AT5G2_RAT
ID AT5G2_RAT Reviewed; 141 AA.
AC Q06646; A2VCW6;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=ATP synthase F(0) complex subunit C2, mitochondrial {ECO:0000305};
DE AltName: Full=ATP synthase lipid-binding protein;
DE AltName: Full=ATP synthase membrane subunit c locus 2 {ECO:0000312|RGD:620051};
DE AltName: Full=ATP synthase proteolipid P2;
DE AltName: Full=ATPase protein 9;
DE AltName: Full=ATPase subunit c;
DE Flags: Precursor;
GN Name=Atp5mc2 {ECO:0000312|RGD:620051}; Synonyms=Atp5g2;
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=8448208; DOI=10.1016/0167-4781(93)90219-4;
RA Higuti T., Kuroiwa K., Kawamura Y., Morimoto K., Tsujita H.;
RT "Molecular cloning and sequence of cDNAs for the import precursors of
RT oligomycin sensitivity conferring protein, ATPase inhibitor protein, and
RT subunit c of H(+)-ATP synthase in rat mitochondria.";
RL Biochim. Biophys. Acta 1172:311-314(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 [3]
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 DNAJC30; interaction is direct.
CC {ECO:0000250|UniProtKB:Q06055}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane
CC protein.
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. They are expressed in a tissue-specific manner.
CC -!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000305}.
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DR EMBL; D13124; BAA02426.1; -; mRNA.
DR EMBL; BC128726; AAI28727.1; -; mRNA.
DR PIR; JS0741; JS0741.
DR RefSeq; NP_598240.1; NM_133556.2.
DR AlphaFoldDB; Q06646; -.
DR SMR; Q06646; -.
DR BioGRID; 251094; 3.
DR CORUM; Q06646; -.
DR STRING; 10116.ENSRNOP00000020675; -.
DR PhosphoSitePlus; Q06646; -.
DR jPOST; Q06646; -.
DR PaxDb; Q06646; -.
DR Ensembl; ENSRNOT00000020676; ENSRNOP00000020675; ENSRNOG00000015320.
DR GeneID; 171082; -.
DR KEGG; rno:171082; -.
DR UCSC; RGD:620051; rat.
DR CTD; 517; -.
DR RGD; 620051; Atp5mc2.
DR eggNOG; KOG3025; Eukaryota.
DR GeneTree; ENSGT00940000157455; -.
DR InParanoid; Q06646; -.
DR OrthoDB; 1564365at2759; -.
DR Reactome; R-RNO-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-RNO-8949613; Cristae formation.
DR PRO; PR:Q06646; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000015320; Expressed in quadriceps femoris and 19 other tissues.
DR ExpressionAtlas; Q06646; baseline and differential.
DR Genevisible; Q06646; RN.
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:0046931; P:pore complex assembly; IDA:RGD.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR GO; GO:1905242; P:response to 3,3',5-triiodo-L-thyronine; IEP:RGD.
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; 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 CHAIN 67..141
FT /note="ATP synthase F(0) complex subunit C2, mitochondrial"
FT /id="PRO_0000002566"
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; 14918 MW; C643B542A8432B98 CRC64;
MYACSKFVST RSLIRSTSQL LSRPLSAVEL KRPQMPTDEG LSCLAVRRPL TSLIPSRSFQ
TSAISRDIDT AAKFIGAGAA TVGVAGSGAG IGTVFGSLII GYARNPSLKQ QLFSYAILGF
ALSEAMGLFC LMVAFLILFA M
