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Protein

Cytochrome c oxidase subunit 4 isoform 1, mitochondrial

Gene

COX4I1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.

GO - Molecular functioni

  1. cytochrome-c oxidase activity Source: MGI

GO - Biological processi

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

Enzyme and pathway databases

ReactomeiREACT_223064. Respiratory electron transport.
REACT_271057. Orphan transporters.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
Alternative name(s):
Cytochrome c oxidase polypeptide IV
Cytochrome c oxidase subunit IV isoform 1
Short name:
COX IV-1
Gene namesi
Name:COX4I1
Synonyms:COX4
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 18

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 9876Mitochondrial matrixAdd
BLAST
Transmembranei99 – 12426HelicalAdd
BLAST
Topological domaini125 – 16945Mitochondrial intermembraneAdd
BLAST

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. integral component of membrane Source: UniProtKB-KW
  3. mitochondrial respiratory chain complex IV Source: MGI
  4. nucleus Source: Ensembl
  5. 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 – 2222Mitochondrion2 PublicationsAdd
BLAST
Chaini23 – 169147Cytochrome c oxidase subunit 4 isoform 1, mitochondrialPRO_0000006083Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei29 – 291N6-acetyllysine; alternateBy similarity
Modified residuei29 – 291N6-succinyllysine; alternateBy similarity
Modified residuei53 – 531N6-acetyllysineBy similarity
Modified residuei60 – 601N6-acetyllysine; alternateBy similarity
Modified residuei60 – 601N6-succinyllysine; alternateBy similarity
Modified residuei67 – 671N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP00423.

Interactioni

Protein-protein interaction databases

DIPiDIP-38979N.
IntActiP00423. 2 interactions.

Structurei

Secondary structure

1
169
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi30 – 323Combined sources
Beta strandi44 – 463Combined sources
Helixi57 – 659Combined sources
Helixi70 – 723Combined sources
Helixi75 – 8511Combined sources
Helixi90 – 934Combined sources
Helixi99 – 12426Combined sources
Helixi131 – 1333Combined sources
Helixi135 – 14713Combined sources
Turni152 – 1554Combined sources
Helixi157 – 1593Combined sources
Turni162 – 1654Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OCCX-ray2.80D/Q23-169[»]
1OCOX-ray2.80D/Q23-169[»]
1OCRX-ray2.35D/Q23-169[»]
1OCZX-ray2.90D/Q23-169[»]
1V54X-ray1.80D/Q23-169[»]
1V55X-ray1.90D/Q23-169[»]
2DYRX-ray1.80D/Q23-169[»]
2DYSX-ray2.20D/Q23-169[»]
2EIJX-ray1.90D/Q23-169[»]
2EIKX-ray2.10D/Q23-169[»]
2EILX-ray2.10D/Q23-169[»]
2EIMX-ray2.60D/Q23-169[»]
2EINX-ray2.70D/Q23-169[»]
2OCCX-ray2.30D/Q23-169[»]
2Y69X-ray1.95D/Q1-169[»]
2YBBelectron microscopy19.00O23-169[»]
2ZXWX-ray2.50D/Q23-169[»]
3ABKX-ray2.00D/Q23-169[»]
3ABLX-ray2.10D/Q23-169[»]
3ABMX-ray1.95D/Q23-169[»]
3AG1X-ray2.20D/Q23-169[»]
3AG2X-ray1.80D/Q23-169[»]
3AG3X-ray1.80D/Q23-169[»]
3AG4X-ray2.05D/Q23-169[»]
3ASNX-ray3.00D/Q23-169[»]
3ASOX-ray2.30D/Q23-169[»]
3WG7X-ray1.90D/Q23-169[»]
ProteinModelPortaliP00423.
SMRiP00423. Positions 26-169.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00423.

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome c oxidase IV family.Curated

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000002407.
HOVERGENiHBG051087.
InParanoidiP00423.
KOiK02263.
OMAiPAYVDRR.
OrthoDBiEOG7BKCWF.
TreeFamiTF105061.

Family and domain databases

Gene3Di1.10.442.10. 1 hit.
InterProiIPR013288. Cyt_c_oxidase_su4.
IPR004203. Cyt_c_oxidase_su4_fam.
[Graphical view]
PANTHERiPTHR10707. PTHR10707. 1 hit.
PfamiPF02936. COX4. 1 hit.
[Graphical view]
PRINTSiPR01873. CYTCOXIDASE4.
SUPFAMiSSF81406. SSF81406. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P00423-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLATRVFSLI GRRAISTSVC VRAHGSVVKS EDYALPSYVD RRDYPLPDVA
60 70 80 90 100
HVKNLSASQK ALKEKEKASW SSLSIDEKVE LYRLKFKESF AEMNRSTNEW
110 120 130 140 150
KTVVGAAMFF IGFTALLLIW EKHYVYGPIP HTFEEEWVAK QTKRMLDMKV
160
APIQGFSAKW DYDKNEWKK
Length:169
Mass (Da):19,572
Last modified:October 23, 1986 - v1
Checksum:i76D2B2D15F8D02A1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34015
, L34012, L34013, L34014 Genomic DNA. Translation: AAA30461.1.
U11070
, U11067, U11068, U11069 Genomic DNA. Translation: AAA93149.1.
BT021029 mRNA. Translation: AAX09046.1.
BC102733 mRNA. Translation: AAI02734.1.
K02064 mRNA. Translation: AAA30463.1.
PIRiA30618. OLBO4.
RefSeqiNP_001001439.1. NM_001001439.3.
XP_005218495.1. XM_005218438.1.
UniGeneiBt.107085.
Bt.16025.

