ATP5S_PONAB
ID ATP5S_PONAB Reviewed; 200 AA.
AC Q5R9E6; Q5NVG1;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=ATP synthase subunit s, mitochondrial;
DE AltName: Full=ATP synthase-coupling factor B;
DE Short=FB;
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;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex, and Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR859443; CAH91614.1; -; mRNA.
DR EMBL; CR926075; CAI29702.1; -; mRNA.
DR RefSeq; NP_001127111.1; NM_001133639.1.
DR AlphaFoldDB; Q5R9E6; -.
DR SMR; Q5R9E6; -.
DR STRING; 9601.ENSPPYP00000006591; -.
DR GeneID; 100174151; -.
DR KEGG; pon:100174151; -.
DR CTD; 27109; -.
DR eggNOG; KOG3864; Eukaryota.
DR InParanoid; Q5R9E6; -.
DR Proteomes; UP000001595; Unplaced.
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_0000002540"
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 43
FT /note="R -> G (in Ref. 1; CAI29702)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="K -> E (in Ref. 1; CAI29702)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 200 AA; 23199 MW; E967261C533A39DA CRC64;
MMLFGKISQQ LCGVKKLPWS CDSRYFWGWL NAVFNKVDYD RIRDVGPDRA ASEWLLRCGA
MVRYHGQERW QKDYNHLPTG PLDKYKIQAI DATDSCIMSI GFDHMEGLEH VEKIRLCKCH
YIEDDCLLRL SQLENLQKTI LEMEIISCGN ITDKGIIALL HLRNLKYLLL SDLPGVREKE
NLVQAFKTAL PSLELKLQLK