ID ATP5S_MOUSE Reviewed; 200 AA. AC Q9CRA7; Q8R2M3; DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 24-JAN-2024, entry version 146. DE RecName: Full=ATP synthase subunit s, mitochondrial {ECO:0000305}; DE AltName: Full=ATP synthase-coupling factor B; DE AltName: Full=Distal membrane arm assembly complex 2-like protein {ECO:0000250|UniProtKB:Q99766}; DE AltName: Full=Mitochondrial ATP synthase regulatory component factor B; DE Flags: Precursor; GN Name=Dmac2l; Synonyms=Atp5s {ECO:0000312|MGI:MGI:1915305}, Atpw; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryo, and Tongue; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). 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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P22027}. CC Mitochondrion inner membrane {ECO:0000250|UniProtKB:P22027}. 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; AK003725; BAB22960.1; -; mRNA. DR EMBL; AK009141; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC027442; AAH27442.1; -; mRNA. DR CCDS; CCDS25954.1; -. DR RefSeq; NP_080812.1; NM_026536.1. DR RefSeq; XP_011242467.1; XM_011244165.1. DR AlphaFoldDB; Q9CRA7; -. DR SMR; Q9CRA7; -. DR BioGRID; 212633; 7. DR STRING; 10090.ENSMUSP00000152430; -. DR iPTMnet; Q9CRA7; -. DR PhosphoSitePlus; Q9CRA7; -. DR SwissPalm; Q9CRA7; -. DR EPD; Q9CRA7; -. DR MaxQB; Q9CRA7; -. DR PaxDb; 10090-ENSMUSP00000021372; -. DR PeptideAtlas; Q9CRA7; -. DR ProteomicsDB; 277269; -. DR Pumba; Q9CRA7; -. DR Antibodypedia; 56666; 161 antibodies from 24 providers. DR DNASU; 68055; -. DR Ensembl; ENSMUST00000021372.6; ENSMUSP00000021372.6; ENSMUSG00000054894.7. DR Ensembl; ENSMUST00000220916.2; ENSMUSP00000152430.2; ENSMUSG00000054894.7. DR GeneID; 68055; -. DR KEGG; mmu:68055; -. DR UCSC; uc007nsr.1; mouse. DR AGR; MGI:1915305; -. DR CTD; 27109; -. DR MGI; MGI:1915305; Dmac2l. DR VEuPathDB; HostDB:ENSMUSG00000054894; -. DR eggNOG; KOG3864; Eukaryota. DR GeneTree; ENSGT00940000156502; -. DR HOGENOM; CLU_100746_0_0_1; -. DR InParanoid; Q9CRA7; -. DR OMA; IFDMLYV; -. DR OrthoDB; 3663496at2759; -. DR PhylomeDB; Q9CRA7; -. DR TreeFam; TF315274; -. DR Reactome; R-MMU-163210; Formation of ATP by chemiosmotic coupling. DR Reactome; R-MMU-8949613; Cristae formation. DR BioGRID-ORCS; 68055; 1 hit in 77 CRISPR screens. DR ChiTaRS; Dmac2l; mouse. DR PRO; PR:Q9CRA7; -. DR Proteomes; UP000000589; Chromosome 12. DR RNAct; Q9CRA7; Protein. DR Bgee; ENSMUSG00000054894; Expressed in interventricular septum and 242 other cell types or tissues. DR ExpressionAtlas; Q9CRA7; baseline and differential. DR Genevisible; Q9CRA7; MM. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; HDA:MGI. 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:0006754; P:ATP biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:1902600; P:proton transmembrane transport; IEA:UniProtKB-KW. DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1. DR InterPro; IPR032675; LRR_dom_sf. DR SUPFAM; SSF52047; RNI-like; 1. PE 1: Evidence at protein level; KW ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; KW Leucine-rich repeat; Magnesium; Membrane; Metal-binding; Mitochondrion; KW Mitochondrion inner membrane; Reference proteome; Repeat; Transit peptide; KW 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_0000002539" 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 CONFLICT 156 FT /note="V -> I (in Ref. 2; AAH27442)" FT /evidence="ECO:0000305" SQ SEQUENCE 200 AA; 23275 MW; 0878BD50B281AA2F CRC64; MMMFGKISRQ LCSLKKIPWS CDSRYFWEWL NTVFNKVDYE RLRDVGPDRA ASEWLLRCGA KVRYCGHQKW LHDYNTLPGS SIDRYKIQAI DATDSCIMDI GLDHMVGLEH VEKITLCKCH YIEDNCLQRL SQLENLRKSL LELEIIACGN VTDNGVIALR HFRNLKYLFL SDLPGVKDKE YLAQVFKTAL PSLELKLNLK //