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ATP5S_MOUSE
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   03-AUG-2022, entry version 138.
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}.
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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.ENSMUSP00000021372; -.
DR   iPTMnet; Q9CRA7; -.
DR   PhosphoSitePlus; Q9CRA7; -.
DR   EPD; Q9CRA7; -.
DR   MaxQB; Q9CRA7; -.
DR   PaxDb; Q9CRA7; -.
DR   PeptideAtlas; Q9CRA7; -.
DR   PRIDE; Q9CRA7; -.
DR   ProteomicsDB; 277269; -.
DR   Antibodypedia; 56666; 150 antibodies from 24 providers.
DR   DNASU; 68055; -.
DR   Ensembl; ENSMUST00000021372; ENSMUSP00000021372; ENSMUSG00000054894.
DR   Ensembl; ENSMUST00000220916; ENSMUSP00000152430; ENSMUSG00000054894.
DR   GeneID; 68055; -.
DR   KEGG; mmu:68055; -.
DR   UCSC; uc007nsr.1; mouse.
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; CAEWIIK; -.
DR   OrthoDB; 1395428at2759; -.
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 72 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 240 other 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:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR026063; ATP5S/ATP5SL.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   PANTHER; PTHR13382:SF10; PTHR13382:SF10; 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
 
 
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