P62897 (CYC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytochrome c, somatic

Gene names

Name:

Cycs

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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. Ref.7 Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases. Ref.7
Subcellular location	Mitochondrion intermembrane space. Note: Loosely associated with the inner membrane.
Tissue specificity	Found in embryos and in adult liver and heart.
Post-translational modification	Binds 1 heme group per subunit. Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the turnover in the reaction with cytochrome c oxidase, down-regulating mitochondrial respiration By similarity.
Sequence similarities	Belongs to the cytochrome c family.

Ontologies

Keywords
Biological process	Apoptosis Electron transport Respiratory chain Transport
Cellular component	Mitochondrion
Ligand	Heme Iron Metal-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mitochondrial intermembrane space Inferred from electronic annotation. Source: UniProtKB-SubCell respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	electron carrier activity Inferred from electronic annotation. Source: InterPro 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	1	Removed Ref.4
	Chain	2 – 105	104	Cytochrome c, somatic		PRO_0000108225
Sites
	Metal binding	19	1	Iron (heme axial ligand)
	Metal binding	81	1	Iron (heme axial ligand)
	Binding site	15	1	Heme (covalent)
	Binding site	18	1	Heme (covalent)
Amino acid modifications
	Modified residue	2	1	N-acetylglycine Ref.4
	Modified residue	49	1	Phosphotyrosine By similarity
	Modified residue	98	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P62897 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: B5BCA779BCE40492	FASTA	105	11,605
	10 20 30 40 50 60 MGDVEKGKKI FVQKCAQCHT VEKGGKHKTG PNLHGLFGRK TGQAAGFSYT DANKNKGITW 70 80 90 100 GEDTLMEYLE NPKKYIPGTK MIFAGIKKKG ERADLIAYLK KATNE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of a mouse somatic cytochrome c gene and three cytochrome c pseudogenes." Limbach K.J., Wu R. Nucleic Acids Res. 13:617-630(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: BALB/c.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: NOD. Tissue: Thymus.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Czech II.
[4]	"Primary structure of mouse, rat, and guinea pig cytochrome c." Carlson S.S., Mross G.A., Wilson A.C., Mead R.T., Wolin L.D., Bowers S.F., Foley N.T., Muijsers A.O., Margoliash E. Biochemistry 16:1437-1442(1977) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2. Strain: BALB/c.
[5]	Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 29-54; 57-74; 81-88 AND 93-100, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[6]	"Change of cytochrome c structure during development of the mouse." Hennig B. Eur. J. Biochem. 55:167-183(1975) [PubMed] [Europe PMC] [Abstract] Cited for: AMINO-ACID COMPOSITION OF TRYPTIC PEPTIDES. Strain: BALB/c.
[7]	"Nuclear Apaf-1 and cytochrome c redistribution following stress-induced apoptosis." Ruiz-Vela A., Gonzalez de Buitrago G., Martinez-A C. FEBS Lett. 517:133-138(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN APOPTOSIS.

Web resources

Protein Spotlight

Life shuttle - Issue 76 of November 2006

Cross-references

Sequence databases
EMBL GenBank DDBJ	X01756 Genomic DNA. Translation: CAA25899.1. AK088098 mRNA. Translation: BAC40143.1. BC034363 mRNA. Translation: AAH34363.1.
IPI	IPI00222419.
PIR	CCMS. A23057.
RefSeq	NP_031834.1. NM_007808.4.
UniGene	Mm.35389.
3D structure databases
ProteinModelPortal	P62897.
SMR	P62897. Positions 2-105.
ModBase	Search...
Protein-protein interaction databases
IntAct	P62897. 2 interactions.
STRING	10090.ENSMUSP00000076944.
PTM databases
PhosphoSite	P62897.
Proteomic databases
PaxDb	P62897.
PRIDE	P62897.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000073080; ENSMUSP00000072829; ENSMUSG00000058927. ENSMUST00000161401; ENSMUSP00000124523; ENSMUSG00000063694.
GeneID	13063.
KEGG	mmu:13063.
Organism-specific databases
CTD	54205.
MGI	MGI:88578. Cycs.
Phylogenomic databases
eggNOG	COG3474.
HOGENOM	HOG000009762.
HOVERGEN	HBG003023.
InParanoid	P62897.
KO	K08738.
OMA	IAYLKQY.
OrthoDB	EOG45DWQX.
Gene expression databases
ArrayExpress	P62897.
Bgee	P62897.
CleanEx	MM_CYCS.
Genevestigator	P62897.
GermOnline	ENSMUSG00000058927. Mus musculus. ENSMUSG00000063694. Mus musculus.
Family and domain databases
InterPro	IPR002327. Cyt_c_1A/1B. IPR009056. Cyt_c_dom. IPR003088. Cyt_c_I. [Graphical view]
PANTHER	PTHR11961. PTHR11961. 1 hit.
Pfam	PF00034. Cytochrom_C. 1 hit. [Graphical view]
PRINTS	PR00604. CYTCHRMECIAB.
SUPFAM	SSF46626. Cytochrome_c. 1 hit.
PROSITE	PS51007. CYTC. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	282990.
SOURCE	Search...

Entry information

Entry name

CYC_MOUSE

Accession

Primary (citable) accession number: P62897
Secondary accession number(s): P00009, Q8C2S2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program