AT5G2_HUMAN
ID AT5G2_HUMAN Reviewed; 141 AA.
AC Q06055; B3KQQ6;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 192.
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|HGNC:HGNC:842};
DE AltName: Full=ATP synthase proteolipid P2;
DE AltName: Full=ATP synthase proton-transporting mitochondrial F(0) complex subunit C2;
DE AltName: Full=ATPase protein 9;
DE AltName: Full=ATPase subunit c;
DE Flags: Precursor;
GN Name=ATP5MC2 {ECO:0000312|HGNC:HGNC:842};
GN Synonyms=ATP5G2 {ECO:0000312|HGNC:HGNC:842}; ORFNames=PSEC0033;
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] (ISOFORM 1).
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] (ISOFORM 1).
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 87-141 (ISOFORMS 1/2/3).
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 DNAJC30.
RX PubMed=30318146; DOI=10.1016/j.cell.2018.09.014;
RA Tebbenkamp A.T.N., Varela L., Choi J., Paredes M.I., Giani A.M., Song J.E.,
RA Sestan-Pesa M., Franjic D., Sousa A.M.M., Liu Z.W., Li M., Bichsel C.,
RA Koch M., Szigeti-Buck K., Liu F., Li Z., Kawasawa Y.I., Paspalas C.D.,
RA Mineur Y.S., Prontera P., Merla G., Picciotto M.R., Arnsten A.F.T.,
RA Horvath T.L., Sestan N.;
RT "The 7q11.23 protein DNAJC30 interacts with ATP synthase and links
RT mitochondria to brain development.";
RL Cell 0:0-0(2018).
RN [8]
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 (PubMed:8328972). Interacts with DNAJC30;
CC interaction is direct (PubMed:30318146). {ECO:0000269|PubMed:30318146,
CC ECO:0000269|PubMed:8328972}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q06055-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q06055-2; Sequence=VSP_037348;
CC Name=3;
CC IsoId=Q06055-3; Sequence=VSP_037349;
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 -!- 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; X69908; CAA49533.1; -; Genomic_DNA.
DR EMBL; D13119; BAA02421.1; -; mRNA.
DR EMBL; AK075351; BAG52118.1; -; mRNA.
DR EMBL; AC073594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC020826; AAH20826.1; -; mRNA.
DR CCDS; CCDS31812.1; -. [Q06055-3]
DR CCDS; CCDS81694.1; -. [Q06055-1]
DR PIR; S34067; S34067.
DR RefSeq; NP_001002031.1; NM_001002031.2. [Q06055-3]
DR RefSeq; NP_001317198.1; NM_001330269.1. [Q06055-1]
DR RefSeq; NP_005167.2; NM_005176.5. [Q06055-1]
DR RefSeq; XP_016874949.1; XM_017019460.1. [Q06055-2]
DR RefSeq; XP_016874950.1; XM_017019461.1. [Q06055-3]
DR AlphaFoldDB; Q06055; -.
DR SMR; Q06055; -.
DR BioGRID; 107002; 6.
DR ComplexPortal; CPX-6151; Mitochondrial proton-transporting ATP synthase complex.
DR IntAct; Q06055; 6.
DR MINT; Q06055; -.
DR STRING; 9606.ENSP00000377878; -.
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; Q06055; -.
DR PhosphoSitePlus; Q06055; -.
DR SwissPalm; Q06055; -.
DR BioMuta; ATP5G2; -.
DR DMDM; 461592; -.
DR jPOST; Q06055; -.
DR MassIVE; Q06055; -.
DR MaxQB; Q06055; -.
DR PaxDb; Q06055; -.
DR PeptideAtlas; Q06055; -.
DR PRIDE; Q06055; -.
DR ProteomicsDB; 58411; -. [Q06055-1]
DR ProteomicsDB; 58412; -. [Q06055-2]
DR ProteomicsDB; 58413; -. [Q06055-3]
DR TopDownProteomics; Q06055-1; -. [Q06055-1]
DR TopDownProteomics; Q06055-2; -. [Q06055-2]
DR TopDownProteomics; Q06055-3; -. [Q06055-3]
DR Antibodypedia; 27225; 159 antibodies from 29 providers.
