ATPD_BOVIN
ID ATPD_BOVIN Reviewed; 168 AA.
AC P05630; A6H7D8;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=ATP synthase subunit delta, mitochondrial {ECO:0000305};
DE AltName: Full=ATP synthase F1 subunit delta {ECO:0000250|UniProtKB:P30049};
DE AltName: Full=F-ATPase delta subunit;
DE Flags: Precursor;
GN Name=ATP5F1D {ECO:0000250|UniProtKB:P30049}; Synonyms=ATP5D;
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].
RC TISSUE=Heart muscle;
RX PubMed=2138455; DOI=10.1042/bj2660421;
RA Runswick M.J., Medd S.M., Walker J.E.;
RT "The delta-subunit of ATP synthase from bovine heart mitochondria.
RT Complementary DNA sequence of its import precursor cloned with the aid of
RT the polymerase chain reaction.";
RL Biochem. J. 266:421-426(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 23-168.
RX PubMed=2864455; DOI=10.1016/0022-2836(85)90313-4;
RA Walker J.E., Fearnley I.M., Gay N.J., Gibson B.W., Northrop F.D.,
RA Powell S.J., Runswick M.J., Saraste M., Tybulewicz V.L.J.;
RT "Primary structure and subunit stoichiometry of F1-ATPase from bovine
RT mitochondria.";
RL J. Mol. Biol. 184:677-701(1985).
RN [4]
RP PROTEIN SEQUENCE OF 23-31.
RC TISSUE=Heart;
RX PubMed=1827992; DOI=10.1021/bi00236a007;
RA Walker J.E., Lutter R., Dupuis A., Runswick M.J.;
RT "Identification of the subunits of F1F0-ATPase from bovine heart
RT mitochondria.";
RL Biochemistry 30:5369-5378(1991).
RN [5]
RP IDENTIFICATION IN THE ATP SYNTHASE COMPLEX.
RX PubMed=17570365; DOI=10.1016/j.febslet.2007.05.079;
RA Chen R., Runswick M.J., Carroll J., Fearnley I.M., Walker J.E.;
RT "Association of two proteolipids of unknown function with ATP synthase from
RT bovine heart mitochondria.";
RL FEBS Lett. 581:3145-3148(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE ATP SYNTHASE
RP COMPLEX.
RX PubMed=25851905; DOI=10.1074/jbc.m115.645283;
RA Lee J., Ding S., Walpole T.B., Holding A.N., Montgomery M.G.,
RA Fearnley I.M., Walker J.E.;
RT "Organization of Subunits in the Membrane Domain of the Bovine F-ATPase
RT Revealed by Covalent Cross-linking.";
RL J. Biol. Chem. 290:13308-13320(2015).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=8065448; DOI=10.1038/370621a0;
RA Abrahams J.P., Leslie A.G.W., Lutter R., Walker J.E.;
RT "Structure at 2.8-A resolution of F1-ATPase from bovine heart
RT mitochondria.";
RL Nature 370:621-628(1994).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 23-168 IN COMPLEX WITH ATPIF1;
RP ATP5F1A; ATP5F1B; ATP5F1C AND ATP5F1E.
RX PubMed=17895376; DOI=10.1073/pnas.0707326104;
RA Gledhill J.R., Montgomery M.G., Leslie A.G., Walker J.E.;
RT "How the regulatory protein, IF(1), inhibits F(1)-ATPase from bovine
RT mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:15671-15676(2007).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC Complex V) produces ATP from ADP in the presence of a proton gradient
CC across the membrane which is generated by electron transport complexes
CC of the respiratory chain. F-type ATPases consist of two structural
CC domains, F(1) - containing the extramembraneous catalytic core, and
CC F(0) - containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP turnover in
CC the catalytic domain of F(1) is coupled via a rotary mechanism of the
CC central stalk subunits to proton translocation. Part of the complex
CC F(1) domain and of the central stalk which is part of the complex
CC rotary element. Rotation of the central stalk against the surrounding
CC alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate
CC catalytic sites on the beta subunits. {ECO:0000250|UniProtKB:P30049}.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) seems to have
CC nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). Component of an
CC ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD,
CC ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D,
CC ATP5F1C, ATP5PO, ATP5MG, ATP5MK and ATP5MJ.
CC {ECO:0000269|PubMed:17570365, ECO:0000269|PubMed:17895376,
CC ECO:0000269|PubMed:25851905}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC -!- SIMILARITY: Belongs to the ATPase epsilon chain family. {ECO:0000305}.
