Cytochrome c oxidase subunit 4 isoform 1, mitochondrial precursor

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P00423 (COX41_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 97. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	COX4I1
Synonyms:	COX4

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	169 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
Subcellular location	Mitochondrion inner membrane.
Sequence similarities	Belongs to the cytochrome c oxidase IV family.

Ontologies

Keywords
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide Transmembrane Transmembrane helix
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial respiratory chain complex IV Inferred from direct assay. Source: MGI
Molecular function	cytochrome-c oxidase activity Inferred from direct assay. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 22

Mitochondrion Ref.5 Ref.6

Chain

23 – 169

147

Cytochrome c oxidase subunit 4 isoform 1, mitochondrial

PRO_0000006083

Regions

Topological domain

23 – 98

Mitochondrial matrix

Transmembrane

99 – 124

Helical

Topological domain

125 – 169

Mitochondrial intermembrane

Amino acid modifications

Modified residue

N6-acetyllysine By similarity

Modified residue

N6-acetyllysine By similarity

Secondary structure

169

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P00423 [UniParc].

Last modified October 23, 1986. Version 1.
Checksum: 76D2B2D15F8D02A1
Show »

FASTA

169

19,572

        10         20         30         40         50         60 
MLATRVFSLI GRRAISTSVC VRAHGSVVKS EDYALPSYVD RRDYPLPDVA HVKNLSASQK 

        70         80         90        100        110        120 
ALKEKEKASW SSLSIDEKVE LYRLKFKESF AEMNRSTNEW KTVVGAAMFF IGFTALLLIW 

       130        140        150        160 
EKHYVYGPIP HTFEEEWVAK QTKRMLDMKV APIQGFSAKW DYDKNEWKK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of the functional gene encoding bovine cytochrome c oxidase subunit IV." Bachman N.J. Gene 162:313-318(1995) [PubMed: 7557450] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Characterization of 954 bovine full-CDS cDNA sequences." Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L. BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract] 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: 6093095] [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: 227780] [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: 227779] [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: 8638158] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[8]	"Structure analysis of bovine heart cytochrome c oxidase at 2.8 A resolution." Tomizaki T., Yamashita E., Yamaguchi H., Aoyama H., Tsukihara T., Shinzawa-Itoh K., Nakashima R., Yaono R., Yoshikawa S. Acta Crystallogr. D 55:31-45(1999) [PubMed: 10089392] [Abstract] 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: 10771420] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS). Tissue: Heart.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L34015

L34014 Genomic DNA. Translation: AAA30461.1.
U11070

U11069 Genomic DNA. Translation: AAA93149.1.
BT021029 mRNA. Translation: AAX09046.1.
BC102733 mRNA. Translation: AAI02734.1.
K02064 mRNA. Translation: AAA30463.1.

IPI

IPI00714240.

PIR

OLBO4. A30618.

RefSeq

NP_001001439.1. NM_001001439.2.

UniGene

Bt.16025.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OCC	X-ray	2.80	D/Q	23-169	[»]
1OCO	X-ray	2.80	D/Q	23-169	[»]
1OCR	X-ray	2.35	D/Q	23-169	[»]
1OCZ	X-ray	2.90	D/Q	23-169	[»]
1V54	X-ray	1.80	D/Q	23-169	[»]
1V55	X-ray	1.90	D/Q	23-169	[»]
2DYR	X-ray	1.80	D/Q	23-169	[»]
2DYS	X-ray	2.20	D/Q	23-169	[»]
2EIJ	X-ray	1.90	D/Q	23-169	[»]
2EIK	X-ray	2.10	D/Q	23-169	[»]
2EIL	X-ray	2.10	D/Q	23-169	[»]
2EIM	X-ray	2.60	D/Q	23-169	[»]
2EIN	X-ray	2.70	D/Q	23-169	[»]
2OCC	X-ray	2.30	D/Q	23-169	[»]
2Y69	X-ray	1.95	D/Q	1-169	[»]
2YBB	electron microscopy	19.00	O	23-169	[»]
2ZXW	X-ray	2.50	D/Q	23-169	[»]
3ABK	X-ray	2.00	D/Q	23-169	[»]
3ABL	X-ray	2.10	D/Q	23-169	[»]
3ABM	X-ray	1.95	D/Q	23-169	[»]
3AG1	X-ray	2.20	D/Q	23-169	[»]
3AG2	X-ray	1.80	D/Q	23-169	[»]
3AG3	X-ray	1.80	D/Q	23-169	[»]
3AG4	X-ray	2.05	D/Q	23-169	[»]
3ASN	X-ray	3.00	D/Q	23-169	[»]
3ASO	X-ray	2.30	D/Q	23-169	[»]

ProteinModelPortal

P00423.

SMR

P00423. Positions 26-169.

ModBase

Search...

Protein-protein interaction databases

IntAct

P00423. 2 interactions.

Proteomic databases

PRIDE

P00423.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000021397; ENSBTAP00000021397; ENSBTAG00000016079.
ENSBTAT00000053881; ENSBTAP00000049613; ENSBTAG00000016079.

GeneID

281090.

KEGG

bta:281090.

Organism-specific databases

CTD

1327.

Phylogenomic databases

eggNOG

maNOG05911.

HOVERGEN

HBG051087.

Family and domain databases

InterPro

IPR004203. Cyt_c_oxidase_su4.
IPR013288. Cyt_c_oxidase_su4_subgr.
[Graphical view]

Gene3D

G3DSA:1.10.442.10. COX4. 1 hit.

K02263.

Pfam

PF02936. COX4. 1 hit.
[Graphical view]

PRINTS

PR01873. CYTCOXIDASE4.

SUPFAM

SSF81406. COX4. 1 hit.

ProtoNet

Search...

Entry information

Entry name

COX41_BOVIN

Accession

Primary (citable) accession number: P00423
Secondary accession number(s): Q3SZS0, Q5E991

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	October 23, 1986
Last modified:	January 25, 2012
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents