[1]	PROTEIN SEQUENCE OF 2-105, AND ACETYLATION AT GLY-2. TISSUE=Heart; PubMed=14469771 [NCBI, ExPASy, EBI, Israel, Japan] Margoliash E., Smith E.L., Kreil G., Tuppy H.; "Amino-acid sequence of horse heart cytochrome c."; Nature 192:1125-1127(1961).
[2]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). PubMed=5545094 [NCBI, ExPASy, EBI, Israel, Japan] Dickerson R.E., Takano T., Eisenberg D., Kallai O.B., Samson L., Cooper A., Margoliash E.; "Ferricytochrome c. I. General features of the horse and bonito proteins at 2.8-A resolution."; J. Biol. Chem. 246:1511-1533(1971).
[3]	X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). DOI=10.1016/0022-2836(90)90200-6; PubMed=2166170 [NCBI, ExPASy, EBI, Israel, Japan] Bushnell G.W., Louie G.V., Brayer G.D.; "High-resolution three-dimensional structure of horse heart cytochrome c."; J. Mol. Biol. 214:585-595(1990).
[4]	X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). DOI=10.1016/S0969-2126(01)00205-2; PubMed=8591047 [NCBI, ExPASy, EBI, Israel, Japan] Sanishvili R., Volz K.W., Westbrook E.M., Margoliash E.; "The low ionic strength crystal structure of horse cytochrome c at 2.1-A resolution and comparison with its high ionic strength counterpart."; Structure 3:707-716(1995).
[5]	STRUCTURE BY NMR. DOI=10.1021/bi00427a027; PubMed=2539855 [NCBI, ExPASy, EBI, Israel, Japan] Feng Y., Roder H., Englander S.W., Wand A.J., di Stefano D.L.; "Proton resonance assignments of horse ferricytochrome c."; Biochemistry 28:195-203(1989).
[6]	STRUCTURE BY NMR. DOI=10.1021/bi961042w; PubMed=8823161 [NCBI, ExPASy, EBI, Israel, Japan] Qi P.X., Beckman R.A., Wand A.J.; "Solution structure of horse heart ferricytochrome c and detection of redox-related structural changes by high-resolution 1H NMR."; Biochemistry 35:12275-12286(1996).
[7]	STRUCTURE BY NMR. TISSUE=Heart; DOI=10.1021/bi970724w; PubMed=9245419 [NCBI, ExPASy, EBI, Israel, Japan] Banci L., Bertini I., Gray H.B., Luchinat C., Reddig T., Rosato A., Turano P.; "Solution structure of oxidized horse heart cytochrome c."; Biochemistry 36:9867-9877(1997).

Comments

FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
SUBCELLULAR LOCATION: Mitochondrion matrix.
PTM: Binds 1 heme group per subunit.
MISCELLANEOUS: Mules and hinnies are heterozygous, having equal amount of horse and donkey cytochromes c.
SIMILARITY: Belongs to the cytochrome c family.
WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of November 2006; URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

PIR

A00005; CCHO.

3D structure databases

PDB

1AKK; NMR; -; A=1-105.	[ExPASy / RCSB / EBI]
1CRC; X-ray; 2.08 A; A/B=1-105.	[ExPASy / RCSB / EBI]
1FI7; NMR; -; A=1-105.	[ExPASy / RCSB / EBI]
1FI9; NMR; -; A=1-105.	[ExPASy / RCSB / EBI]
1GIW; NMR; -; A=1-105.	[ExPASy / RCSB / EBI]
1HRC; X-ray; 1.90 A; A=1-105.	[ExPASy / RCSB / EBI]
1I5T; NMR; -; A=1-105.	[ExPASy / RCSB / EBI]
1LC1; NMR; -; A=1-105.	[ExPASy / RCSB / EBI]
1LC2; NMR; -; A=1-105.	[ExPASy / RCSB / EBI]
1M60; NMR; -; A=1-105.	[ExPASy / RCSB / EBI]
1OCD; NMR; -; A=1-105.	[ExPASy / RCSB / EBI]
1U75; X-ray; 2.55 A; B=1-105.	[ExPASy / RCSB / EBI]
1WEJ; X-ray; 1.80 A; F=1-105.	[ExPASy / RCSB / EBI]
2FRC; NMR; -; A=1-105.	[ExPASy / RCSB / EBI]
2GIW; NMR; -; A=1-105.	[ExPASy / RCSB / EBI]
2PCB; X-ray; 2.80 A; B=1-105.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1AKK; -.
1CRC; -.
1FI7; -.
1FI9; -.
1GIW; -.
1HRC; -.
1I5T; -.
1LC1; -.
1LC2; -.
1M60; -.
1OCD; -.
1U75; -.
1WEJ; -.
2FRC; -.
2GIW; -.
2PCB; -.

DisProt

DP00006; -.

ModBase

P00004.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from sequence or structural similarity from UniProtKB).
GO:0005759;	Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005746;	Cellular component: mitochondrial respiratory chain (inferred from electronic annotation from UniProtKB-KW).
GO:0045155;	Molecular function: electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity (inferred from sequence or structural similarity from UniProtKB).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0006309;	Biological process: DNA fragmentation during apoptosis (inferred from sequence or structural similarity from UniProtKB).
GO:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR009056; Cyt_c_monohaem.
IPR003088; Cyt_CI.
IPR002327; Cyt_CIAB.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.760.10; Cytochrome_c_R; 1.

PANTHER

PTHR11961; Cyt_CIAB; 1.

Pfam

PF00034; Cytochrom_C; 1.
Pfam graphical view of domain structure.

PRINTS

PR00604; CYTCHRMECIAB.

ProDom

PD000375; Cyt_CIAB; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS51007; CYTC; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P00004.

Phylogenomic databases

HOVERGEN

P00004; -.

Other

LinkHub

P00004; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 105`	`104`	`Cytochrome c.`	`PRO_0000108217`
`METAL`	`19 19`		`Iron (heme axial ligand).`
`METAL`	`81 81`		`Iron (heme axial ligand).`
`BINDING`	`15 15`		`Heme (covalent).`
`BINDING`	`18 18`		`Heme (covalent).`
`MOD_RES`	`2 2`		`N-acetylglycine.`
`HELIX`	`4 14`	`11`
`TURN`	`15 18`	`4`
`HELIX`	`51 55`	`5`
`HELIX`	`62 70`	`9`
`HELIX`	`72 75`	`4`
`HELIX`	`89 102`	`14`

Sequence information

Length: 105 AA [This is the length of the unprocessed precursor]

Molecular weight: 11833 Da [This is the MW of the unprocessed precursor]

CRC64: 659BA128E53C3868 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGDVEKGKKI FVQKCAQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGFTYT DANKNKGITW 

        70         80         90        100 
KEETLMEYLE NPKKYIPGTK MIFAGIKKKT EREDLIAYLK KATNE

P00004 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools