ID ATP5S_HUMAN Reviewed; 200 AA. AC Q99766; A0A2R8YDJ1; A0A5K1VW60; A8K1U3; D9N156; Q8WWX3; Q96F77; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2024, sequence version 4. DT 27-MAR-2024, entry version 174. DE RecName: Full=ATP synthase subunit s, mitochondrial {ECO:0000305}; DE AltName: Full=ATP synthase-coupling factor B; DE Short=FB; DE AltName: Full=Distal membrane arm assembly complex 2-like protein {ECO:0000312|HGNC:HGNC:18799}; DE AltName: Full=Mitochondrial ATP synthase regulatory component factor B; DE Flags: Precursor; GN Name=DMAC2L {ECO:0000312|HGNC:HGNC:18799}; GN Synonyms=ATP5S {ECO:0000312|HGNC:HGNC:18799}, ATPW; 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 [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT LEU-3. RC TISSUE=Brain; RX PubMed=9110174; DOI=10.1101/gr.7.4.353; RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.; RT "Large-scale concatenation cDNA sequencing."; RL Genome Res. 7:353-358(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, SUBUNIT, RP AND VARIANT LEU-3. RX PubMed=11744738; DOI=10.1074/jbc.m111256200; RA Belogrudov G.I., Hatefi Y.; RT "Factor B and the mitochondrial ATP synthase complex."; RL J. Biol. Chem. 277:6097-6103(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-3. RC TISSUE=Hippocampus; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., RA Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LEU-3. 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT LEU-3. RC TISSUE=Uterus; 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 [7] 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 [8] 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: Involved in regulation of mitochondrial membrane ATP CC synthase. Necessary for H(+) conduction of ATP synthase. Facilitates CC energy-driven catalysis of ATP synthesis by blocking a proton leak CC through an alternative proton exit pathway. CC {ECO:0000250|UniProtKB:P22027}. CC -!- SUBUNIT: Homotetramer. Associates with ATP synthase. CC {ECO:0000250|UniProtKB:P22027}. CC -!- INTERACTION: CC Q99766-3; Q03828: EVX2; NbExp=3; IntAct=EBI-13309711, EBI-17280301; CC Q99766-3; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-13309711, EBI-6426443; CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P22027}. CC Mitochondrion inner membrane {ECO:0000250|UniProtKB:P22027}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q99766-1; Sequence=Displayed; CC Name=2; CC IsoId=Q99766-2; Sequence=VSP_040059, VSP_040062; CC Name=3; CC IsoId=Q99766-3; Sequence=VSP_040060, VSP_040061; CC -!- SIMILARITY: Belongs to the ATP synthase subunit s family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U79253; AAB50202.1; -; mRNA. DR EMBL; AY052377; AAL13058.1; -; mRNA. DR EMBL; AK290008; BAF82697.1; -; mRNA. DR EMBL; AL359397; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471078; EAW65718.1; -; Genomic_DNA. DR EMBL; CH471078; EAW65722.1; -; Genomic_DNA. DR EMBL; BC011549; AAH11549.1; -; mRNA. DR RefSeq; NP_001003803.1; NM_001003803.2. [Q99766-1] DR RefSeq; NP_001003805.1; NM_001003805.2. [Q99766-3] DR RefSeq; XP_005267594.1; XM_005267537.3. [Q99766-1] DR RefSeq; XP_011534955.1; XM_011536653.2. DR RefSeq; XP_016876709.1; XM_017021220.1. DR AlphaFoldDB; Q99766; -. DR SMR; Q99766; -. DR BioGRID; 118006; 21. DR IntAct; Q99766; 18. DR STRING; 9606.ENSP00000451583; -. DR iPTMnet; Q99766; -. DR PhosphoSitePlus; Q99766; -. DR SwissPalm; Q99766; -. DR BioMuta; ATP5S; -. DR DMDM; 313104249; -. DR EPD; Q99766; -. DR jPOST; Q99766; -. DR MassIVE; Q99766; -. DR MaxQB; Q99766; -. DR PaxDb; 9606-ENSP00000308334; -. DR PeptideAtlas; Q99766; -. DR ProteomicsDB; 78466; -. [Q99766-1] DR ProteomicsDB; 78467; -. [Q99766-2] DR ProteomicsDB; 78468; -. [Q99766-3] DR Pumba; Q99766; -. DR Antibodypedia; 56666; 161 antibodies from 24 providers. DR DNASU; 27109; -. DR Ensembl; ENST00000245448.11; ENSP00000245448.7; ENSG00000125375.18. [Q99766-3] DR Ensembl; ENST00000311459.12; ENSP00000308334.8; ENSG00000125375.18. [Q99766-1] DR Ensembl; ENST00000426751.7; ENSP00000389246.3; ENSG00000125375.18. [Q99766-2] DR