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Protein

Cytochrome c oxidase subunit 5A, mitochondrial

Gene

COX5A

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

This is the heme A-containing chain of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.

GO - Molecular functioni

  1. cytochrome-c oxidase activity Source: AgBase
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. hydrogen ion transmembrane transport Source: GOC
Complete GO annotation...

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.9.3.1. 908.
ReactomeiREACT_281214. Respiratory electron transport.
REACT_321619. Orphan transporters.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome c oxidase subunit 5A, mitochondrial
Alternative name(s):
Cytochrome c oxidase polypeptide Va
Gene namesi
Name:COX5A
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Chromosome 21

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. mitochondrial inner membrane Source: AgBase
  3. mitochondrion Source: AgBase
  4. respiratory chain complex IV Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4343Mitochondrion2 PublicationsAdd
BLAST
Chaini44 – 152109Cytochrome c oxidase subunit 5A, mitochondrialPRO_0000006099Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei89 – 891N6-acetyllysineBy similarity
Modified residuei115 – 1151N6-acetyllysineBy similarity
Modified residuei143 – 1431PhosphothreonineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP00426.
PRIDEiP00426.

2D gel databases

UCD-2DPAGEP00426.

Interactioni

Protein-protein interaction databases

DIPiDIP-38982N.
IntActiP00426. 2 interactions.

Structurei

Secondary structure

1
152
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi51 – 6212Combined sources
Helixi69 – 7911Combined sources
Beta strandi82 – 843Combined sources
Helixi88 – 10013Combined sources
Helixi104 – 11714Combined sources
Turni118 – 1203Combined sources
Helixi124 – 13916Combined sources
Turni144 – 1507Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OCCX-ray2.80E/R44-152[»]
1OCOX-ray2.80E/R44-152[»]
1OCRX-ray2.35E/R44-152[»]
1OCZX-ray2.90E/R44-152[»]
1V54X-ray1.80E/R44-152[»]
1V55X-ray1.90E/R44-152[»]
2DYRX-ray1.80E/R44-152[»]
2DYSX-ray2.20E/R44-152[»]
2EIJX-ray1.90E/R44-152[»]
2EIKX-ray2.10E/R44-152[»]
2EILX-ray2.10E/R44-152[»]
2EIMX-ray2.60E/R44-152[»]
2EINX-ray2.70E/R44-152[»]
2OCCX-ray2.30E/R44-152[»]
2Y69X-ray1.95E/R1-152[»]
2YBBelectron microscopy19.00P44-152[»]
2ZXWX-ray2.50E/R44-152[»]
3ABKX-ray2.00E/R44-152[»]
3ABLX-ray2.10E/R44-152[»]
3ABMX-ray1.95E/R44-152[»]
3AG1X-ray2.20E/R44-152[»]
3AG2X-ray1.80E/R44-152[»]
3AG3X-ray1.80E/R44-152[»]
3AG4X-ray2.05E/R44-152[»]
3ASNX-ray3.00E/R44-152[»]
3ASOX-ray2.30E/R44-152[»]
3WG7X-ray1.90E/R44-152[»]
SMRiP00426. Positions 44-152.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00426.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiNOG284808.
GeneTreeiENSGT00390000001424.
HOGENOMiHOG000160656.
HOVERGENiHBG051088.
InParanoidiP00426.
KOiK02264.
OMAiSIRCYSH.
OrthoDBiEOG74J99R.
TreeFamiTF105062.

Family and domain databases

Gene3Di1.25.40.40. 1 hit.
InterProiIPR003204. Cyt_c_oxidase_su5A/6.
[Graphical view]
PANTHERiPTHR14200. PTHR14200. 1 hit.
PfamiPF02284. COX5A. 1 hit.
[Graphical view]
SUPFAMiSSF48479. SSF48479. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00426-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLGAAVRRCS VAAAAVARAS PRGLLHPTPA PGQAAAVQSL RCYSHGSHET
60 70 80 90 100
DEEFDARWVT YFNKPDIDAW ELRKGMNTLV GYDLVPEPKI IDAALRACRR
110 120 130 140 150
LNDFASAVRI LEVVKDKAGP HKEIYPYVIQ ELRPTLNELG ISTPEELGLD

KV
Length:152
Mass (Da):16,735
Last modified:October 25, 2004 - v2
Checksum:iCE8FA765A8ABBA02
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY528254 mRNA. Translation: AAS20602.1.
BC109608 mRNA. Translation: AAI09609.1.
PIRiA00493. CABO.
RefSeqiNP_001002891.1. NM_001002891.1.
XP_005221971.1. XM_005221914.2.
UniGeneiBt.55686.

