P00015 (CYC2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

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 › 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. 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 By similarity.
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. 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	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	apoptotic process Inferred from direct assay. Source: MGI electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW hydrogen peroxide metabolic process Inferred from direct assay. Source: MGI transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix 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 direct assay. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.3

Chain

2 – 105

104

Cytochrome c, testis-specific

PRO_0000108226

Sites

Metal binding

19

1

Iron (heme axial ligand)

Metal binding

81

1

Iron (heme axial ligand)

Binding site

15

1

Heme (covalent) Ref.3

Binding site

18

1

Heme (covalent) Ref.3

Amino acid modifications

Modified residue

2

1

N-acetylglycine Ref.3

Modified residue

49

1

Phosphotyrosine By similarity

Modified residue

98

1

Phosphotyrosine By similarity

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 [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

EMBL
GenBank
DDBJ

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.

IPI

IPI00230033.

PIR

CCMST. B28160.

RefSeq

NP_034119.1. NM_009989.2.

UniGene

Mm.4872.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AIU	X-ray	1.60	A	2-104	[»]

ProteinModelPortal

P00015.

SMR

P00015. Positions 2-105.

ModBase

Search...

Protein-protein interaction databases

STRING

P00015.

PTM databases

PhosphoSite

P00015.

Proteomic databases

PRIDE

P00015.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000028430; ENSMUSP00000028430; ENSMUSG00000056436.

GeneID

13067.

KEGG

mmu:13067.

NMPDR

fig|10090.3.peg.6178.

Organism-specific databases

CTD

13067.

MGI

MGI:88579. Cyct.

Phylogenomic databases

HOGENOM

HBG692582.

HOVERGEN

HBG003023.

InParanoid

P00015.

OMA

IFIQKCA.

OrthoDB

EOG45DWQX.

PhylomeDB

P00015.

Gene expression databases

ArrayExpress

P00015.

Bgee

P00015.

CleanEx

MM_CYCT.

Genevestigator

P00015.

GermOnline

ENSMUSG00000056436. Mus musculus.

Family and domain databases

InterPro

IPR002327. Cyt_c_1A/1B.
IPR009056. Cyt_c_dom.
IPR003088. Cyt_c_I.
[Graphical view]

Gene3D

G3DSA:1.10.760.10. Cytochrome_c_R. 1 hit.

KO

K08738.

PANTHER

PTHR11961. Cyt_CIAB. 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

283000.

SOURCE

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:	November 16, 2011
This is version 112 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program