Ensembl; ENST00000554204.7; ENSP00000451583.3; ENSG00000125375.18. [Q99766-1] DR Ensembl; ENST00000554438.6; ENSP00000509859.1; ENSG00000125375.18. [Q99766-1] DR Ensembl; ENST00000554951.6; ENSP00000494641.2; ENSG00000125375.18. [Q99766-1] DR Ensembl; ENST00000557421.7; ENSP00000506374.1; ENSG00000125375.18. [Q99766-1] DR Ensembl; ENST00000672419.1; ENSP00000499920.1; ENSG00000125375.18. [Q99766-3] DR Ensembl; ENST00000672910.1; ENSP00000500502.1; ENSG00000125375.18. [Q99766-3] DR GeneID; 27109; -. DR KEGG; hsa:27109; -. DR MANE-Select; ENST00000557421.7; ENSP00000506374.1; NM_001382507.1; NP_001369436.1. DR UCSC; uc001wxv.4; human. [Q99766-1] DR AGR; HGNC:18799; -. DR CTD; 27109; -. DR DisGeNET; 27109; -. DR GeneCards; DMAC2L; -. DR HGNC; HGNC:18799; DMAC2L. DR HPA; ENSG00000125375; Low tissue specificity. DR MalaCards; DMAC2L; -. DR MIM; 618579; gene. DR neXtProt; NX_Q99766; -. DR OpenTargets; ENSG00000125375; -. DR VEuPathDB; HostDB:ENSG00000125375; -. DR eggNOG; KOG3864; Eukaryota. DR GeneTree; ENSGT00940000156502; -. DR HOGENOM; CLU_1969785_0_0_1; -. DR InParanoid; Q99766; -. DR OMA; IFDMLYV; -. DR OrthoDB; 3663496at2759; -. DR PhylomeDB; Q99766; -. DR TreeFam; TF315274; -. DR PathwayCommons; Q99766; -. DR Reactome; R-HSA-163210; Formation of ATP by chemiosmotic coupling. DR Reactome; R-HSA-8949613; Cristae formation. DR SignaLink; Q99766; -. DR BioGRID-ORCS; 27109; 12 hits in 1149 CRISPR screens. DR ChiTaRS; ATP5S; human. DR GeneWiki; ATP5S; -. DR GenomeRNAi; 27109; -. DR Pharos; Q99766; Tbio. DR PRO; PR:Q99766; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; Q99766; Protein. DR Bgee; ENSG00000125375; Expressed in sperm and 207 other cell types or tissues. DR ExpressionAtlas; Q99766; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome. DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0015078; F:proton transmembrane transporter activity; NAS:UniProtKB. DR GO; GO:0006754; P:ATP biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:1902600; P:proton transmembrane transport; NAS:UniProtKB. DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1. DR InterPro; IPR032675; LRR_dom_sf. DR SUPFAM; SSF52047; RNI-like; 1. DR Genevisible; Q99766; HS. PE 1: Evidence at protein level; KW Alternative splicing; ATP synthesis; CF(0); Direct protein sequencing; KW Hydrogen ion transport; Ion transport; Leucine-rich repeat; Magnesium; KW Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; KW Reference proteome; Repeat; Transit peptide; Transport. FT TRANSIT 1..25 FT /note="Mitochondrion" FT /evidence="ECO:0000250|UniProtKB:P22027" FT CHAIN 26..200 FT /note="ATP synthase subunit s, mitochondrial" FT /id="PRO_0000002538" FT REPEAT 62..87 FT /note="LRR 1" FT /evidence="ECO:0000250|UniProtKB:P22027" FT REPEAT 88..116 FT /note="LRR 2" FT /evidence="ECO:0000250|UniProtKB:P22027" FT REPEAT 117..141 FT /note="LRR 3" FT /evidence="ECO:0000250|UniProtKB:P22027" FT REPEAT 142..173 FT /note="LRR 4" FT /evidence="ECO:0000250|UniProtKB:P22027" FT REGION 1..61 FT /note="N-terminal domain" FT /evidence="ECO:0000250|UniProtKB:P22027" FT BINDING 59 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P22027" FT BINDING 93 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P22027" FT VAR_SEQ 106..121 FT /note="EGLEHVEKIRLCKCHY -> GNYPIVLLIENADDLQ (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9110174" FT /id="VSP_040059" FT VAR_SEQ 107..112 FT /note="GLEHVE -> TSNICC (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_040060" FT VAR_SEQ 113..200 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_040061" FT VAR_SEQ 122..200 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9110174" FT /id="VSP_040062" FT VARIANT 3 FT /note="P -> L (in dbSNP:rs2275592)" FT /evidence="ECO:0000269|PubMed:11744738, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:9110174, ECO:0000269|Ref.5" FT /id="VAR_060296" SQ SEQUENCE 200 AA; 23226 MW; D850F7B6485D0591 CRC64; MMPFGKISQQ LCGVKKLPWS CDSRYFWGWL NAVFNKVDYD RIRDVGPDRA ASEWLLRCGA MVRYHGQERW QKDYNHLPTG PLDKYKIQAI DATDSCIMSI GFDHMEGLEH VEKIRLCKCH YIEDDCLLRL SQLENLQKTI LEMEIISCGN ITDKGIIALR HLRNLKYLLL SDLPGVREKE NLVQAFKTAL PSLELKLQLK //