DR DNASU; 517; -.
DR Ensembl; ENST00000338662.6; ENSP00000340315.6; ENSG00000135390.21. [Q06055-1]
DR Ensembl; ENST00000394349.9; ENSP00000377878.5; ENSG00000135390.21. [Q06055-1]
DR Ensembl; ENST00000549164.5; ENSP00000447317.1; ENSG00000135390.21. [Q06055-1]
DR Ensembl; ENST00000552242.5; ENSP00000448801.2; ENSG00000135390.21. [Q06055-1]
DR Ensembl; ENST00000673498.1; ENSP00000499883.1; ENSG00000135390.21. [Q06055-3]
DR GeneID; 517; -.
DR KEGG; hsa:517; -.
DR MANE-Select; ENST00000394349.9; ENSP00000377878.5; NM_005176.7; NP_005167.3.
DR UCSC; uc001sec.4; human. [Q06055-1]
DR CTD; 517; -.
DR DisGeNET; 517; -.
DR GeneCards; ATP5MC2; -.
DR HGNC; HGNC:842; ATP5MC2.
DR HPA; ENSG00000135390; Low tissue specificity.
DR MIM; 603193; gene.
DR neXtProt; NX_Q06055; -.
DR OpenTargets; ENSG00000135390; -.
DR PharmGKB; PA25132; -.
DR VEuPathDB; HostDB:ENSG00000135390; -.
DR eggNOG; KOG3025; Eukaryota.
DR GeneTree; ENSGT00940000157455; -.
DR HOGENOM; CLU_116822_1_0_1; -.
DR InParanoid; Q06055; -.
DR OrthoDB; 1564365at2759; -.
DR PhylomeDB; Q06055; -.
DR TreeFam; TF300140; -.
DR BioCyc; MetaCyc:HS05994-MON; -.
DR PathwayCommons; Q06055; -.
DR Reactome; R-HSA-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-HSA-8949613; Cristae formation.
DR SignaLink; Q06055; -.
DR BioGRID-ORCS; 517; 49 hits in 1074 CRISPR screens.
DR ChiTaRS; ATP5MC2; human.
DR GeneWiki; ATP5G2; -.
DR GenomeRNAi; 517; -.
DR Pharos; Q06055; Tbio.
DR PRO; PR:Q06055; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q06055; protein.
DR Bgee; ENSG00000135390; Expressed in apex of heart and 205 other tissues.
DR ExpressionAtlas; Q06055; baseline and differential.
DR Genevisible; Q06055; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IC:ComplexPortal.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IC:ComplexPortal.
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: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 Alternative splicing; CF(0); Hydrogen ion transport; Ion transport;
KW Lipid-binding; Membrane; Methylation; Mitochondrion; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..66
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 67..141
FT /note="ATP synthase F(0) complex subunit C2, mitochondrial"
FT /id="PRO_0000002562"
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"
FT VAR_SEQ 1
FT /note="M -> MPELILYVAITLSVAERLVGPGHACAEPSFRSSRCSAPLCLLCSGSS
FT SPATAPHPLKM (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_037348"
FT VAR_SEQ 1
FT /note="M -> MPELILSPATAPHPLKM (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_037349"
FT VARIANT 58
FT /note="S -> I (in dbSNP:rs13819)"
FT /id="VAR_011920"
FT VARIANT 141
FT /note="M -> K (in dbSNP:rs1803177)"
FT /id="VAR_011921"
FT CONFLICT 63
FT /note="A -> T (in Ref. 3; BAG52118)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="S -> F (in Ref. 3; BAG52118)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 141 AA; 14637 MW; 6E627A504A7AE52D CRC64;
MFACSKFVST PSLVKSTSQL LSRPLSAVVL KRPEILTDES LSSLAVSCPL TSLVSSRSFQ
TSAISRDIDT AAKFIGAGAA TVGVAGSGAG IGTVFGSLII GYARNPSLKQ QLFSYAILGF
ALSEAMGLFC LMVAFLILFA M
