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Protein

Cytochrome c oxidase subunit 2

Gene

MT-CO2

Organism
Bos taurus (Bovine)
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 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

Complete GO annotation...

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Keywords - Ligandi

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

Subcellular locationi

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

GO - Cellular componenti

Complete GO annotation...

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. differential.

Interactioni

Protein-protein interaction databases

DIPiDIP-39024N.
IntActiP68530. 1 interactor.
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[»]
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.
OMAiVVLPMEM.
OrthoDBiEOG091G0IO9.
TreeFamiTF344269.

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.

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.

Cross-referencesi

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.

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[»]
ProteinModelPortaliP68530.
SMRiP68530.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-39024N.
IntActiP68530. 1 interactor.
STRINGi9913.ENSBTAP00000053151.

Protein family/group databases

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

PTM databases

iPTMnetiP68530.

Proteomic databases

PaxDbiP68530.
PeptideAtlasiP68530.
PRIDEiP68530.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000060549; ENSBTAP00000053151; ENSBTAG00000043556.
GeneIDi3283880.
KEGGibta:3283880.

Organism-specific databases

CTDi4513.

Phylogenomic databases

eggNOGiKOG4767. Eukaryota.
COG1622. LUCA.
GeneTreeiENSGT00390000017410.
HOGENOMiHOG000264988.
HOVERGENiHBG012727.
InParanoidiP68530.
KOiK02261.
OMAiVVLPMEM.
OrthoDBiEOG091G0IO9.
TreeFamiTF344269.

Miscellaneous databases

EvolutionaryTraceiP68530.

Gene expression databases

BgeeiENSBTAG00000043556.
ExpressionAtlasiP68530. differential.

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_BOVIN
AccessioniPrimary (citable) accession number: P68530
Secondary accession number(s): P00404
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 30, 2016
This is version 106 of the entry and version 1 of the sequence. [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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.