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DR EMBL; X17019; CAA34885.1; -; mRNA.
DR EMBL; BC146208; AAI46209.1; -; mRNA.
DR PIR; S09202; PWBOD.
DR RefSeq; NP_788843.1; NM_176670.2.
DR PDB; 1E79; X-ray; 2.40 A; H=23-168.
DR PDB; 1H8E; X-ray; 2.00 A; H=23-168.
DR PDB; 2CK3; X-ray; 1.90 A; H=23-168.
DR PDB; 2JDI; X-ray; 1.90 A; H=23-168.
DR PDB; 2V7Q; X-ray; 2.10 A; H=23-168.
DR PDB; 2W6H; X-ray; 5.00 A; H=1-168.
DR PDB; 2W6I; X-ray; 4.00 A; H=1-168.
DR PDB; 2W6J; X-ray; 3.84 A; H=1-168.
DR PDB; 2WSS; X-ray; 3.20 A; H/Q=23-168.
DR PDB; 2XND; X-ray; 3.50 A; H=37-167.
DR PDB; 4ASU; X-ray; 2.60 A; H=23-168.
DR PDB; 4YXW; X-ray; 3.10 A; H=23-168.
DR PDB; 5ARA; EM; 6.70 A; H=23-168.
DR PDB; 5ARE; EM; 7.40 A; H=23-168.
DR PDB; 5ARH; EM; 7.20 A; H=23-168.
DR PDB; 5ARI; EM; 7.40 A; H=23-168.
DR PDB; 5FIJ; EM; 7.40 A; H=23-168.
DR PDB; 5FIK; EM; 6.40 A; H=23-168.
DR PDB; 5FIL; EM; 7.10 A; H=23-168.
DR PDB; 6YY0; EM; 3.23 A; H=23-168.
DR PDB; 6Z1R; EM; 3.29 A; H=23-168.
DR PDB; 6Z1U; EM; 3.47 A; H=23-168.
DR PDB; 6ZG7; EM; 3.49 A; H=23-168.
DR PDB; 6ZG8; EM; 3.49 A; H=23-168.
DR PDB; 6ZIK; EM; 3.66 A; H=23-168.
DR PDB; 6ZPO; EM; 4.00 A; H=23-168.
DR PDB; 6ZQM; EM; 3.29 A; H=23-168.
DR PDB; 6ZQN; EM; 4.00 A; H=23-168.
DR PDB; 7AJB; EM; 9.20 A; AH/H=23-168.
DR PDB; 7AJC; EM; 11.90 A; AH/H=23-168.
DR PDB; 7AJD; EM; 9.00 A; AH/H=23-168.
DR PDB; 7AJE; EM; 9.40 A; AH/H=23-168.
DR PDB; 7AJF; EM; 8.45 A; AH/H=23-168.
DR PDB; 7AJG; EM; 10.70 A; AH/H=23-168.
DR PDB; 7AJH; EM; 9.70 A; AH/H=23-168.
DR PDB; 7AJI; EM; 11.40 A; AH/H=23-168.
DR PDB; 7AJJ; EM; 13.10 A; AH/H=23-168.
DR PDBsum; 1E79; -.
DR PDBsum; 1H8E; -.
DR PDBsum; 2CK3; -.
DR PDBsum; 2JDI; -.
DR PDBsum; 2V7Q; -.
DR PDBsum; 2W6H; -.
DR PDBsum; 2W6I; -.
DR PDBsum; 2W6J; -.
DR PDBsum; 2WSS; -.
DR PDBsum; 2XND; -.
DR PDBsum; 4ASU; -.
DR PDBsum; 4YXW; -.
DR PDBsum; 5ARA; -.
DR PDBsum; 5ARE; -.
DR PDBsum; 5ARH; -.
DR PDBsum; 5ARI; -.
DR PDBsum; 5FIJ; -.
DR PDBsum; 5FIK; -.
DR PDBsum; 5FIL; -.
DR PDBsum; 6YY0; -.
DR PDBsum; 6Z1R; -.
DR PDBsum; 6Z1U; -.
DR PDBsum; 6ZG7; -.
DR PDBsum; 6ZG8; -.
DR PDBsum; 6ZIK; -.
DR PDBsum; 6ZPO; -.
DR PDBsum; 6ZQM; -.
DR PDBsum; 6ZQN; -.
DR PDBsum; 7AJB; -.
DR PDBsum; 7AJC; -.
DR PDBsum; 7AJD; -.
DR PDBsum; 7AJE; -.