Genome annotation databases

EnsembliENSBTAT00000022949; ENSBTAP00000022949; ENSBTAG00000017267.
GeneIDi444878.
KEGGibta:444878.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY528254 mRNA. Translation: AAS20602.1.
BC109608 mRNA. Translation: AAI09609.1.
PIRiA00493. CABO.
RefSeqiNP_001002891.1. NM_001002891.1.
XP_005221971.1. XM_005221914.2.
UniGeneiBt.55686.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OCCX-ray2.80E/R44-152[»]
1OCOX-ray2.80E/R44-152[»]
1OCRX-ray2.35E/R44-152[»]
1OCZX-ray2.90E/R44-152[»]
1V54X-ray1.80E/R44-152[»]
1V55X-ray1.90E/R44-152[»]
2DYRX-ray1.80E/R44-152[»]
2DYSX-ray2.20E/R44-152[»]
2EIJX-ray1.90E/R44-152[»]
2EIKX-ray2.10E/R44-152[»]
2EILX-ray2.10E/R44-152[»]
2EIMX-ray2.60E/R44-152[»]
2EINX-ray2.70E/R44-152[»]
2OCCX-ray2.30E/R44-152[»]
2Y69X-ray1.95E/R1-152[»]
2YBBelectron microscopy19.00P44-152[»]
2ZXWX-ray2.50E/R44-152[»]
3ABKX-ray2.00E/R44-152[»]
3ABLX-ray2.10E/R44-152[»]
3ABMX-ray1.95E/R44-152[»]
3AG1X-ray2.20E/R44-152[»]
3AG2X-ray1.80E/R44-152[»]
3AG3X-ray1.80E/R44-152[»]
3AG4X-ray2.05E/R44-152[»]
3ASNX-ray3.00E/R44-152[»]
3ASOX-ray2.30E/R44-152[»]
3WG7X-ray1.90E/R44-152[»]
SMRiP00426. Positions 44-152.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-38982N.
IntActiP00426. 2 interactions.

2D gel databases

UCD-2DPAGEP00426.

Proteomic databases

PaxDbiP00426.
PRIDEiP00426.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000022949; ENSBTAP00000022949; ENSBTAG00000017267.
GeneIDi444878.
KEGGibta:444878.

Organism-specific databases

CTDi9377.

Phylogenomic databases

eggNOGiNOG284808.
GeneTreeiENSGT00390000001424.
HOGENOMiHOG000160656.
HOVERGENiHBG051088.
InParanoidiP00426.
KOiK02264.
OMAiSIRCYSH.
OrthoDBiEOG74J99R.
TreeFamiTF105062.

Enzyme and pathway databases

BRENDAi1.9.3.1. 908.
ReactomeiREACT_281214. Respiratory electron transport.
REACT_321619. Orphan transporters.

Miscellaneous databases

EvolutionaryTraceiP00426.
NextBioi20831766.

Family and domain databases

Gene3Di1.25.40.40. 1 hit.
InterProiIPR003204. Cyt_c_oxidase_su5A/6.
[Graphical view]
PANTHERiPTHR14200. PTHR14200. 1 hit.
PfamiPF02284. COX5A. 1 hit.
[Graphical view]
SUPFAMiSSF48479. SSF48479. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of gene expression in the bovine blastocyst or hatched blastocyst in vitro using ACP method."
    Shin M.L., Cui X.S., Park S.Y., Kim E.Y., Park S.P., Lee W.J., Hwang K.C., Kim N.H.
    Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Liver.
  3. "Amino acid sequence of subunit V of bovine heart cytochrome oxidase, the heme alpha-containing subunit."
    Tanaka M., Haniu M., Yasunobu K.T., Yu C.-A., Yu L., Wei Y.-H., King T.E.
    J. Biol. Chem. 254:3879-3885(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 44-152.
    Tissue: Heart.
  4. "Tissue-specific differences between heart and liver cytochrome c oxidase."
    Yanamura W., Zhang Y.-Z., Takamiya S., Capaldi R.A.
    Biochemistry 27:4909-4914(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 44-77.
    Tissue: Liver.
  5. "The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A."
    Tsukihara T., Aoyama H., Yamashita E., Tomizaki T., Yamaguchi H., Shinzawa-Itoh K., Nakashima R., Yaono R., Yoshikawa S.
    Science 272:1136-1144(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 44-152.
  6. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 44-152.
    Tissue: Heart.
  7. "X-ray structure of azide-bound fully oxidized cytochrome c oxidase from bovine heart at 2.9 A resolution."
    Fei M.J., Yamashita E., Inoue N., Yao M., Yamaguchi H., Tsukihara T., Shinzawa-Itoh K., Nakashima R., Yoshikawa S.
    Acta Crystallogr. D 56:529-535(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 44-152.
    Tissue: Heart.

Entry informationi

Entry nameiCOX5A_BOVIN
AccessioniPrimary (citable) accession number: P00426
Secondary accession number(s): Q32LF6, Q6QRN2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 25, 2004
Last modified: April 1, 2015
This is version 120 of the entry and version 2 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

External Data

Dasty 3

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 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.