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Protein

Cytochrome c oxidase subunit 2

Gene

MT-CO2

Organism
Gerbillurus vallinus (Brush-tailed hairy-footed gerbil)
Status
Reviewed-Annotation score: 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.

Cofactori

Cu cationNote: Binds a copper A center.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi161 – 1611Copper ABy similarity
Metal bindingi196 – 1961Copper ABy similarity
Metal bindingi200 – 2001Copper ABy similarity
Metal bindingi204 – 2041Copper ABy similarity

GO - Molecular functioni

GO - Biological processi

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:MT-CO2
Synonyms:COII, COXII, MTCO2
Encoded oniMitochondrion
OrganismiGerbillurus vallinus (Brush-tailed hairy-footed gerbil)
Taxonomic identifieri49440 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeGerbillinaeGerbillurus

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_0000254922Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ37476.
SMRiQ37476. Positions 1-227.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG012727.

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.

Q37476-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAYPFQLGLQ DATSPIMEEL TNFHDHTLMI VFLISSLVLY LISLMLTTKL
60 70 80 90 100
IHTNTMDAQE VETVWTILPA IILIMIALPS LRILYLMDEI NNPVLTVKTM
110 120 130 140 150
GHQWYWSYEY TDYEDLCFDS YMTPTNELKP GELRLLEVDN RVVLPMELPI
160 170 180 190 200
RMLISSEDVL HSWAVPSLGL KTDAIPGRLN QATITSNRPG VFYGQCSEIC
210 220
GSNHSFMPIV LEMIPLKLFE NWSTSMI
Length:227
Mass (Da):25,963
Last modified:November 1, 1996 - v1
Checksum:i62B99D2863960086
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U62574 Genomic DNA. Translation: AAB05785.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U62574 Genomic DNA. Translation: AAB05785.1.

3D structure databases

ProteinModelPortaliQ37476.
SMRiQ37476. Positions 1-227.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG012727.

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

  1. "Evolution of eutherian cytochrome c oxidase subunit II: heterogeneous rates of protein evolution and altered interaction with cytochrome c."
    Adkins R.M., Honeycutt R.L., Disotell T.R.
    Mol. Biol. Evol. 13:1393-1404(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiCOX2_GERVA
AccessioniPrimary (citable) accession number: Q37476
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: November 1, 1996
Last modified: October 14, 2015
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.