DR PDBsum; 7AJF; -.
DR PDBsum; 7AJG; -.
DR PDBsum; 7AJH; -.
DR PDBsum; 7AJI; -.
DR PDBsum; 7AJJ; -.
DR AlphaFoldDB; P05630; -.
DR SMR; P05630; -.
DR CORUM; P05630; -.
DR DIP; DIP-39022N; -.
DR IntAct; P05630; 5.
DR MINT; P05630; -.
DR STRING; 9913.ENSBTAP00000000721; -.
DR BindingDB; P05630; -.
DR ChEMBL; CHEMBL612444; -.
DR PaxDb; P05630; -.
DR PeptideAtlas; P05630; -.
DR PRIDE; P05630; -.
DR Ensembl; ENSBTAT00000000721; ENSBTAP00000000721; ENSBTAG00000000550.
DR GeneID; 338081; -.
DR KEGG; bta:338081; -.
DR CTD; 513; -.
DR VEuPathDB; HostDB:ENSBTAG00000000550; -.
DR VGNC; VGNC:26302; ATP5F1D.
DR eggNOG; KOG1758; Eukaryota.
DR GeneTree; ENSGT00390000017576; -.
DR HOGENOM; CLU_084338_0_1_1; -.
DR InParanoid; P05630; -.
DR OMA; TLPHQTI; -.
DR OrthoDB; 1438381at2759; -.
DR TreeFam; TF313029; -.
DR Reactome; R-BTA-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-BTA-8949613; Cristae formation.
DR EvolutionaryTrace; P05630; -.
DR PRO; PR:P05630; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000000550; Expressed in laryngeal cartilage and 107 other tissues.
DR GO; GO:0005740; C:mitochondrial envelope; IDA:MGI.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
DR GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1); IBA:GO_Central.
DR GO; GO:0045259; C:proton-transporting ATP synthase complex; IDA:MGI.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IDA:MGI.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:Ensembl.
DR GO; GO:0009060; P:aerobic respiration; ISS:UniProtKB.
DR GO; GO:0033615; P:mitochondrial proton-transporting ATP synthase complex assembly; ISS:UniProtKB.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IEA:Ensembl.
DR GO; GO:1902600; P:proton transmembrane transport; IDA:MGI.
DR CDD; cd12152; F1-ATPase_delta; 1.
DR Gene3D; 2.60.15.10; -; 1.
DR HAMAP; MF_00530; ATP_synth_epsil_bac; 1.
DR InterPro; IPR036794; ATP_F1_dsu/esu_C_sf.
DR InterPro; IPR001469; ATP_synth_F1_dsu/esu.
DR InterPro; IPR020546; ATP_synth_F1_dsu/esu_N.
DR InterPro; IPR036771; ATPsynth_dsu/esu_N.
DR PANTHER; PTHR13822; PTHR13822; 1.
DR Pfam; PF02823; ATP-synt_DE_N; 1.
DR SUPFAM; SSF46604; SSF46604; 1.
DR SUPFAM; SSF51344; SSF51344; 1.
DR TIGRFAMs; TIGR01216; ATP_synt_epsi; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP synthesis; CF(1); Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW Transport.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:1827992,
FT ECO:0000269|PubMed:2864455"
FT CHAIN 23..168
FT /note="ATP synthase subunit delta, mitochondrial"
FT /id="PRO_0000002660"
FT MOD_RES 136
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9D3D9"
FT MOD_RES 136
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9D3D9"
FT MOD_RES 165
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9D3D9"
FT MOD_RES 165
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9D3D9"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:6YY0"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:6YY0"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:6YY0"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:6ZG7"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:6YY0"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:6YY0"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:6YY0"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:6YY0"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:6YY0"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:6YY0"
FT STRAND 112..118
FT /evidence="ECO:0007829|PDB:6YY0"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:6YY0"
FT HELIX 128..142
FT /evidence="ECO:0007829|PDB:6YY0"
FT HELIX 147..167
FT /evidence="ECO:0007829|PDB:6YY0"
SQ SEQUENCE 168 AA; 17612 MW; 7C47BBAD5A151608 CRC64;
MLPSALLRRP GLGRLVRQVR LYAEAAAAQA PAAGPGQMSF TFASPTQVFF NSANVRQVDV
PTQTGAFGIL AAHVPTLQVL RPGLVVVHAE DGTTSKYFVS SGSVTVNADS SVQLLAEEAV
TLDMLDLGAA KANLEKAQSE LLGAADEATR AEIQIRIEAN EALVKALE
