ID   CYC2_MOUSE              Reviewed;         105 AA.
AC   P00015;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 186.
DE   RecName: Full=Cytochrome c, testis-specific;
GN   Name=Cyct;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2834389; DOI=10.1016/s0021-9258(18)68712-5;
RA   Virbasius J.V., Scarpulla R.C.;
RT   "Structure and expression of rodent genes encoding the testis-specific
RT   cytochrome c. Differences in gene structure and evolution between somatic
RT   and testicular variants.";
RL   J. Biol. Chem. 263:6791-6796(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, CLEAVAGE OF INITIATOR METHIONINE,
RP   AND ACETYLATION AT GLY-2.
RC   STRAIN=BALB/cJ;
RX   PubMed=240690; DOI=10.1111/j.1432-1033.1975.tb02149.x;
RA   Hennig B.;
RT   "Change of cytochrome c structure during development of the mouse.";
RL   Eur. J. Biochem. 55:167-183(1975).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the cytochrome
CC       c heme group can accept an electron from the heme group of the
CC       cytochrome c1 subunit of cytochrome reductase. Cytochrome c then
CC       transfers this electron to the cytochrome oxidase complex, the final
CC       protein carrier in the mitochondrial electron-transport chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic
CC       members or activation of the pro-apoptotic members of the Bcl-2 family
CC       leads to altered mitochondrial membrane permeability resulting in
CC       release of cytochrome c into the cytosol. Binding of cytochrome c to
CC       Apaf-1 triggers the activation of caspase-9, which then accelerates
CC       apoptosis by activating other caspases (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely
CC       associated with the inner membrane.
CC   -!- TISSUE SPECIFICITY: This is one of two isocytochromes C found in the
CC       testis. The other is identical with the form found in other mouse
CC       tissues. These cytochromes are assumed to be located in the sperm.
CC   -!- PTM: Binds 1 heme c group covalently per subunit.
CC   -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC       turnover in the reaction with cytochrome c oxidase, down-regulating
CC       mitochondrial respiration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of
CC       November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
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DR   EMBL; M20625; AAA37501.1; -; mRNA.
DR   EMBL; X55771; CAA39293.1; -; mRNA.
DR   EMBL; AK005582; BAB24136.1; -; mRNA.
DR   EMBL; AK018833; BAB31455.1; -; mRNA.
DR   EMBL; AK018851; BAB31464.1; -; mRNA.
DR   CCDS; CCDS16156.1; -.
DR   PIR; B28160; CCMST.
DR   RefSeq; NP_034119.1; NM_009989.3.
DR   RefSeq; XP_011237575.1; XM_011239273.1.
DR   PDB; 2AIU; X-ray; 1.60 A; A=1-105.
DR   PDBsum; 2AIU; -.
DR   AlphaFoldDB; P00015; -.
DR   SMR; P00015; -.
DR   BioGRID; 198996; 2.
DR   STRING; 10090.ENSMUSP00000028430; -.
DR   iPTMnet; P00015; -.
DR   PhosphoSitePlus; P00015; -.
DR   SwissPalm; P00015; -.
DR   jPOST; P00015; -.
DR   MaxQB; P00015; -.
DR   PaxDb; 10090-ENSMUSP00000028430; -.
DR   PeptideAtlas; P00015; -.
DR   ProteomicsDB; 279229; -.
DR   DNASU; 13067; -.
DR   Ensembl; ENSMUST00000028430.6; ENSMUSP00000028430.5; ENSMUSG00000056436.5.
DR   GeneID; 13067; -.
DR   KEGG; mmu:13067; -.
DR   UCSC; uc008key.2; mouse.
DR   AGR; MGI:88579; -.
DR   CTD; 13067; -.
DR   MGI; MGI:88579; Cyct.
DR   VEuPathDB; HostDB:ENSMUSG00000056436; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   GeneTree; ENSGT00940000157883; -.
DR   HOGENOM; CLU_060944_3_0_1; -.
DR   InParanoid; P00015; -.
DR   OMA; NKGVIWG; -.
DR   OrthoDB; 4150at2759; -.
DR   PhylomeDB; P00015; -.
DR   TreeFam; TF300226; -.
DR   BioGRID-ORCS; 13067; 2 hits in 77 CRISPR screens.
DR   ChiTaRS; Cyct; mouse.
DR   EvolutionaryTrace; P00015; -.
DR   PRO; PR:P00015; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; P00015; Protein.
DR   Bgee; ENSMUSG00000056436; Expressed in spermatocyte and 71 other cell types or tissues.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0042743; P:hydrogen peroxide metabolic process; IDA:MGI.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IDA:MGI.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; CYTOCHROME C; 1.
DR   PANTHER; PTHR11961:SF6; CYTOCHROME C, TESTIS-SPECIFIC; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   PROSITE; PS51007; CYTC; 1.
DR   Genevisible; P00015; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Apoptosis; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:240690"
FT   CHAIN           2..105
FT                   /note="Cytochrome c, testis-specific"
FT                   /id="PRO_0000108226"
FT   BINDING         15
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT                   ECO:0000269|PubMed:240690"
FT   BINDING         18
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT                   ECO:0000269|PubMed:240690"
FT   BINDING         19
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   BINDING         81
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:240690"
FT   HELIX           4..14
FT                   /evidence="ECO:0007829|PDB:2AIU"
FT   TURN            15..18
FT                   /evidence="ECO:0007829|PDB:2AIU"
FT   STRAND          39..42
FT                   /evidence="ECO:0007829|PDB:2AIU"
FT   HELIX           51..55
FT                   /evidence="ECO:0007829|PDB:2AIU"
FT   HELIX           62..70
FT                   /evidence="ECO:0007829|PDB:2AIU"
FT   HELIX           72..75
FT                   /evidence="ECO:0007829|PDB:2AIU"
FT   HELIX           89..104
FT                   /evidence="ECO:0007829|PDB:2AIU"
SQ   SEQUENCE   105 AA;  11714 MW;  00C275FC70B5AAF9 CRC64;
     MGDAEAGKKI FVQKCAQCHT VEKGGKHKTG PNLWGLFGRK TGQAPGFSYT DANKNKGVIW
     SEETLMEYLE NPKKYIPGTK MIFAGIKKKS EREDLIKYLK QATSS
//