CYC2_MOUSE
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 03-AUG-2022, entry version 178.
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; 1.
DR STRING; 10090.ENSMUSP00000028430; -.
DR iPTMnet; P00015; -.
DR PhosphoSitePlus; P00015; -.
DR jPOST; P00015; -.
DR MaxQB; P00015; -.
DR PaxDb; P00015; -.
DR PeptideAtlas; P00015; -.
DR PRIDE; P00015; -.
DR ProteomicsDB; 279229; -.
DR DNASU; 13067; -.
DR Ensembl; ENSMUST00000028430; ENSMUSP00000028430; ENSMUSG00000056436.
DR GeneID; 13067; -.
DR KEGG; mmu:13067; -.
DR UCSC; uc008key.2; mouse.
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; WSENTLM; -.
DR OrthoDB; 1533604at2759; -.
DR PhylomeDB; P00015; -.
DR TreeFam; TF300226; -.
DR BioGRID-ORCS; 13067; 2 hits in 72 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 69 other tissues.
DR Genevisible; P00015; MM.
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:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IDA:MGI.
DR Gene3D; 1.10.760.10; -; 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; PTHR11961; 1.
DR Pfam; PF00034; Cytochrom_C; 1.
DR PRINTS; PR00604; CYTCHRMECIAB.
DR SUPFAM; SSF46626; SSF46626; 1.
DR PROSITE; PS51007; CYTC; 1.
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
