AT5G1_RAT
ID AT5G1_RAT Reviewed; 136 AA.
AC Q06645;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=ATP synthase F(0) complex subunit C1, mitochondrial {ECO:0000305};
DE AltName: Full=ATP synthase lipid-binding protein;
DE AltName: Full=ATP synthase membrane subunit c locus 1 {ECO:0000312|RGD:61933};
DE AltName: Full=ATP synthase proteolipid P1;
DE AltName: Full=ATPase protein 9;
DE AltName: Full=ATPase subunit c;
DE Flags: Precursor;
GN Name=Atp5mc1 {ECO:0000312|RGD:61933}; Synonyms=Atp5g1;
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 IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE ATP SYNTHASE
RP COMPLEX.
RX PubMed=17575325; DOI=10.1074/mcp.m700097-mcp200;
RA Meyer B., Wittig I., Trifilieff E., Karas M., Schaegger H.;
RT "Identification of two proteins associated with mammalian ATP synthase.";
RL Mol. Cell. Proteomics 6:1690-1699(2007).
RN [3]
RP METHYLATION AT LYS-104.
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: Homooligomer (By similarity). F-type ATPases have 2
CC components, CF(1) - the catalytic core - and CF(0) - the membrane
CC proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1),
CC delta(1), epsilon(1). CF(0) has three main subunits: a, b and c.
CC Component of an ATP synthase complex composed of ATP5PB, ATP5MC1,
CC ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A,
CC ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and ATP5MJ
CC (PubMed:17575325). Interacts with TMEM70 (homooligomer form); this
CC interaction facilitates the oligomer formation of subunit c/ATP5MC1 (c-
CC ring) and the c-ring membrane insertion and also protects ATP5MC1
CC against intramitochondrial proteolysis (By similarity).
CC {ECO:0000250|UniProtKB:P05496, ECO:0000269|PubMed:17575325}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane
CC protein.
CC -!- PTM: Trimethylated by ATPSCKMT at Lys-104. 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; D13123; BAA02425.1; -; mRNA.
DR PIR; JS0740; JS0740.
DR RefSeq; NP_059007.1; NM_017311.1.
DR RefSeq; XP_006247250.1; XM_006247188.3.
DR RefSeq; XP_006247251.1; XM_006247189.1.
DR AlphaFoldDB; Q06645; -.
DR SMR; Q06645; -.
DR CORUM; Q06645; -.
DR STRING; 10116.ENSRNOP00000009815; -.
DR jPOST; Q06645; -.
DR PaxDb; Q06645; -.
DR GeneID; 29754; -.
DR KEGG; rno:29754; -.
DR UCSC; RGD:61933; rat.
DR CTD; 516; -.
DR RGD; 61933; Atp5mc1.
DR eggNOG; KOG3025; Eukaryota.
DR HOGENOM; CLU_116822_1_0_1; -.
DR InParanoid; Q06645; -.
DR OMA; VPQSTFF; -.
DR OrthoDB; 1564365at2759; -.
DR PhylomeDB; Q06645; -.
DR TreeFam; TF300140; -.
DR Reactome; R-RNO-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-RNO-8949613; Cristae formation.
DR PRO; PR:Q06645; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000007235; Expressed in heart and 19 other tissues.
DR Genevisible; Q06645; RN.
DR GO; GO:0034703; C:cation channel complex; IDA:RGD.
DR GO; GO:0150034; C:distal axon; IDA:RGD.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; NAS:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
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:0006754; P:ATP biosynthetic process; IMP:RGD.
DR GO; GO:0046034; P:ATP metabolic process; IDA:RGD.
DR GO; GO:1905232; P:cellular response to L-glutamate; IMP:RGD.
DR GO; GO:0009631; P:cold acclimation; IEP:RGD.
DR GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; IMP:RGD.
DR GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; IMP:RGD.
DR GO; GO:0046931; P:pore complex assembly; IDA:RGD.
DR GO; GO:0045773; P:positive regulation of axon extension; IMP:RGD.
DR GO; GO:1901216; P:positive regulation of neuron death; IMP: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..61
FT /note="Mitochondrion"
FT CHAIN 62..136
FT /note="ATP synthase F(0) complex subunit C1, mitochondrial"
FT /id="PRO_0000002559"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 119
FT /note="Reversibly protonated during proton transport"
FT /evidence="ECO:0000250"
FT MOD_RES 104
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:30530489"
SQ SEQUENCE 136 AA; 14244 MW; 91060591516D6AF6 CRC64;
MQTTKALLIS PVLIRSCTRG LIRPVSASLL SRPEAPSKKP SCCSSPLQVA RREFQTSVIS
RDIDTAAKFI GAGAATVGVA GSGAGIGTVF GSLIIGYARN PSLKQQLFSY AILGFALSEA
MGLFCLMVAF LILFAM
