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 22-NOV-2017, entry version 93. DE RecName: Full=ATP synthase F(0) complex subunit C3, mitochondrial; DE AltName: Full=ATP synthase lipid-binding protein; DE AltName: Full=ATP synthase proteolipid P3; DE AltName: Full=ATPase protein 9; DE AltName: Full=ATPase subunit c; DE Flags: Precursor; GN Name=Atp5g3; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=11459924; 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). CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP CC synthase or Complex V) produces ATP from ADP in the presence of a CC proton gradient across the membrane which is generated by electron CC transport complexes of the respiratory chain. F-type ATPases CC consist of two structural domains, F(1) - containing the CC extramembraneous catalytic core and F(0) - containing the membrane CC proton channel, linked together by a central stalk and a CC peripheral stalk. During catalysis, ATP synthesis in the catalytic CC domain of F(1) is coupled via a rotary mechanism of the central CC stalk subunits to proton translocation. Part of the complex F(0) CC 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 CC core - and CF(0) - the membrane proton channel. CF(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) CC has three main subunits: a, b and c. CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- DISEASE: Note=This protein is the major protein stored in the CC storage bodies of animals or humans affected with ceroid CC lipofuscinosis (Batten disease). CC -!- MISCELLANEOUS: There are three genes which encode the CC mitochondrial ATP synthase proteolipid and they specify precursors CC with different import sequences but identical mature proteins. CC {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 UniGene; Rn.2180; -. DR ProteinModelPortal; Q71S46; -. DR SMR; Q71S46; -. DR CORUM; Q71S46; -. DR STRING; 10116.ENSRNOP00000055032; -. DR PaxDb; Q71S46; -. DR PRIDE; Q71S46; -. DR GeneID; 114630; -. DR KEGG; rno:114630; -. DR UCSC; RGD:620052; rat. DR CTD; 518; -. DR RGD; 620052; Atp5g3. DR eggNOG; KOG3025; Eukaryota. DR eggNOG; COG0636; LUCA. DR HOGENOM; HOG000235246; -. DR HOVERGEN; HBG050605; -. DR InParanoid; Q71S46; -. DR KO; K02128; -. DR PhylomeDB; Q71S46; -. DR PRO; PR:Q71S46; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central. DR GO; GO:0005739; C:mitochondrion; ISO:RGD. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IBA:GO_Central. DR GO; GO:0007568; P:aging; IEP:RGD. DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro. DR GO; GO:0015986; P:ATP synthesis coupled proton transport; IBA:GO_Central. DR GO; GO:0045471; P:response to ethanol; 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; IPR002379; ATPase_proteolipid_c-like_dom. DR InterPro; IPR035921; F1F0_ATP_C_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 2: Evidence at transcript level; KW CF(0); Complete proteome; Hydrogen ion transport; Ion transport; KW Lipid-binding; Membrane; Mitochondrion; Reference proteome; KW Transit peptide; Transmembrane; Transmembrane helix; Transport. FT TRANSIT 1 67 Mitochondrion. {ECO:0000250}. FT CHAIN 68 142 ATP synthase F(0) complex subunit C3, FT mitochondrial. FT /FTId=PRO_0000002570. FT TRANSMEM 83 103 Helical. {ECO:0000255}. FT TRANSMEM 118 138 Helical. {ECO:0000255}. FT SITE 125 125 Reversibly protonated during proton FT transport. {ECO:0000250}. SQ SEQUENCE 142 AA; 14693 MW; 19EC0D1710A0AA3F CRC64; MFACAKLACT PSLIRAGSRV AYRPISASVL SRPEASRTGE GSTVFNGAQN GVSQLIQREF QTSAISRDID TAAKFIGAGA ATVGVAGSGA GIGTVFGSLI IGYARNPSLK QQLFSYAILG FALSEAMGLF CLMVAFLILF AM //