Reviewed, UniProtKB/Swiss-Prot P00015 (CYC2_MOUSE)

Names and origin

Protein names

Recommended name:
    Cytochrome c, testis-specific

Gene names

Name:

Cyct

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › 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.
Subcellular location	Mitochondrion matrix.
Tissue specificity	This is one of two isocytochromes C found in the testis. The other is identical with the form found in other mouse tissues. These cytochromes are assumed to be located in the sperm.
Post-translational modification	Binds 1 heme group per subunit.
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	apoptosis Inferred from direct assay. Source: MGI hydrogen peroxide metabolic process Inferred from direct assay. Source: MGI
Molecular function	heme binding Inferred from direct assay. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 105

104

Cytochrome c, testis-specific

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

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

105

Helix Strand Turn

Details...

Helix

4 – 14

11

Turn

15 – 18

4

Beta strand

39 – 42

4

Helix

51 – 55

5

Helix

62 – 70

9

Helix

72 – 75

4

Helix

89 – 104

16

Sequences

	Sequence		Length	Mass (Da)
	P00015-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 00C275FC70B5AAF9	FASTA	105	11,714
	10 20 30 40 50 60 MGDAEAGKKI FVQKCAQCHT VEKGGKHKTG PNLWGLFGRK TGQAPGFSYT DANKNKGVIW 70 80 90 100 SEETLMEYLE NPKKYIPGTK MIFAGIKKKS EREDLIKYLK QATSS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and expression of rodent genes encoding the testis-specific cytochrome c. Differences in gene structure and evolution between somatic and testicular variants." Virbasius J.V., Scarpulla R.C. J. Biol. Chem. 263:6791-6796(1988) [PubMed: 2834389] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Testis.
[3]	"Change of cytochrome c structure during development of the mouse." Hennig B. Eur. J. Biochem. 55:167-183(1975) [PubMed: 240690] [Abstract] Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-105. Strain: BALB/c.
+	Additional computationally mapped references.

Web resources

Protein Spotlight

Life shuttle - Issue 76 of November 2006

Cross-references

Sequence databases

EMBLGenBankDDBJ

M20625 mRNA. Translation: AAA37501.1.
X55771 mRNA. Translation: CAA39293.1.
AK005582 mRNA. Translation: BAB24136.1.
AK018833 mRNA. Translation: BAB31455.1.
AK018851 mRNA. Translation: BAB31464.1.

PIR

CCMST. B28160.

RefSeq

NP_034119.1.

UniGene

Mm.4872

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AIU	X-ray	1.60	A	1-105	[»]

ModBase

Search...

Genome annotation databases

Ensembl

ENSMUSG00000056436. Mus musculus. [Contig view]

GeneID

13067.

KEGG

mmu:13067.

NMPDR

fig|10090.3.peg.6178.

Organism-specific databases

MGI

MGI:88579. Cyct.

Phylogenomic databases

HOGENOM

P00015.

HOVERGEN

P00015.

Gene expression databases

ArrayExpress

P00015.

CleanEx

MM_CYCT.

GermOnline

ENSMUSG00000056436. Mus musculus.

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]

BLOCKS

Search...

Other Resources

SOURCE

Search...

ProtoNet

Search...

Entry information

Entry name

CYC2_MOUSE

Accession

Primary (citable) accession number: P00015

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	July 22, 2008
This is version 83 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)