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Protein

Cytochrome c oxidase subunit 2

Gene

MT-CO2

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -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 A11
Metal bindingi196Copper A11
Metal bindingi196Copper A21
Metal bindingi198Copper A2; via carbonyl oxygen1
Metal bindingi198Magnesium; shared with chain I1
Metal bindingi200Copper A11
Metal bindingi200Copper A21
Metal bindingi204Copper A21
Metal bindingi207Copper A11

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processElectron transport, Respiratory chain, Transport
LigandCopper, Metal-binding

Protein family/group databases

TCDBi3.D.4.7.1 the proton-translocating cytochrome oxidase (cox) superfamily

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, COX2, COXII, MTCO2
Encoded oniMitochondrion
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Mitochondrion

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 14Mitochondrial intermembraneAdd BLAST14
Transmembranei15 – 45Helical; Name=IAdd BLAST31
Topological domaini46 – 59Mitochondrial matrixAdd BLAST14
Transmembranei60 – 87Helical; Name=IIAdd BLAST28
Topological domaini88 – 227Mitochondrial intermembraneAdd BLAST140

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001835171 – 227Cytochrome c oxidase subunit 2Add BLAST227

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-formylmethionine1 Publication1
Modified residuei218PhosphotyrosineBy similarity1

Keywords - PTMi

Formylation, Phosphoprotein

Proteomic databases

PaxDbiP68530
PeptideAtlasiP68530
PRIDEiP68530

PTM databases

iPTMnetiP68530

Expressioni

Gene expression databases

BgeeiENSBTAG00000043556
ExpressionAtlasiP68530 baseline

Interactioni

Subunit structurei

Found in a complex with TMEM177, COA6, COX18, COX20, SCO1 and SCO2. Interacts with TMEM177 in a COX20-dependent manner. Interacts with COX20. Interacts with COX16.By similarity

Protein-protein interaction databases

CORUMiP68530
DIPiDIP-39024N
IntActiP68530, 2 interactors
STRINGi9913.ENSBTAP00000053151

Structurei

Secondary structure

1227
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi15 – 45Combined sources31
Helixi59 – 88Combined sources30
Beta strandi94 – 102Combined sources9
Beta strandi105 – 110Combined sources6
Beta strandi112 – 114Combined sources3
Beta strandi116 – 120Combined sources5
Helixi125 – 127Combined sources3
Turni134 – 136Combined sources3
Beta strandi138 – 140Combined sources3
Beta strandi142 – 145Combined sources4
Beta strandi150 – 159Combined sources10
Beta strandi161 – 165Combined sources5
Helixi166 – 168Combined sources3
Beta strandi170 – 174Combined sources5
Beta strandi180 – 184Combined sources5
Beta strandi190 – 195Combined sources6
Helixi204 – 206Combined sources3
Beta strandi208 – 214Combined sources7
Helixi216 – 225Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OCCX-ray2.80B/O1-227[»]
1OCOX-ray2.80B/O1-227[»]
1OCRX-ray2.35B/O1-227[»]
1OCZX-ray2.90B/O1-227[»]
1V54X-ray1.80B/O1-227[»]
1V55X-ray1.90B/O1-227[»]
2DYRX-ray1.80B/O1-227[»]
2DYSX-ray2.20B/O1-227[»]
2EIJX-ray1.90B/O1-227[»]
2EIKX-ray2.10B/O1-227[»]
2EILX-ray2.10B/O1-227[»]
2EIMX-ray2.60B/O1-227[»]
2EINX-ray2.70B/O1-227[»]
2OCCX-ray2.30B/O1-227[»]
2Y69X-ray1.95B/O1-227[»]
2YBBelectron microscopy19.00M1-227[»]
2ZXWX-ray2.50B/O1-227[»]
3ABKX-ray2.00B/O1-227[»]
3ABLX-ray2.10B/O1-227[»]
3ABMX-ray1.95B/O1-227[»]
3AG1X-ray2.20B/O1-227[»]
3AG2X-ray1.80B/O1-227[»]
3AG3X-ray1.80B/O1-227[»]
3AG4X-ray2.05B/O1-227[»]
3ASNX-ray3.00B/O1-227[»]
3ASOX-ray2.30B/O1-227[»]
3WG7X-ray1.90B/O1-227[»]
3X2QX-ray2.00B/O1-227[»]
5B1AX-ray1.50B/O1-227[»]
5B1BX-ray1.60B/O1-227[»]
5B3SX-ray1.68B/O2-227[»]
5GPNelectron microscopy5.40z1-227[»]
5IY5X-ray2.00B/O1-227[»]
5LUFelectron microscopy9.10y1-227[»]
5W97X-ray2.30B/b1-227[»]
5WAUX-ray1.95B/b1-227[»]
5X19X-ray2.20B/O1-227[»]
5X1BX-ray2.40B/O1-227[»]
5X1FX-ray2.20B/O1-227[»]
5XDQX-ray1.77B/O1-227[»]
5XDXX-ray1.99B/O1-227[»]
5XTHelectron microscopy3.90y1-227[»]
5XTIelectron microscopy17.40By/y1-227[»]
ProteinModelPortaliP68530
SMRiP68530
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP68530

