Cytochrome c - Equus caballus (Horse)

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Reviewed, UniProtKB/Swiss-Prot P00004 (CYC_HORSE)

Last modified November 25, 2008. Version 81. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein names

Recommended name:
Cytochrome c

Gene names

Name:	CYCS
Synonyms:	CYC

Organism

Equus caballus (Horse)

Taxonomic identifier

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Perissodactyla › Equidae › Equus

Protein attributes

Sequence length	105 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	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.
Post-translational modification	Binds 1 heme group per subunit.
Miscellaneous	Mules and hinnies are heterozygous, having equal amount of horse and donkey cytochromes c.
Sequence similarities	Belongs to the cytochrome c family.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Mitochondrion
Ligand	Heme Iron Metal-binding
PTM	Acetylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA fragmentation during apoptosis Inferred from sequence or structural similarity. Source: UniProtKB electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from sequence or structural similarity. Source: UniProtKB mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity Inferred from sequence or structural similarity. Source: UniProtKB heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

Removed

Chain

104

Cytochrome c

PRO_0000108217

Sites

Metal binding

1

Iron (heme axial ligand)

Metal binding

1

Iron (heme axial ligand)

Binding site

1

Heme (covalent)

Binding site

1

Heme (covalent)

Amino acid modifications

Modified residue

1

N-acetylglycine

Secondary structure

1

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105

Helix Strand Turn

Sequences

Sequence

Length

Mass (Da)

Tools

P00004-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 659BA128E53C3868
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105

11,833

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

        70         80         90        100 
KEETLMEYLE NPKKYIPGTK MIFAGIKKKT EREDLIAYLK KATNE

References

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

Web resources

Protein Spotlight

Life shuttle - Issue 76 of November 2006

Cross-references

Sequence databases

PIR

CCHO. A00005.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AKK	NMR	-	A	1-105	[»]
1CRC	X-ray	2.08	A/B	1-105	[»]
1FI7	NMR	-	A	1-105	[»]
1FI9	NMR	-	A	1-105	[»]
1GIW	NMR	-	A	1-105	[»]
1HRC	X-ray	1.90	A	1-105	[»]
1I5T	NMR	-	A	1-105	[»]
1LC1	NMR	-	A	1-105	[»]
1LC2	NMR	-	A	1-105	[»]
1M60	NMR	-	A	1-105	[»]
1OCD	NMR	-	A	1-105	[»]
1U75	X-ray	2.55	B	1-105	[»]
1WEJ	X-ray	1.80	F	1-105	[»]
2FRC	NMR	-	A	1-105	[»]
2GIW	NMR	-	A	1-105	[»]
2PCB	X-ray	2.80	B	1-105	[»]

DisProt

ModBase

Phylogenomic databases

HOVERGEN

Family and domain databases

InterPro

IPR009056. Cyt_c_monohaem.
IPR003088. Cyt_CI.
IPR002327. Cyt_CIAB.
[Graphical view]

Gene3D

G3DSA:1.10.760.10. Cytochrome_c_R. 1 hit.

PANTHER

PTHR11961. Cyt_CIAB. 1 hit.

Pfam

PF00034. Cytochrom_C. 1 hit.
[Graphical view]

PRINTS

PR00604. CYTCHRMECIAB.

ProDom

PD000375. Cyt_CIAB. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS51007. CYTC. 1 hit.
[Graphical view]

ProtoNet

Other Resources

LinkHub

Entry information

Entry name

CYC_HORSE

Accession

Primary (citable) accession number: P00004

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	November 25, 2008
This is version 81 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents