ID AT5G3_RAT Reviewed; 142 AA. AC Q71S46; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 03-AUG-2022, entry version 114. 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:0000312|RGD:620052}; 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:0000312|RGD:620052}; Synonyms=Atp5g3; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=11459924; DOI=10.1152/physiolgenomics.2001.6.2.91; RA Li H.S., Zhang J.Y., Thompson B.S., Deng X.Y., Ford M.E., Wood P.G., RA Stolz D.B., Eagon P.K., Whitcomb D.C.; RT "Rat mitochondrial ATP synthase ATP5G3: cloning and upregulation in RT pancreas after chronic ethanol feeding."; RL Physiol. Genomics 6:91-98(2001). RN [2] RP METHYLATION AT LYS-110. 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-110. 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; AF315374; AAG60677.1; -; mRNA. DR RefSeq; NP_446208.1; NM_053756.1. DR AlphaFoldDB; Q71S46; -. DR SMR; Q71S46; -. DR CORUM; Q71S46; -. DR STRING; 10116.ENSRNOP00000055032; -. DR jPOST; Q71S46; -. DR PaxDb; Q71S46; -. DR PRIDE; Q71S46; -. DR UCSC; RGD:620052; rat. DR RGD; 620052; Atp5mc3. DR eggNOG; KOG3025; Eukaryota. DR InParanoid; Q71S46; -. DR PhylomeDB; Q71S46; -. DR Reactome; R-RNO-1268020; Mitochondrial protein import. DR Reactome; R-RNO-163210; Formation of ATP by chemiosmotic coupling. DR Reactome; R-RNO-8949613; Cristae formation. DR PRO; PR:Q71S46; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0034703; C:cation channel complex; IDA:RGD. DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central. 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; IDA:RGD. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro. DR GO; GO:0007568; P:aging; IEP:RGD. DR GO; GO:0046931; P:pore complex assembly; IDA:RGD. DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central. DR GO; GO:0061959; P:response to (R)-carnitine; IEP:RGD. DR GO; GO:0045471; P:response to ethanol; IEP:RGD. DR GO; GO:0035994; P:response to muscle stretch; IEP:RGD. 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..67 FT /note="Mitochondrion" FT /evidence="ECO:0000250" FT CHAIN 68..142 FT /note="ATP synthase F(0) complex subunit C3, mitochondrial" FT /id="PRO_0000002570" FT TRANSMEM 83..103 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 118..138 FT /note="Helical" FT /evidence="ECO:0000255" FT SITE 125 FT /note="Reversibly protonated during proton transport" FT /evidence="ECO:0000250" FT MOD_RES 110 FT /note="N6,N6,N6-trimethyllysine" FT /evidence="ECO:0000269|PubMed:30530489" SQ SEQUENCE 142 AA; 14693 MW; 19EC0D1710A0AA3F CRC64; MFACAKLACT PSLIRAGSRV AYRPISASVL SRPEASRTGE GSTVFNGAQN GVSQLIQREF QTSAISRDID TAAKFIGAGA ATVGVAGSGA GIGTVFGSLI IGYARNPSLK QQLFSYAILG FALSEAMGLF CLMVAFLILF AM //