Genome annotation databases

EnsembliENSBTAT00000021397; ENSBTAP00000021397; ENSBTAG00000016079.
ENSBTAT00000053881; ENSBTAP00000049613; ENSBTAG00000016079.
GeneIDi281090.
KEGGibta:281090.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34015
, L34012, L34013, L34014 Genomic DNA. Translation: AAA30461.1.
U11070
, U11067, U11068, U11069 Genomic DNA. Translation: AAA93149.1.
BT021029 mRNA. Translation: AAX09046.1.
BC102733 mRNA. Translation: AAI02734.1.
K02064 mRNA. Translation: AAA30463.1.
PIRiA30618. OLBO4.
RefSeqiNP_001001439.1. NM_001001439.3.
XP_005218495.1. XM_005218438.1.
UniGeneiBt.107085.
Bt.16025.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OCCX-ray2.80D/Q23-169[»]
1OCOX-ray2.80D/Q23-169[»]
1OCRX-ray2.35D/Q23-169[»]
1OCZX-ray2.90D/Q23-169[»]
1V54X-ray1.80D/Q23-169[»]
1V55X-ray1.90D/Q23-169[»]
2DYRX-ray1.80D/Q23-169[»]
2DYSX-ray2.20D/Q23-169[»]
2EIJX-ray1.90D/Q23-169[»]
2EIKX-ray2.10D/Q23-169[»]
2EILX-ray2.10D/Q23-169[»]
2EIMX-ray2.60D/Q23-169[»]
2EINX-ray2.70D/Q23-169[»]
2OCCX-ray2.30D/Q23-169[»]
2Y69X-ray1.95D/Q1-169[»]
2YBBelectron microscopy19.00O23-169[»]
2ZXWX-ray2.50D/Q23-169[»]
3ABKX-ray2.00D/Q23-169[»]
3ABLX-ray2.10D/Q23-169[»]
3ABMX-ray1.95D/Q23-169[»]
3AG1X-ray2.20D/Q23-169[»]
3AG2X-ray1.80D/Q23-169[»]
3AG3X-ray1.80D/Q23-169[»]
3AG4X-ray2.05D/Q23-169[»]
3ASNX-ray3.00D/Q23-169[»]
3ASOX-ray2.30D/Q23-169[»]
3WG7X-ray1.90D/Q23-169[»]
ProteinModelPortaliP00423.
SMRiP00423. Positions 26-169.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-38979N.
IntActiP00423. 2 interactions.

Proteomic databases

PRIDEiP00423.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000021397; ENSBTAP00000021397; ENSBTAG00000016079.
ENSBTAT00000053881; ENSBTAP00000049613; ENSBTAG00000016079.
GeneIDi281090.
KEGGibta:281090.

Organism-specific databases

CTDi1327.

Phylogenomic databases

GeneTreeiENSGT00390000002407.
HOVERGENiHBG051087.
InParanoidiP00423.
KOiK02263.
OMAiPAYVDRR.
OrthoDBiEOG7BKCWF.
TreeFamiTF105061.

Enzyme and pathway databases

ReactomeiREACT_223064. Respiratory electron transport.
REACT_271057. Orphan transporters.

Miscellaneous databases

EvolutionaryTraceiP00423.
NextBioi20805164.

Family and domain databases

Gene3Di1.10.442.10. 1 hit.
InterProiIPR013288. Cyt_c_oxidase_su4.
IPR004203. Cyt_c_oxidase_su4_fam.
[Graphical view]
PANTHERiPTHR10707. PTHR10707. 1 hit.
PfamiPF02936. COX4. 1 hit.
[Graphical view]
PRINTSiPR01873. CYTCOXIDASE4.
SUPFAMiSSF81406. SSF81406. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of the functional gene encoding bovine cytochrome c oxidase subunit IV."
    Bachman N.J.
    Gene 162:313-318(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Liver.
  4. "Isolation and characterization of a cDNA clone for bovine cytochrome c oxidase subunit IV."
    Lomax M.I., Bachman N.J., Nasoff M.S., Caruthers M.H., Grossman L.I.
    Proc. Natl. Acad. Sci. U.S.A. 81:6295-6299(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-104.
  5. "Studies on cytochrome c oxidase, VI. Polypeptide IV: the complete primary structure."
    Sacher R., Steffens G.J., Buse G.
    Hoppe-Seyler's Z. Physiol. Chem. 360:1385-1392(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 23-109.
    Tissue: Heart.
  6. "Studies on cytochrome c oxidase, V. Polypeptide IV: alignment and amino acid sequences on cyanogen bromide fragments."
    Sacher R., Buse G., Steffens G.J.
    Hoppe-Seyler's Z. Physiol. Chem. 360:1377-1383(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 23-109.
    Tissue: Heart.
  7. "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(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
  8. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
    Tissue: Heart.
  9. "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(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
    Tissue: Heart.

Entry informationi

Entry nameiCOX41_BOVIN
AccessioniPrimary (citable) accession number: P00423
Secondary accession number(s): Q3SZS0, Q5E991
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 23, 1986
Last modified: January 7, 2015
This is version 119 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

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.