ATP5L_HUMAN
ID ATP5L_HUMAN Reviewed; 103 AA.
AC O75964; A8K0K3; Q96BV6; Q9UBZ7;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=ATP synthase subunit g, mitochondrial {ECO:0000305};
DE Short=ATPase subunit g;
DE AltName: Full=ATP synthase membrane subunit g {ECO:0000305};
GN Name=ATP5MG {ECO:0000312|HGNC:HGNC:14247}; Synonyms=ATP5L;
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 [MRNA].
RC TISSUE=Thymus;
RA Kang Y.J., Hwang M.Y., Lee M.Y., Lee H.C., Sohn U.;
RT "Molecular cloning and chromosomal assignment of F1F0-type ATP synthase
RT subunit g from human infant thymus.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhang M., Yu L., Zhou Y., Hu P.R., Xin Y.R., Zhao S.Y.;
RT "Cloning and characterization of a novel human cDNA homologous to Bos
RT taurus F1Fo-ATP synthase complex Fo membrane domain g subunit mRNA.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-24, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
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
CC F(0) - containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation. Part of the complex
CC F(0) domain. Minor subunit located with subunit a in the membrane.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(0) seems to have nine
CC subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). Component of an ATP
CC synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME,
CC ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C,
CC ATP5PO, ATP5MG, ATP5MK and ATP5MJ (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC O75964; P13473-2: LAMP2; NbExp=3; IntAct=EBI-1044001, EBI-21591415;
CC O75964; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-1044001, EBI-2623095;
CC O75964; Q8WW59: SPRYD4; NbExp=2; IntAct=EBI-1044001, EBI-8602056;
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC -!- SIMILARITY: Belongs to the ATPase g subunit family. {ECO:0000305}.
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DR EMBL; AF092124; AAC61597.1; -; mRNA.
DR EMBL; AF087846; AAP97159.1; -; mRNA.
DR EMBL; AF070655; AAD20961.1; -; mRNA.
DR EMBL; AL050277; CAB43378.1; -; mRNA.
DR EMBL; CR533494; CAG38525.1; -; mRNA.
DR EMBL; CR542211; CAG47007.1; -; mRNA.
DR EMBL; AK289568; BAF82257.1; -; mRNA.
DR EMBL; CH471065; EAW67376.1; -; Genomic_DNA.
DR EMBL; BC015128; AAH15128.1; -; mRNA.
DR EMBL; BC070165; AAH70165.1; -; mRNA.
DR CCDS; CCDS8397.1; -.
DR PIR; T08727; T08727.
DR RefSeq; NP_006467.4; NM_006476.4.
DR AlphaFoldDB; O75964; -.
DR SMR; O75964; -.
DR BioGRID; 115876; 147.
DR ComplexPortal; CPX-6151; Mitochondrial proton-transporting ATP synthase complex.
DR CORUM; O75964; -.
DR IntAct; O75964; 53.
DR MINT; O75964; -.
DR STRING; 9606.ENSP00000300688; -.
DR DrugBank; DB11638; Artenimol.
DR DrugBank; DB12695; Phenethyl Isothiocyanate.
DR TCDB; 3.A.2.1.15; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR CarbonylDB; O75964; -.
DR iPTMnet; O75964; -.
DR PhosphoSitePlus; O75964; -.
DR SwissPalm; O75964; -.
DR BioMuta; ATP5L; -.
DR EPD; O75964; -.
DR jPOST; O75964; -.
DR MassIVE; O75964; -.
DR MaxQB; O75964; -.
DR PaxDb; O75964; -.
DR PeptideAtlas; O75964; -.
DR PRIDE; O75964; -.
DR ProteomicsDB; 50328; -.
DR TopDownProteomics; O75964; -.
DR Antibodypedia; 45792; 66 antibodies from 19 providers.
DR DNASU; 10632; -.
DR Ensembl; ENST00000300688.8; ENSP00000300688.3; ENSG00000167283.9.
DR GeneID; 10632; -.
DR KEGG; hsa:10632; -.
DR MANE-Select; ENST00000300688.8; ENSP00000300688.3; NM_006476.5; NP_006467.4.
DR UCSC; uc001psx.4; human.
DR CTD; 10632; -.
DR DisGeNET; 10632; -.
DR GeneCards; ATP5MG; -.
DR HGNC; HGNC:14247; ATP5MG.
DR HPA; ENSG00000167283; Low tissue specificity.
DR MIM; 617473; gene.
DR neXtProt; NX_O75964; -.
DR OpenTargets; ENSG00000167283; -.
DR PharmGKB; PA25143; -.
DR VEuPathDB; HostDB:ENSG00000167283; -.
DR eggNOG; KOG4103; Eukaryota.
DR GeneTree; ENSGT00390000009724; -.
DR HOGENOM; CLU_152793_1_1_1; -.
DR InParanoid; O75964; -.
DR OMA; ATEVCMW; -.
DR OrthoDB; 1461139at2759; -.
DR PhylomeDB; O75964; -.
DR TreeFam; TF313978; -.
DR BioCyc; MetaCyc:HS09535-MON; -.
DR PathwayCommons; O75964; -.
DR Reactome; R-HSA-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-HSA-8949613; Cristae formation.
DR SignaLink; O75964; -.
DR SIGNOR; O75964; -.
DR BioGRID-ORCS; 10632; 432 hits in 1038 CRISPR screens.
DR ChiTaRS; ATP5MG; human.
DR GeneWiki; ATP5L; -.
DR GenomeRNAi; 10632; -.
DR Pharos; O75964; Tbio.
DR PRO; PR:O75964; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; O75964; protein.
DR Bgee; ENSG00000167283; Expressed in ganglionic eminence and 210 other tissues.
DR ExpressionAtlas; O75964; baseline and differential.
DR Genevisible; O75964; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
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); IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:LIFEdb.
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 GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IDA:UniProtKB.
DR InterPro; IPR006808; ATP_synth_F0_gsu_mt.
DR InterPro; IPR016702; ATP_synth_su_G_mt_met.
DR PANTHER; PTHR12386; PTHR12386; 1.
DR Pfam; PF04718; ATP-synt_G; 1.
DR PIRSF; PIRSF017835; ATP-synth_g_mitoch_animal; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP synthesis; CF(0); Hydrogen ion transport; Ion transport;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..103
FT /note="ATP synthase subunit g, mitochondrial"
FT /id="PRO_0000071691"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 11
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CPQ8"
FT MOD_RES 24
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 35
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CPQ8"
FT MOD_RES 54
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CPQ8"
FT CONFLICT 2
FT /note="A -> G (in Ref. 1; AAC61597)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="R -> K (in Ref. 1; AAC61597)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="V -> A (in Ref. 8; AAH15128)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 103 AA; 11428 MW; 03D484BCF836E6C2 CRC64;
MAQFVRNLVE KTPALVNAAV TYSKPRLATF WYYAKVELVP PTPAEIPRAI QSLKKIVNSA
QTGSFKQLTV KEAVLNGLVA TEVLMWFYVG EIIGKRGIIG YDV
