ID   Q8BTB6_MOUSE            Unreviewed;        38 AA.
AC   Q8BTB6;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 124.
DE   RecName: Full=ATP synthase subunit e, mitochondrial {ECO:0000256|ARBA:ARBA00021462, ECO:0000256|RuleBase:RU367005};
GN   Name=Atp5me {ECO:0000313|Ensembl:ENSMUSP00000113882.2,
GN   ECO:0000313|MGI:MGI:106636};
GN   Synonyms=Atp5k {ECO:0000313|MGI:MGI:106636};
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 {ECO:0000313|EMBL:BAC25330.1};
RN   [1] {ECO:0000313|EMBL:BAC25330.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC25330.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:BAC25330.1};
RX   PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2] {ECO:0000313|EMBL:BAC25330.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC25330.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:BAC25330.1};
RX   PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to prepare
RT   full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [3] {ECO:0000313|EMBL:BAC25330.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC25330.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:BAC25330.1};
RX   PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N.,
RA   Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R.,
RA   Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S.,
RA   Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y.,
RA   Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y.,
RA   Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format sequencing
RT   pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [4] {ECO:0000313|EMBL:BAC25330.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC25330.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:BAC25330.1};
RA   Adachi J., Aizawa K., Akahira S., Akimura T., Arai A., Aono H., Arakawa T.,
RA   Bono H., Carninci P., Fukuda S., Fukunishi Y., Furuno M., Hanagaki T.,
RA   Hara A., Hayatsu N., Hiramoto K., Hiraoka T., Hori F., Imotani K.,
RA   Ishii Y., Itoh M., Izawa M., Kasukawa T., Kato H., Kawai J., Kojima Y.,
RA   Konno H., Kouda M., Koya S., Kurihara C., Matsuyama T., Miyazaki A.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Okazaki Y., Okido T., Owa C.,
RA   Saito H., Saito R., Sakai C., Sakai K., Sano H., Sasaki D., Shibata K.,
RA   Shibata Y., Shinagawa A., Shiraki T., Sogabe Y., Suzuki H., Tagami M.,
RA   Tagawa A., Takahashi F., Tanaka T., Tejima Y., Toya T., Yamamura T.,
RA   Yasunishi A., Yoshida K., Yoshino M., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:BAC25330.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC25330.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:BAC25330.1};
RX   PubMed=11217851; DOI=10.1038/35055500;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6] {ECO:0000313|EMBL:BAC25330.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC25330.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:BAC25330.1};
RX   PubMed=12466851; DOI=10.1038/nature01266;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [7] {ECO:0000313|EMBL:BAC25330.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC25330.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:BAC25330.1};
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [8] {ECO:0000313|EMBL:BAC25330.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC25330.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:BAC25330.1};
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [9] {ECO:0000313|Ensembl:ENSMUSP00000113882.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000113882.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [10] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
RN   [11] {ECO:0000313|Ensembl:ENSMUSP00000113882.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000113882.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC       Complex V) produces ATP from ADP in the presence of a proton gradient
CC       across the membrane which is generated by electron transport complexes
CC       of the respiratory chain. F-type ATPases consist of two structural
CC       domains, F(1) - containing the extramembraneous catalytic core, and
CC       F(0) - containing the membrane proton channel, linked together by a
CC       central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC       in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC       the central stalk subunits to proton translocation. Part of the complex
CC       F(0) domain. Minor subunit located with subunit a in the membrane.
CC       {ECO:0000256|ARBA:ARBA00003606, ECO:0000256|RuleBase:RU367005}.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC       - and CF(0) - the membrane proton channel.
CC       {ECO:0000256|RuleBase:RU367005}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|RuleBase:RU367005}.
CC   -!- SIMILARITY: Belongs to the ATPase e subunit family.
CC       {ECO:0000256|ARBA:ARBA00007333, ECO:0000256|RuleBase:RU367005}.
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DR   EMBL; AK011342; BAC25330.1; -; mRNA.
DR   ProteomicsDB; 308692; -.
DR   Antibodypedia; 22135; 213 antibodies from 28 providers.
DR   Ensembl; ENSMUST00000118632.2; ENSMUSP00000113882.2; ENSMUSG00000050856.17.
DR   AGR; MGI:106636; -.
DR   MGI; MGI:106636; Atp5me.
DR   VEuPathDB; HostDB:ENSMUSG00000050856; -.
DR   GeneTree; ENSGT00390000005102; -.
DR   HOGENOM; CLU_3335403_0_0_1; -.
DR   ChiTaRS; Atp5k; mouse.
DR   Proteomes; UP000000589; Chromosome 5.
DR   Bgee; ENSMUSG00000050856; Expressed in facial nucleus and 249 other cell types or tissues.
DR   GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-UniRule.
DR   GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro.
DR   InterPro; IPR008386; ATP_synth_F0_esu_mt.
DR   PANTHER; PTHR12427; ATP SYNTHASE E CHAIN, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR12427:SF1; ATP SYNTHASE SUBUNIT E, MITOCHONDRIAL; 1.
DR   Pfam; PF05680; ATP-synt_E; 1.
PE   1: Evidence at protein level;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   ATP synthesis {ECO:0000256|ARBA:ARBA00023310,
KW   ECO:0000256|RuleBase:RU367005};
KW   CF(0) {ECO:0000256|ARBA:ARBA00022547, ECO:0000256|RuleBase:RU367005};
KW   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW   ECO:0000256|RuleBase:RU367005};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU367005}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW   ECO:0000256|RuleBase:RU367005};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792,
KW   ECO:0000256|RuleBase:RU367005};
KW   Proteomics identification {ECO:0007829|EPD:Q8BTB6,
KW   ECO:0007829|MaxQB:Q8BTB6};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367005}.
SQ   SEQUENCE   38 AA;  4228 MW;  59FD4BD187F39797 CRC64;
     MVPPVQVSPL IKFGRYSALI IGMAYGAKRY TQDDSILK
//