ID   ATPD_PIG                Reviewed;          80 AA.
AC   Q95312;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 107.
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; Fragment;
GN   Name=ATP5F1D {ECO:0000250|UniProtKB:P30049}; Synonyms=ATP5D;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Small intestine;
RA   Winteroe A.K., Fredholm M., Davies W.;
RT   "Evaluation and characterization of a porcine small intestine cDNA
RT   library.";
RL   Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC   -!- SIMILARITY: Belongs to the ATPase epsilon chain family. {ECO:0000305}.
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DR   EMBL; Z81163; CAB03549.1; -; mRNA.
DR   STRING; 9823.ENSSSCP00000014280; -.
DR   PaxDb; Q95312; -.
DR   eggNOG; KOG1758; Eukaryota.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; ISS:UniProtKB.
DR   GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1); IBA:GO_Central.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
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   Gene3D; 2.60.15.10; -; 1.
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; SSF51344; SSF51344; 1.
PE   2: Evidence at transcript level;
KW   ATP synthesis; CF(1); Hydrogen ion transport; Ion transport; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Transit peptide; Transport.
FT   TRANSIT         1..22
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..>80
FT                   /note="ATP synthase subunit delta, mitochondrial"
FT                   /id="PRO_0000002663"
FT   NON_TER         80
SQ   SEQUENCE   80 AA;  8302 MW;  F887D08E810D5A75 CRC64;
     MLPATLLRXS GLGRVVRQAR AYXEAAAAPX SAAGPGXMSF TFASPTQVFF NGANVRQVDV
     PTQTGAFGIL ASHVPTLQVL