ATPD_RAT
ID ATPD_RAT Reviewed; 168 AA.
AC P35434;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=ATP synthase subunit delta, mitochondrial {ECO:0000305};
DE AltName: Full=ATP synthase F1 subunit delta {ECO:0000312|RGD:621372};
DE AltName: Full=F-ATPase delta subunit;
DE Flags: Precursor;
GN Name=Atp5f1d {ECO:0000312|RGD:621372}; Synonyms=Atp5d;
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 [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RA Pan W., Pedersen P.L.;
RL Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 23-35.
RC TISSUE=Heart;
RA Dunn M.J.;
RL Submitted (MAR-1996) to UniProtKB.
RN [3]
RP PRELIMINARY PROTEIN SEQUENCE OF 23-59.
RA Godinot C.;
RL Submitted (FEB-1991) to the PIR data bank.
RN [4]
RP PROTEIN SEQUENCE OF 137-165, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
RA Lubec G., Chen W.-Q., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE ATP SYNTHASE
RP COMPLEX.
RX PubMed=17575325; DOI=10.1074/mcp.m700097-mcp200;
RA Meyer B., Wittig I., Trifilieff E., Karas M., Schaegger H.;
RT "Identification of two proteins associated with mammalian ATP synthase.";
RL Mol. Cell. Proteomics 6:1690-1699(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:17575325}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC -!- SIMILARITY: Belongs to the ATPase epsilon chain family. {ECO:0000305}.
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DR EMBL; U00926; AAC28872.1; -; mRNA.
DR PIR; B33160; B33160.
DR RefSeq; NP_620806.1; NM_139106.1.
DR AlphaFoldDB; P35434; -.
DR SMR; P35434; -.
DR BioGRID; 251461; 2.
DR CORUM; P35434; -.
DR IntAct; P35434; 3.
DR MINT; P35434; -.
DR STRING; 10116.ENSRNOP00000020670; -.
DR iPTMnet; P35434; -.
DR PhosphoSitePlus; P35434; -.
DR UCD-2DPAGE; P35434; -.
DR jPOST; P35434; -.
DR PaxDb; P35434; -.
DR PRIDE; P35434; -.
DR GeneID; 245965; -.
DR KEGG; rno:245965; -.
DR UCSC; RGD:621372; rat.
DR CTD; 513; -.
DR RGD; 621372; Atp5f1d.
DR eggNOG; KOG1758; Eukaryota.
DR InParanoid; P35434; -.
DR OrthoDB; 1286602at2759; -.
DR PhylomeDB; P35434; -.
DR Reactome; R-RNO-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-RNO-8949613; Cristae formation.
DR PRO; PR:P35434; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:RGD.
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); IDA:RGD.
DR GO; GO:0045259; C:proton-transporting ATP synthase complex; TAS:RGD.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; TAS:RGD.
DR GO; GO:0009060; P:aerobic respiration; ISS:UniProtKB.
DR GO; GO:0006754; P:ATP biosynthetic process; TAS:RGD.
DR GO; GO:0046034; P:ATP metabolic process; IDA:RGD.
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; ISO:RGD.
DR GO; GO:1904638; P:response to resveratrol; IEP:RGD.
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 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|Ref.2"
FT CHAIN 23..168
FT /note="ATP synthase subunit delta, mitochondrial"
FT /id="PRO_0000002664"
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 CONFLICT 24
FT /note="Q -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="S -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="P -> S (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="D -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 168 AA; 17595 MW; C8628F8BF266F849 CRC64;
MLPAALLRHP GLRRLVLQAR TYAQAAASPA PAAGPGQMSF TFASPTQVFF DGANVRQVDV
PTLTGAFGIL ASHVPTLQVL RPGLVMVHAE DGTTTKYFVS SGSVTVNADS SVQLLAEEVV
TLDMLDLGAA RANLEKAQSE LSGAADEAAR AEIQIRIEAN EALVKALE
