conflicti165 – 1651V → I in CAA32957 (PubMed:2504926).Curated
Sequence conflicti165 – 1651V → I in AAA67314 (PubMed:1848093).Curated
Sequence conflicti179 – 1791L → P in AAA67314 (PubMed:1848093).Curated
Sequence conflicti189 – 1891P → L no nucleotide entry (Ref. 4) Curated
Sequence conflicti189 – 1891P → L in AAA67314 (PubMed:1848093).Curated
Sequence conflicti208 – 2081P → L no nucleotide entry (Ref. 4) Curated
Sequence conflicti208 – 2081P → L in AAA67314 (PubMed:1848093).Curated
Sequence conflicti218 – 2181Y → H in AAA67374 (PubMed:6285344).Curated

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.
SMRiP00406. Positions 1-227.
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.
HOGENOMiHOG000264988.
HOVERGENiHBG012727.
InParanoidiP00406.
KOiK02261.
OMAiMDEINNP.

Miscellaneous databases

PROiP00406.

Gene expression databases

ExpressionAtlasiP00406. baseline.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Novel features of animal mtDNA evolution as shown by sequences of two rat cytochrome oxidase subunit II genes."
    Brown G.G., Simpson M.V.
    Proc. Natl. Acad. Sci. U.S.A. 79:3246-3250(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: R.norvegicus and R.rattus.
  2. "Non-random patterns of nucleotide substitutions and codon strategy in the mammalian mitochondrial genes coding for identified and unidentified reading frames."
    Pepe G., Holtrop M., Gadaleta G., Kroon A.M., Cantatore P., Gallerani R., de Benedetto C., Quagliariello C., Sbisa E., Saccone C.
    Biochem. Int. 6:553-563(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Wistar.
  3. "The complete nucleotide sequence of the Rattus norvegicus mitochondrial genome: cryptic signals revealed by comparative analysis between vertebrates."
    Gadaleta G., Pepe G., de Candia G., Quagliariello C., Sbisa E., Saccone C.
    J. Mol. Evol. 28:497-516(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Wistar.
  4. "Analysis of a DNA segment from rat liver mitochondria containing the genes for the cytochrome oxidase subunits I, II, II, ATPase subunit 6, and several tRNA genes."
    Grosskopf R., Feldmann H.
    Curr. Genet. 4:151-158(1981)
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Sprague-Dawley.
    Tissue: Liver.
  5. "Conversion of a mitochondrial gene for mammalian cytochrome c oxidase subunit II into its universal codon equivalent and expression in vivo and in vitro."
    Cao J.L., Revzin A., Ferguson-Miller S.
    Biochemistry 30:2642-2650(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  7. "Hormonal regulation of hypothalamic gene expression: identification of multiple novel estrogen induced genes."
    Law S.W., Apostolakis E.M., Samora P.J., O'Malley B.W., Clark J.H.
    J. Steroid Biochem. Mol. Biol. 51:131-136(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-56.
  8. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

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: June 8, 2016
This is version 138 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.