AT5G1_HUMAN
ID AT5G1_HUMAN Reviewed; 136 AA.
AC P05496;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 203.
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|HGNC:HGNC:841};
DE AltName: Full=ATP synthase proteolipid P1;
DE AltName: Full=ATP synthase proton-transporting mitochondrial F(0) complex subunit C1;
DE AltName: Full=ATPase protein 9;
DE AltName: Full=ATPase subunit c;
DE Flags: Precursor;
GN Name=ATP5MC1 {ECO:0000312|HGNC:HGNC:841};
GN Synonyms=ATP5G1 {ECO:0000312|HGNC:HGNC:841};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8328972; DOI=10.1042/bj2930051;
RA Dyer M.R., Walker J.E.;
RT "Sequences of members of the human gene family for the c subunit of
RT mitochondrial ATP synthase.";
RL Biochem. J. 293:51-64(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8485160; DOI=10.1016/0167-4781(93)90249-d;
RA Higuti T., Kawamura Y., Kuroiwa K., Miyazaki S., Tsujita H.;
RT "Molecular cloning and sequence of two cDNAs for human subunit c of H(+)-
RT ATP synthase in mitochondria.";
RL Biochim. Biophys. Acta 1173:87-90(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 37-136.
RC TISSUE=Liver;
RX PubMed=2883974; DOI=10.1016/0006-291x(87)91446-x;
RA Farrell L.B., Nagley P.;
RT "Human liver cDNA clones encoding proteolipid subunit 9 of the
RT mitochondrial ATPase complex.";
RL Biochem. Biophys. Res. Commun. 144:1257-1264(1987).
RN [7]
RP INTERACTION WITH TMEM70, AND SUBUNIT.
RX PubMed=31652072; DOI=10.1096/fj.201900685rr;
RA Kovalcikova J., Vrbacky M., Pecina P., Tauchmannova K., Nuskova H.,
RA Kaplanova V., Brazdova A., Alan L., Elias J., Cunatova K., Korinek V.,
RA Sedlacek R., Mracek T., Houstek J.;
RT "TMEM70 facilitates biogenesis of mammalian ATP synthase by promoting
RT subunit c incorporation into the rotor structure of the enzyme.";
RL FASEB J. 33:14103-14117(2019).
RN [8]
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).
RN [9]
RP INTERACTION WITH TMEM70.
RX PubMed=33359711; DOI=10.1016/j.bbamcr.2020.118942;
RA Bahri H., Buratto J., Rojo M., Dompierre J.P., Salin B., Blancard C.,
RA Cuvellier S., Rose M., Ben Ammar Elgaaied A., Tetaud E., di Rago J.P.,
RA Devin A., Duvezin-Caubet S.;
RT "TMEM70 forms oligomeric scaffolds within mitochondrial cristae promoting
RT in situ assembly of mammalian ATP synthase proton channel.";
RL Biochim. Biophys. Acta 1868:118942-118942(2021).
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 (PubMed:31652072). 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 (By
CC similarity). 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 (PubMed:31652072). {ECO:0000250,
CC ECO:0000269|PubMed:31652072}.
CC -!- INTERACTION:
CC P05496; P35609: ACTN2; NbExp=3; IntAct=EBI-10194585, EBI-77797;
CC P05496; Q86WT6: TRIM69; NbExp=4; IntAct=EBI-10194585, EBI-749955;
CC P05496; Q86WT6-2: TRIM69; NbExp=3; IntAct=EBI-10194585, EBI-11525489;
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 -!- 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. Is the major protein stored in
CC the storage bodies of animals or humans affected with ceroid
CC lipofuscinosis (Batten disease).
CC -!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000305}.
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DR EMBL; X69907; CAA49532.1; -; Genomic_DNA.
DR EMBL; D13118; BAA02420.1; -; mRNA.
DR EMBL; AL080089; CAB45704.1; -; mRNA.
DR EMBL; BT007230; AAP35894.1; -; mRNA.
