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   27-MAR-2024, entry version 212.
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   PDB; 8H9F; EM; 2.69 A; 1/2/3/4/5/6/7/8=62-136.
DR   PDB; 8H9J; EM; 3.26 A; 1/2/3/4/5/6/7/8=62-136.
DR   PDB; 8H9M; EM; 3.00 A; 1/2/3/4/5/6/7/8=62-136.
DR   PDB; 8H9Q; EM; 3.47 A; 1/2/3/4/5/6/7/8=62-136.
DR   PDB; 8H9S; EM; 2.53 A; 1/2/3/4/5/6/7/8=62-136.
DR   PDB; 8H9T; EM; 2.77 A; 1/2/3/4/5/6/7/8=62-136.
DR   PDB; 8H9U; EM; 2.61 A; 1/2/3/4/5/6/7/8=62-136.
DR   PDB; 8H9V; EM; 3.02 A; 1/2/3/4/5/6/7/8=62-136.
DR   PDBsum; 8H9F; -.
DR   PDBsum; 8H9J; -.
DR   PDBsum; 8H9M; -.
DR   PDBsum; 8H9Q; -.
DR   PDBsum; 8H9S; -.
DR   PDBsum; 8H9T; -.
DR   PDBsum; 8H9U; -.
DR   PDBsum; 8H9V; -.
DR   AlphaFoldDB; P05496; -.
DR   EMDB; EMD-34565; -.
DR   SMR; P05496; -.
DR   BioGRID; 107001; 38.
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; 9606-ENSP00000377033; -.
DR   PeptideAtlas; P05496; -.
DR   ProteomicsDB; 51842; -.
DR   Pumba; P05496; -.
DR   TopDownProteomics; P05496; -.
DR   Antibodypedia; 30318; 143 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   AGR; HGNC:841; -.
DR   CTD; 516; -.
DR   DisGeNET; 516; -.
DR   GeneCards; ATP5MC1; -.
DR   HGNC; HGNC:841; ATP5MC1.
DR   HPA; ENSG00000159199; Tissue enhanced (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; KIIGTGM; -.
DR   OrthoDB; 316029at2759; -.
DR   PhylomeDB; P05496; -.
DR   TreeFam; TF300140; -.
DR   BioCyc; MetaCyc:ENSG00000159199-MONOMER; -.
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; 73 hits in 1146 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 200 other cell types or tissues.
DR   ExpressionAtlas; P05496; baseline and differential.
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: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   CDD; cd18182; ATP-synt_Fo_c_ATP5G3; 1.
DR   Gene3D; 1.20.20.10; F1F0 ATP synthase subunit C; 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; ATP SYNTHASE LIPID-BINDING PROTEIN, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR10031:SF0; ATPASE PROTEIN 9; 1.
DR   Pfam; PF00137; ATP-synt_C; 1.
DR   PRINTS; PR00124; ATPASEC.
DR   SUPFAM; SSF81333; F1F0 ATP synthase subunit C; 1.
DR   PROSITE; PS00605; ATPASE_C; 1.
DR   Genevisible; P05496; HS.
PE   1: Evidence at protein level;
KW   3D-structure; CF(0); Hydrogen ion transport; Ion transport; Lipid-binding;
KW   Membrane; 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"
FT   HELIX           63..77
FT                   /evidence="ECO:0007829|PDB:8H9M"
FT   HELIX           80..99
FT                   /evidence="ECO:0007829|PDB:8H9M"
FT   HELIX           101..103
FT                   /evidence="ECO:0007829|PDB:8H9M"
FT   HELIX           104..133
FT                   /evidence="ECO:0007829|PDB:8H9M"
SQ   SEQUENCE   136 AA;  14277 MW;  1AFF1F16BB532647 CRC64;
     MQTAGALFIS PALIRCCTRG LIRPVSASFL NSPVNSSKQP SYSNFPLQVA RREFQTSVVS
     RDIDTAAKFI GAGAATVGVA GSGAGIGTVF GSLIIGYARN PSLKQQLFSY AILGFALSEA
     MGLFCLMVAF LILFAM
//