AT5G3_MOUSE
ID AT5G3_MOUSE Reviewed; 141 AA.
AC P56384;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=ATP synthase F(0) complex subunit C3, mitochondrial {ECO:0000305};
DE AltName: Full=ATP synthase lipid-binding protein;
DE AltName: Full=ATP synthase membrane subunit c locus 3 {ECO:0000250|UniProtKB:P48201};
DE AltName: Full=ATP synthase proteolipid P3;
DE AltName: Full=ATPase protein 9;
DE AltName: Full=ATPase subunit c;
DE Flags: Precursor;
GN Name=Atp5mc3 {ECO:0000250|UniProtKB:P48201}; Synonyms=Atp5g3;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Testis, and Thymus;
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 [2]
RP METHYLATION AT LYS-109.
RX PubMed=30530489; DOI=10.1074/jbc.ra118.005473;
RA Malecki J.M., Willemen H.L.D.M., Pinto R., Ho A.Y.Y., Moen A.,
RA Kjoenstad I.F., Burgering B.M.T., Zwartkruis F., Eijkelkamp N.,
RA Falnes P.O.;
RT "Lysine methylation by the mitochondrial methyltransferase FAM173B
RT optimizes the function of mitochondrial ATP synthase.";
RL J. Biol. Chem. 294:1128-1141(2019).
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 F(0)
CC - containing the membrane proton channel, linked together by a central
CC stalk and a peripheral stalk. During catalysis, ATP synthesis in the
CC catalytic domain of F(1) is coupled via a rotary mechanism of the
CC central stalk subunits to proton translocation. Part of the complex
CC F(0) domain. A homomeric c-ring of probably 10 subunits is part of the
CC complex rotary element.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a, b and c. Interacts with TMEM70 and TMEM242 (By
CC similarity). {ECO:0000250|UniProtKB:P48201}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- PTM: Trimethylated by ATPSCKMT at Lys-109. Methylation is required for
CC proper incorporation of the C subunit into the ATP synthase complex and
CC mitochondrial respiration. {ECO:0000269|PubMed:30530489}.
CC -!- DISEASE: Note=This protein is the major protein stored in the storage
CC bodies of animals or humans affected with ceroid lipofuscinosis (Batten
CC disease).
CC -!- MISCELLANEOUS: There are three genes which encode the mitochondrial ATP
CC synthase proteolipid and they specify precursors with different import
CC sequences but identical mature proteins. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK077930; BAC37071.1; -; mRNA.
DR EMBL; AK087955; BAC40056.1; -; mRNA.
DR CCDS; CCDS16136.1; -.
DR RefSeq; NP_001288650.1; NM_001301721.1.
DR RefSeq; NP_778180.1; NM_175015.3.
DR AlphaFoldDB; P56384; -.
DR SMR; P56384; -.
DR STRING; 10090.ENSMUSP00000018914; -.
DR PhosphoSitePlus; P56384; -.
DR jPOST; P56384; -.
DR PaxDb; P56384; -.
DR PRIDE; P56384; -.
DR ProteomicsDB; 277126; -.
DR Antibodypedia; 53295; 47 antibodies from 17 providers.
DR DNASU; 228033; -.
DR Ensembl; ENSMUST00000018914; ENSMUSP00000018914; ENSMUSG00000018770.
DR Ensembl; ENSMUST00000111996; ENSMUSP00000107627; ENSMUSG00000018770.
DR GeneID; 228033; -.
DR KEGG; mmu:228033; -.
DR UCSC; uc008kdm.2; mouse.
DR CTD; 228033; -.
DR MGI; MGI:2442035; Atp5g3.
DR VEuPathDB; HostDB:ENSMUSG00000018770; -.
DR eggNOG; KOG3025; Eukaryota.
DR GeneTree; ENSGT00940000154298; -.
DR HOGENOM; CLU_116822_1_0_1; -.
DR InParanoid; P56384; -.
DR OMA; CKMFACA; -.
DR OrthoDB; 1564365at2759; -.
DR PhylomeDB; P56384; -.
DR TreeFam; TF300140; -.
DR Reactome; R-MMU-1268020; Mitochondrial protein import.
DR Reactome; R-MMU-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-MMU-8949613; Cristae formation.
DR BioGRID-ORCS; 228033; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Atp5g3; mouse.
DR PRO; PR:P56384; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P56384; protein.
DR Bgee; ENSMUSG00000018770; Expressed in myocardium of ventricle and 252 other tissues.
DR ExpressionAtlas; P56384; baseline and differential.
DR Genevisible; P56384; MM.
DR GO; GO:0034703; C:cation channel complex; ISO:MGI.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
DR GO; GO:0022834; F:ligand-gated channel activity; ISO:MGI.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046931; P:pore complex assembly; ISO:MGI.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR Gene3D; 1.20.20.10; -; 1.
DR HAMAP; MF_01396; ATP_synth_c_bact; 1.
DR InterPro; IPR000454; ATP_synth_F0_csu.
DR InterPro; IPR020537; ATP_synth_F0_csu_DDCD_BS.
DR InterPro; IPR038662; ATP_synth_F0_csu_sf.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR PANTHER; PTHR10031; PTHR10031; 1.
DR Pfam; PF00137; ATP-synt_C; 1.
DR PRINTS; PR00124; ATPASEC.
DR SUPFAM; SSF81333; SSF81333; 1.
DR PROSITE; PS00605; ATPASE_C; 1.
PE 1: Evidence at protein level;
KW CF(0); Hydrogen ion transport; Ion transport; Lipid-binding; Membrane;
KW Methylation; Mitochondrion; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..66
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 67..141
FT /note="ATP synthase F(0) complex subunit C3, mitochondrial"
FT /id="PRO_0000002568"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 124
FT /note="Reversibly protonated during proton transport"
FT /evidence="ECO:0000250"
FT MOD_RES 109
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:30530489"
SQ SEQUENCE 141 AA; 14745 MW; 2B549F5AE7874554 CRC64;
MFACAKLART PALIRAGSRV AYRPISASVL SRPETRTGEG STVFNGAQNG VCQLIRREFQ
TSVISRDIDT AAKFIGAGAA TVGVAGSGAG IGTVFGSLII GYARNPSLKQ QLFSYAILGF
ALSEAMGLFC LMVAFLILFA M
