ID   ATP5S_RAT               Reviewed;         200 AA.
AC   Q5XIM4;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
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 {ECO:0000312|RGD:1359208};
GN   Synonyms=Atp5s {ECO:0000312|RGD:1359208};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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).
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; BC083655; AAH83655.1; -; mRNA.
DR   RefSeq; NP_001007750.1; NM_001007749.1.
DR   RefSeq; XP_006240236.1; XM_006240174.3.
DR   RefSeq; XP_006240237.1; XM_006240175.3.
DR   RefSeq; XP_006240238.1; XM_006240176.3.
DR   AlphaFoldDB; Q5XIM4; -.
DR   SMR; Q5XIM4; -.
DR   STRING; 10116.ENSRNOP00000006509; -.
DR   iPTMnet; Q5XIM4; -.
DR   PhosphoSitePlus; Q5XIM4; -.
DR   PaxDb; Q5XIM4; -.
DR   PRIDE; Q5XIM4; -.
DR   Ensembl; ENSRNOT00000006509; ENSRNOP00000006509; ENSRNOG00000004893.
DR   GeneID; 362749; -.
DR   KEGG; rno:362749; -.
DR   UCSC; RGD:1359208; rat.
DR   CTD; 27109; -.
DR   RGD; 1359208; Dmac2l.
DR   eggNOG; KOG3864; Eukaryota.
DR   GeneTree; ENSGT00940000156502; -.
DR   HOGENOM; CLU_100746_0_0_1; -.
DR   InParanoid; Q5XIM4; -.
DR   OMA; CAEWIIK; -.
DR   OrthoDB; 1395428at2759; -.
DR   PhylomeDB; Q5XIM4; -.
DR   TreeFam; TF315274; -.
DR   Reactome; R-RNO-163210; Formation of ATP by chemiosmotic coupling.
DR   Reactome; R-RNO-8949613; Cristae formation.
DR   PRO; PR:Q5XIM4; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   Bgee; ENSRNOG00000004893; Expressed in heart and 20 other tissues.
DR   Genevisible; Q5XIM4; RN.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript 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_0000002541"
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"
SQ   SEQUENCE   200 AA;  23324 MW;  8EC195A78F6B3978 CRC64;
     MMMFGKISRQ LFSLKKIPWS CDSRYFWEWL NTVFNKVDYE RIKDVGPDRA ASEWLLRCGA
     KVRYCGHQKW LQDYNKLPGG SVDRYKIQAI DATDSCIMDI GFDHLVGLEH VERITLCRCH
     YIEDNCLQRL SQLENLRKSL LELEIIACGN VTDNGVIALR HFKNLKYLFL SDLPGIKDKE
     YLAEVFTKAL PSLELKLNLK