AT5G1_MOUSE
ID AT5G1_MOUSE Reviewed; 136 AA.
AC Q9CR84; Q3TIE9;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
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:0000250|UniProtKB:P05496};
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:0000250|UniProtKB:P05496}; Synonyms=Atp5g1;
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=BALB/cJ, and C57BL/6J; TISSUE=Liver, Small intestine, and Tongue;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
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 [5]
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 (By similarity). {ECO:0000250}.
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. Component of an ATP synthase complex composed of
CC ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-
CC ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and
CC ATP5MJ (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
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 but identical mature proteins. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000305}.
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DR EMBL; AK008191; BAB25522.1; -; mRNA.
DR EMBL; AK008998; BAB26015.1; -; mRNA.
DR EMBL; AK009883; BAB26561.1; -; mRNA.
DR EMBL; AK010868; BAB27233.1; -; mRNA.
DR EMBL; AK011054; BAB27363.1; -; mRNA.
DR EMBL; AK011432; BAB27617.1; -; mRNA.
DR EMBL; AK167884; BAE39897.1; -; mRNA.
DR EMBL; AL603682; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466556; EDL16011.1; -; Genomic_DNA.
DR EMBL; CH466556; EDL16012.1; -; Genomic_DNA.
DR EMBL; CH466556; EDL16013.1; -; Genomic_DNA.
DR EMBL; BC003854; AAH03854.1; -; mRNA.
DR EMBL; BC094664; AAH94664.1; -; mRNA.
DR CCDS; CCDS25289.1; -.
DR RefSeq; NP_001154891.1; NM_001161419.1.
DR RefSeq; NP_031532.2; NM_007506.6.
DR AlphaFoldDB; Q9CR84; -.
DR SMR; Q9CR84; -.
DR STRING; 10090.ENSMUSP00000103312; -.
DR PhosphoSitePlus; Q9CR84; -.
DR jPOST; Q9CR84; -.
DR PaxDb; Q9CR84; -.
DR PRIDE; Q9CR84; -.
DR ProteomicsDB; 277056; -.
DR DNASU; 11951; -.
DR Ensembl; ENSMUST00000090541; ENSMUSP00000088029; ENSMUSG00000006057.
DR Ensembl; ENSMUST00000107684; ENSMUSP00000103312; ENSMUSG00000006057.
DR Ensembl; ENSMUST00000107686; ENSMUSP00000103314; ENSMUSG00000006057.
DR Ensembl; ENSMUST00000178611; ENSMUSP00000137633; ENSMUSG00000006057.
DR GeneID; 11951; -.
DR KEGG; mmu:11951; -.
DR UCSC; uc007lbf.2; mouse.
DR CTD; 11951; -.
DR MGI; MGI:107653; Atp5g1.
DR VEuPathDB; HostDB:ENSMUSG00000006057; -.
DR eggNOG; KOG3025; Eukaryota.
DR GeneTree; ENSGT00940000159720; -.
DR HOGENOM; CLU_116822_1_0_1; -.
DR InParanoid; Q9CR84; -.
DR OMA; ACHRPRC; -.
DR OrthoDB; 1564365at2759; -.
DR PhylomeDB; Q9CR84; -.
DR TreeFam; TF300140; -.
DR Reactome; R-MMU-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-MMU-8949613; Cristae formation.
DR BioGRID-ORCS; 11951; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Atp5g1; mouse.
DR PRO; PR:Q9CR84; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9CR84; protein.
DR Bgee; ENSMUSG00000006057; Expressed in right kidney and 150 other tissues.
DR Genevisible; Q9CR84; MM.
DR GO; GO:0034703; C:cation channel complex; ISO:MGI.
DR GO; GO:0150034; C:distal axon; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; ISS:UniProtKB.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO: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:0006754; P:ATP biosynthetic process; ISO:MGI.
DR GO; GO:0046034; P:ATP metabolic process; ISO:MGI.
DR GO; GO:1905232; P:cellular response to L-glutamate; ISO:MGI.
DR GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; ISO:MGI.
DR GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; ISO:MGI.
DR GO; GO:0046931; P:pore complex assembly; ISO:MGI.
DR GO; GO:0045773; P:positive regulation of axon extension; ISO:MGI.
DR GO; GO:1901216; P:positive regulation of neuron death; 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..61
FT /note="Mitochondrion"
FT CHAIN 62..136
FT /note="ATP synthase F(0) complex subunit C1, mitochondrial"
FT /id="PRO_0000395412"
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"
FT CONFLICT 12
FT /note="A -> V (in Ref. 1; BAE39897)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 136 AA; 14200 MW; 12B9ABDEE627994C CRC64;
MQTTKALLIS PALIRSCTRG LIRPVSASLL SRPEAPSKQP SCSSSPLQVA RREFQTSVIS
RDIDTAAKFI GAGAATVGVA GSGAGIGTVF GSLIIGYARN PSLKQQLFSY AILGFALSEA
MGLFCLMVAF LILFAM
