ATP5S_BOVIN
ID ATP5S_BOVIN Reviewed; 200 AA.
AC P22027; Q32L55; Q5S3X8;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 134.
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, ATPW;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16579955; DOI=10.1016/j.abb.2006.02.021;
RA Belogrudov G.I.;
RT "Bovine factor B: cloning, expression, and characterization.";
RL Arch. Biochem. Biophys. 451:68-78(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 26-80.
RC TISSUE=Heart;
RX PubMed=2148527; DOI=10.1016/0014-5793(90)80819-5;
RA Kantham L., Raychowdhury R., Ogata K.K., Javed A., Rice J., Sanadi D.R.;
RT "Amino-terminal amino acid sequence of beef heart mitochondrial coupling
RT factor B.";
RL FEBS Lett. 277:105-108(1990).
RN [4]
RP FUNCTION, ASSOCIATION WITH ATP SYNTHASE, AND SUBCELLULAR LOCATION.
RX PubMed=12361715; DOI=10.1016/s0003-9861(02)00431-9;
RA Belogrudov G.I.;
RT "Factor B is essential for ATP synthesis by mitochondria.";
RL Arch. Biochem. Biophys. 406:271-274(2002).
RN [5] {ECO:0007744|PDB:3DZE, ECO:0007744|PDB:3E2J, ECO:0007744|PDB:3E3Z, ECO:0007744|PDB:3E4G}
RP X-RAY CRYSTALLOGRAPHY (0.96 ANGSTROMS) OF 26-200 OF MUTANT GLU-28,
RP FUNCTION, MAGNESIUM-BINDING SITES, LEUCINE-RICH REPEATS, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=18768789; DOI=10.1073/pnas.0805689105;
RA Lee J.K., Belogrudov G.I., Stroud R.M.;
RT "Crystal structure of bovine mitochondrial factor B at 0.96-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:13379-13384(2008).
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:0000269|PubMed:12361715, ECO:0000269|PubMed:18768789}.
CC -!- SUBUNIT: Homotetramer. Associates with ATP synthase.
CC {ECO:0000269|PubMed:18768789}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12361715}.
CC Mitochondrion inner membrane {ECO:0000305|PubMed:18768789}.
CC -!- SIMILARITY: Belongs to the ATP synthase subunit s family.
CC {ECO:0000305}.
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DR EMBL; AY780292; AAV52866.1; -; mRNA.
DR EMBL; BC109757; AAI09758.1; -; mRNA.
DR PIR; S13005; S13005.
DR RefSeq; NP_001007813.1; NM_001007812.3.
DR RefSeq; XP_010807544.1; XM_010809242.2.
DR PDB; 3DZE; X-ray; 1.15 A; A=26-200.
DR PDB; 3E2J; X-ray; 2.90 A; A/B/C/D=26-200.
DR PDB; 3E3Z; X-ray; 1.70 A; A=26-200.
DR PDB; 3E4G; X-ray; 0.96 A; A=26-200.
DR PDBsum; 3DZE; -.
DR PDBsum; 3E2J; -.
DR PDBsum; 3E3Z; -.
DR PDBsum; 3E4G; -.
DR AlphaFoldDB; P22027; -.
DR SMR; P22027; -.
DR DIP; DIP-46291N; -.
DR STRING; 9913.ENSBTAP00000020228; -.
DR PaxDb; P22027; -.
DR PRIDE; P22027; -.
DR Ensembl; ENSBTAT00000020228; ENSBTAP00000020228; ENSBTAG00000015202.
DR GeneID; 493709; -.
DR KEGG; bta:493709; -.
DR CTD; 27109; -.
DR VEuPathDB; HostDB:ENSBTAG00000015202; -.
DR VGNC; VGNC:54625; DMAC2L.
DR eggNOG; KOG3864; Eukaryota.
DR GeneTree; ENSGT00940000156502; -.
DR HOGENOM; CLU_100746_0_0_1; -.
DR InParanoid; P22027; -.
DR OMA; CAEWIIK; -.
DR OrthoDB; 1395428at2759; -.
DR TreeFam; TF315274; -.
DR EvolutionaryTrace; P22027; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000015202; Expressed in biceps femoris and 107 other tissues.
DR ExpressionAtlas; P22027; baseline and differential.
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 1: Evidence at protein level;
KW 3D-structure; 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:0000269|PubMed:2148527"
FT CHAIN 26..200
FT /note="ATP synthase subunit s, mitochondrial"
FT /id="PRO_0000002537"
FT REPEAT 62..87
FT /note="LRR 1"
FT /evidence="ECO:0000269|PubMed:18768789"
FT REPEAT 88..116
FT /note="LRR 2"
FT /evidence="ECO:0000269|PubMed:18768789"
FT REPEAT 117..141
FT /note="LRR 3"
FT /evidence="ECO:0000269|PubMed:18768789"
FT REPEAT 142..173
FT /note="LRR 4"
FT /evidence="ECO:0000269|PubMed:18768789"
FT REGION 1..61
FT /note="N-terminal domain"
FT /evidence="ECO:0000269|PubMed:18768789"
FT BINDING 59
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:18768789,
FT ECO:0007744|PDB:3E2J"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:18768789,
FT ECO:0007744|PDB:3E2J"
FT VARIANT 26
FT /note="Missing (in one third of the chains)"
FT CONFLICT 58
FT /note="C -> G (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 26..35
FT /evidence="ECO:0007829|PDB:3E4G"
FT HELIX 39..45
FT /evidence="ECO:0007829|PDB:3E4G"
FT HELIX 47..57
FT /evidence="ECO:0007829|PDB:3E4G"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:3E4G"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:3E4G"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:3E4G"
FT HELIX 99..105
FT /evidence="ECO:0007829|PDB:3E4G"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:3E4G"
FT HELIX 124..131
FT /evidence="ECO:0007829|PDB:3E4G"
FT HELIX 134..139
FT /evidence="ECO:0007829|PDB:3E4G"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:3E4G"
FT HELIX 153..158
FT /evidence="ECO:0007829|PDB:3E4G"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:3E4G"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:3E4G"
FT HELIX 179..189
FT /evidence="ECO:0007829|PDB:3E4G"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:3E4G"
SQ SEQUENCE 200 AA; 23293 MW; 2C439BE3835E206D CRC64;
MMLFGKISQQ LCGLKKLPWS RDSRYFWGWL NAVFNKVDHD RIRDVGPDRA ASEWLLRCGA
MVRYHGQQRW QKDYNHLPTG PLDKYKIQAI DATDSCIMSI GFDHMEGLQY VEKIRLCKCH
YIEDGCLERL SQLENLQKSM LEMEIISCGN VTDKGIIALH HFRNLKYLFL SDLPGVKEKE
KIVQAFKTSL PSLELKLDLK