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4767 Eukaryota
COG1622 LUCA
GeneTreeiENSGT00390000017410
HOGENOMiHOG000264988
HOVERGENiHBG012727
InParanoidiP68530
KOiK02261
OMAiWSYEYTD
OrthoDBiEOG091G0IO9
TreeFamiTF344269

Family and domain databases

CDDicd13912 CcO_II_C, 1 hit
Gene3Di1.10.287.90, 1 hit
2.60.40.420, 1 hit
InterProiView protein in InterPro
IPR002429 CcO_II-like_C
IPR034210 CcO_II_C
IPR001505 Copper_CuA
IPR008972 Cupredoxin
IPR014222 Cyt_c_oxidase_su2
IPR011759 Cyt_c_oxidase_su2_TM_dom
IPR036257 Cyt_c_oxidase_su2_TM_sf
PfamiView protein in Pfam
PF00116 COX2, 1 hit
PF02790 COX2_TM, 1 hit
SUPFAMiSSF49503 SSF49503, 1 hit
SSF81464 SSF81464, 1 hit
TIGRFAMsiTIGR02866 CoxB, 1 hit
PROSITEiView protein in PROSITE
PS00078 COX2, 1 hit
PS50857 COX2_CUA, 1 hit
PS50999 COX2_TM, 1 hit

Sequencei

Sequence statusi: Complete.

P68530-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAYPMQLGFQ DATSPIMEEL LHFHDHTLMI VFLISSLVLY IISLMLTTKL
60 70 80 90 100
THTSTMDAQE VETIWTILPA IILILIALPS LRILYMMDEI NNPSLTVKTM
110 120 130 140 150
GHQWYWSYEY TDYEDLSFDS YMIPTSELKP GELRLLEVDN RVVLPMEMTI
160 170 180 190 200
RMLVSSEDVL HSWAVPSLGL KTDAIPGRLN QTTLMSSRPG LYYGQCSEIC
210 220
GSNHSFMPIV LELVPLKYFE KWSASML
Length:227
Mass (Da):26,021
Last modified:July 21, 1986 - v1
Checksum:iC562D5B39FA9771A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti58A → P in AAA31644 (PubMed:6265319).Curated1
Sequence conflicti118F → L in AAA31644 (PubMed:6265319).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00654 Genomic DNA Translation: CAA24000.1
M10544 Genomic DNA Translation: AAA31644.1
AF490528 Genomic DNA Translation: AAM08331.1
AF490529 Genomic DNA Translation: AAM08344.1
AF493541 Genomic DNA Translation: AAM12792.1
AF493542 Genomic DNA Translation: AAM12805.1
PIRiB00152 OBBO2
RefSeqiYP_209208.1, NC_006853.1

Genome annotation databases

EnsembliENSBTAT00000060549; ENSBTAP00000053151; ENSBTAG00000043556
GeneIDi3283880
KEGGibta:3283880

Similar proteinsi

Entry informationi

Entry nameiCOX2_BOVIN
AccessioniPrimary (citable) accession number: P68530
Secondary accession number(s): P00404
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: March 28, 2018
This is version 115 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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