PROTEIN SEQUENCE OF 2-105.
DOI=10.1021/bi00525a030; PubMed=6272840 [NCBI, ExPASy, EBI, Israel, Japan]
Shelnutt J.A., Rousseau D.L., Dethmers J.K., Margoliash E.;
"Protein influences on porphyrin structure in cytochrome c: evidence from Raman difference spectroscopy.";
Biochemistry 20:6485-6497(1981).

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.
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

A00004; CCMKP.

3D structure databases

HSSP

P00004; 2PCB. [HSSP ENTRY / PDB]

SMR

P00003; 2-105.

ModBase

P00003.

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

P00003.

Phylogenomic databases

HOVERGEN

P00003; -.

Other

UniRef

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

Keywords

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_0000108208`
`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 (Probable).`

Sequence information

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

Molecular weight: 11841 Da [This is the MW of the unprocessed precursor]

CRC64: F552A2FC63C0CEBE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGDVFKGKRI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQASGFTYT EANKNKGIIW 

        70         80         90        100 
GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE

P00003 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