DR EMBL; BC004963; AAH04963.1; -; mRNA.
DR EMBL; M16453; AAA51806.1; -; mRNA.
DR CCDS; CCDS11539.1; -.
DR PIR; S34066; S34066.
DR RefSeq; NP_001002027.1; NM_001002027.1.
DR RefSeq; NP_005166.1; NM_005175.2.
DR AlphaFoldDB; P05496; -.
DR SMR; P05496; -.
DR BioGRID; 107001; 37.
DR ComplexPortal; CPX-6151; Mitochondrial proton-transporting ATP synthase complex.
DR CORUM; P05496; -.
DR IntAct; P05496; 10.
DR STRING; 9606.ENSP00000377033; -.
DR TCDB; 3.A.2.1.15; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR iPTMnet; P05496; -.
DR PhosphoSitePlus; P05496; -.
DR BioMuta; ATP5G1; -.
DR EPD; P05496; -.
DR jPOST; P05496; -.
DR MassIVE; P05496; -.
DR PaxDb; P05496; -.
DR PeptideAtlas; P05496; -.
DR PRIDE; P05496; -.
DR ProteomicsDB; 51842; -.
DR TopDownProteomics; P05496; -.
DR Antibodypedia; 30318; 126 antibodies from 29 providers.
DR DNASU; 516; -.
DR Ensembl; ENST00000355938.9; ENSP00000348205.5; ENSG00000159199.14.
DR Ensembl; ENST00000393366.7; ENSP00000377033.2; ENSG00000159199.14.
DR GeneID; 516; -.
DR KEGG; hsa:516; -.
DR MANE-Select; ENST00000393366.7; ENSP00000377033.2; NM_005175.3; NP_005166.1.
DR CTD; 516; -.
DR DisGeNET; 516; -.
DR GeneCards; ATP5MC1; -.
DR HGNC; HGNC:841; ATP5MC1.
DR HPA; ENSG00000159199; Tissue enhanced (skeletal muscle, tongue).
DR MIM; 603192; gene.
DR neXtProt; NX_P05496; -.
DR OpenTargets; ENSG00000159199; -.
DR PharmGKB; PA25131; -.
DR VEuPathDB; HostDB:ENSG00000159199; -.
DR eggNOG; KOG3025; Eukaryota.
DR GeneTree; ENSGT00940000154298; -.
DR InParanoid; P05496; -.
DR OMA; CMGFCIL; -.
DR OrthoDB; 1564365at2759; -.
DR PhylomeDB; P05496; -.
DR TreeFam; TF300140; -.
DR BioCyc; MetaCyc:ENSG00000159199-MON; -.
DR PathwayCommons; P05496; -.
DR Reactome; R-HSA-1268020; Mitochondrial protein import.
DR Reactome; R-HSA-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-HSA-8949613; Cristae formation.
DR SignaLink; P05496; -.
DR SIGNOR; P05496; -.
DR BioGRID-ORCS; 516; 67 hits in 1071 CRISPR screens.
DR ChiTaRS; ATP5G1; human.
DR GeneWiki; ATP5G1; -.
DR GenomeRNAi; 516; -.
DR Pharos; P05496; Tbio.
DR PRO; PR:P05496; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P05496; protein.
DR Bgee; ENSG00000159199; Expressed in apex of heart and 198 other tissues.
DR ExpressionAtlas; P05496; baseline and differential.
DR Genevisible; P05496; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
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); IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:LIFEdb.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
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_0000002557"
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 53
FT /note="E -> G (in Ref. 6; AAA51806)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 136 AA; 14277 MW; 1AFF1F16BB532647 CRC64;
MQTAGALFIS PALIRCCTRG LIRPVSASFL NSPVNSSKQP SYSNFPLQVA RREFQTSVVS
RDIDTAAKFI GAGAATVGVA GSGAGIGTVF GSLIIGYARN PSLKQQLFSY AILGFALSEA
MGLFCLMVAF LILFAM
