ATP5L_MOUSE
ID ATP5L_MOUSE Reviewed; 103 AA.
AC Q9CPQ8; O70590; Q5M9M8;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=ATP synthase subunit g, mitochondrial {ECO:0000305};
DE Short=ATPase subunit g;
DE AltName: Full=ATP synthase membrane subunit g {ECO:0000305};
GN Name=Atp5mg {ECO:0000250|UniProtKB:O75964}; Synonyms=Atp5l;
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].
RC STRAIN=ICR; TISSUE=Mammary gland;
RX PubMed=10361692; DOI=10.1271/bbb.63.767;
RA Baik M., Jeon D., Kim H.;
RT "Sequence of a cDNA encoding mouse F1F0-ATP synthase g subunit.";
RL Biosci. Biotechnol. Biochem. 63:767-768(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Cerebellum, Hippocampus, Liver, Small intestine, and Tongue;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 12-54, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-11; LYS-35 AND LYS-54, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
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 -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(0) seems to have nine
CC subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). Component of an ATP
CC synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME,
CC ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C,
CC ATP5PO, ATP5MG, ATP5MK and ATP5MJ (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC -!- SIMILARITY: Belongs to the ATPase g subunit family. {ECO:0000305}.
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DR EMBL; Y17223; CAA76699.1; -; mRNA.
DR EMBL; AK005175; BAB23862.1; -; mRNA.
DR EMBL; AK005321; BAB23952.1; -; mRNA.
DR EMBL; AK005380; BAB23987.1; -; mRNA.
DR EMBL; AK008002; BAB25401.1; -; mRNA.
DR EMBL; AK008012; BAB25408.1; -; mRNA.
DR EMBL; AK008030; BAB25420.1; -; mRNA.
DR EMBL; AK008087; BAB25451.1; -; mRNA.
DR EMBL; AK008183; BAB25516.1; -; mRNA.
DR EMBL; AK008251; BAB25558.1; -; mRNA.
DR EMBL; AK008321; BAB25600.1; -; mRNA.
DR EMBL; AK009465; BAB26305.1; -; mRNA.
DR EMBL; AK009468; BAB26308.1; -; mRNA.
DR EMBL; AK009471; BAB26310.1; -; mRNA.
DR EMBL; AK009612; BAB26392.1; -; mRNA.
DR EMBL; AK009806; BAB26514.1; -; mRNA.
DR EMBL; AK011038; BAB27351.1; -; mRNA.
DR EMBL; AK011046; BAB27357.1; -; mRNA.
DR EMBL; AK011099; BAB27396.1; -; mRNA.
DR EMBL; AK019252; BAB31628.1; -; mRNA.
DR EMBL; AK019274; BAB31641.1; -; mRNA.
DR EMBL; AK019320; BAB31664.1; -; mRNA.
DR EMBL; AK019343; BAB31670.1; -; mRNA.
DR EMBL; AK019350; BAB31672.1; -; mRNA.
DR EMBL; AK019355; BAB31676.1; -; mRNA.
DR EMBL; BC031384; AAH31384.1; -; mRNA.
DR EMBL; BC086880; AAH86880.1; -; mRNA.
DR EMBL; BC089555; AAH89555.1; -; mRNA.
DR EMBL; BC094407; AAH94407.1; -; mRNA.
DR CCDS; CCDS40604.1; -.
DR RefSeq; NP_038823.2; NM_013795.5.
DR AlphaFoldDB; Q9CPQ8; -.
DR SMR; Q9CPQ8; -.
DR BioGRID; 205227; 67.
DR IntAct; Q9CPQ8; 3.
DR MINT; Q9CPQ8; -.
DR STRING; 10090.ENSMUSP00000047960; -.
DR iPTMnet; Q9CPQ8; -.
DR PhosphoSitePlus; Q9CPQ8; -.
DR EPD; Q9CPQ8; -.
DR jPOST; Q9CPQ8; -.
DR MaxQB; Q9CPQ8; -.
DR PaxDb; Q9CPQ8; -.
DR PeptideAtlas; Q9CPQ8; -.
DR PRIDE; Q9CPQ8; -.
DR ProteomicsDB; 277090; -.
DR TopDownProteomics; Q9CPQ8; -.
DR DNASU; 27425; -.
DR Ensembl; ENSMUST00000043675; ENSMUSP00000047960; ENSMUSG00000038717.
DR GeneID; 27425; -.
DR KEGG; mmu:27425; -.
DR UCSC; uc009per.2; mouse.
DR CTD; 27425; -.
DR MGI; MGI:1351597; Atp5l.
DR VEuPathDB; HostDB:ENSMUSG00000038717; -.
DR eggNOG; KOG4103; Eukaryota.
DR GeneTree; ENSGT00390000009724; -.
DR HOGENOM; CLU_152793_1_1_1; -.
DR InParanoid; Q9CPQ8; -.
DR OMA; ATEVCMW; -.
DR OrthoDB; 1461139at2759; -.
DR PhylomeDB; Q9CPQ8; -.
DR TreeFam; TF313978; -.
DR Reactome; R-MMU-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-MMU-8949613; Cristae formation.
DR BioGRID-ORCS; 27425; 14 hits in 73 CRISPR screens.
DR ChiTaRS; Atp5l; mouse.
DR PRO; PR:Q9CPQ8; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9CPQ8; protein.
DR Bgee; ENSMUSG00000038717; Expressed in quadriceps femoris and 86 other tissues.
DR Genevisible; Q9CPQ8; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; ISS:UniProtKB.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0008553; F:P-type proton-exporting transporter activity; ISO:MGI.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; ISO:MGI.
DR GO; GO:0046034; P:ATP metabolic process; ISO:MGI.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; ISO:MGI.
DR InterPro; IPR006808; ATP_synth_F0_gsu_mt.
DR InterPro; IPR016702; ATP_synth_su_G_mt_met.
DR PANTHER; PTHR12386; PTHR12386; 1.
DR Pfam; PF04718; ATP-synt_G; 1.
DR PIRSF; PIRSF017835; ATP-synth_g_mitoch_animal; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP synthesis; CF(0); Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O75964"
FT CHAIN 2..103
FT /note="ATP synthase subunit g, mitochondrial"
FT /id="PRO_0000071692"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O75964"
FT MOD_RES 11
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 24
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O75964"
FT MOD_RES 35
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 54
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT CONFLICT 56
FT /note="I -> M (in Ref. 1; CAA76699)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 103 AA; 11425 MW; 66BB25CECD67AA33 CRC64;
MAKFIRNFAE KAPSMVAAAV TYSKPRLATF WHYAKVELVP PTPAEIPTAI QSVKKIIQSA
KTGSFKHLTV KEAVLNGLVA TEVWMWFYIG EIIGKRGIVG YDV
