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ATP synthase subunit delta, mitochondrial (ATP synthase F1 subunit delta) (F-ATPase delta subunit)

 ATPD_RAT                Reviewed;         168 AA.
P35434;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
25-APR-2018, entry version 143.
RecName: Full=ATP synthase subunit delta, mitochondrial {ECO:0000305};
AltName: Full=ATP synthase F1 subunit delta {ECO:0000312|RGD:621372};
AltName: Full=F-ATPase delta subunit;
Flags: Precursor;
Name=Atp5f1d {ECO:0000312|RGD:621372}; Synonyms=Atp5d;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Liver;
Pan W., Pedersen P.L.;
Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
[2]
PROTEIN SEQUENCE OF 23-35.
TISSUE=Heart;
Dunn M.J.;
Submitted (MAR-1996) to UniProtKB.
[3]
PRELIMINARY PROTEIN SEQUENCE OF 23-59.
Godinot C.;
Submitted (FEB-1991) to the PIR data bank.
[4]
PROTEIN SEQUENCE OF 137-165, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
Lubec G., Chen W.-Q., Kang S.U.;
Submitted (JUL-2007) to UniProtKB.
[5]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE ATP
SYNTHASE COMPLEX.
PubMed=17575325; DOI=10.1074/mcp.M700097-MCP200;
Meyer B., Wittig I., Trifilieff E., Karas M., Schaegger H.;
"Identification of two proteins associated with mammalian ATP
synthase.";
Mol. Cell. Proteomics 6:1690-1699(2007).
-!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP
synthase or Complex V) produces ATP from ADP in the presence of a
proton gradient across the membrane which is generated by electron
transport complexes of the respiratory chain. F-type ATPases
consist of two structural domains, F(1) - containing the
extramembraneous catalytic core, and F(0) - containing the
membrane proton channel, linked together by a central stalk and a
peripheral stalk. During catalysis, ATP turnover in the catalytic
domain of F(1) is coupled via a rotary mechanism of the central
stalk subunits to proton translocation. Part of the complex F(1)
domain and of the central stalk which is part of the complex
rotary element. Rotation of the central stalk against the
surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in
three separate catalytic sites on the beta subunits.
-!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
core - and CF(0) - the membrane proton channel. CF(1) has five
subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0)
seems to have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or
A6L). Component of an ATP synthase complex composed of ATP5F1,
ATP5MC1, ATP5F1E, ATP5H, ATP5I, ATP5J, ATP5J2, MT-ATP6, MT-ATP8,
ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5O, ATP5L, USMG5 and MP68.
{ECO:0000269|PubMed:17575325}.
-!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
-!- SIMILARITY: Belongs to the ATPase epsilon chain family.
{ECO:0000305}.
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EMBL; U00926; AAC28872.1; -; mRNA.
PIR; B33160; B33160.
RefSeq; NP_620806.1; NM_139106.1.
UniGene; Rn.3879; -.
ProteinModelPortal; P35434; -.
SMR; P35434; -.
BioGrid; 251461; 1.
CORUM; P35434; -.
IntAct; P35434; 2.
MINT; P35434; -.
STRING; 10116.ENSRNOP00000020670; -.
iPTMnet; P35434; -.
PhosphoSitePlus; P35434; -.
UCD-2DPAGE; P35434; -.
PaxDb; P35434; -.
PRIDE; P35434; -.
GeneID; 245965; -.
KEGG; rno:245965; -.
UCSC; RGD:621372; rat.
CTD; 513; -.
RGD; 621372; Atp5f1d.
eggNOG; KOG1758; Eukaryota.
eggNOG; COG0355; LUCA.
HOGENOM; HOG000216023; -.
HOVERGEN; HBG001856; -.
InParanoid; P35434; -.
KO; K02134; -.
PhylomeDB; P35434; -.
PRO; PR:P35434; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:RGD.
GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic core F(1); IDA:RGD.
GO; GO:0005739; C:mitochondrion; ISO:RGD.
GO; GO:0045259; C:proton-transporting ATP synthase complex; TAS:RGD.
GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IDA:RGD.
GO; GO:0016887; F:ATPase activity; IMP:RGD.
GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; TAS:RGD.
GO; GO:0006754; P:ATP biosynthetic process; TAS:RGD.
GO; GO:0046034; P:ATP metabolic process; IDA:RGD.
GO; GO:0015986; P:ATP synthesis coupled proton transport; TAS:RGD.
CDD; cd12152; F1-ATPase_delta; 1.
Gene3D; 2.60.15.10; -; 1.
HAMAP; MF_00530; ATP_synth_epsil_bac; 1.
InterPro; IPR036794; ATP_F1_dsu/esu_C_sf.
InterPro; IPR001469; ATP_synth_F1_dsu/esu.
InterPro; IPR020546; ATP_synth_F1_dsu/esu_N.
InterPro; IPR036771; ATPsynth_dsu/esu_N.
PANTHER; PTHR13822; PTHR13822; 1.
Pfam; PF02823; ATP-synt_DE_N; 1.
ProDom; PD000944; ATPase_F1-cplx_dsu/esu; 1.
SUPFAM; SSF46604; SSF46604; 1.
SUPFAM; SSF51344; SSF51344; 1.
TIGRFAMs; TIGR01216; ATP_synt_epsi; 1.
1: Evidence at protein level;
Acetylation; ATP synthesis; CF(1); Complete proteome;
Direct protein sequencing; Hydrogen ion transport; Ion transport;
Membrane; Mitochondrion; Mitochondrion inner membrane;
Reference proteome; Transit peptide; Transport.
TRANSIT 1 22 Mitochondrion. {ECO:0000269|Ref.2}.
CHAIN 23 168 ATP synthase subunit delta,
mitochondrial.
/FTId=PRO_0000002664.
MOD_RES 136 136 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q9D3D9}.
MOD_RES 136 136 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q9D3D9}.
MOD_RES 165 165 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q9D3D9}.
MOD_RES 165 165 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q9D3D9}.
CONFLICT 24 24 Q -> E (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 28 28 S -> A (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 31 31 P -> S (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 51 51 D -> N (in Ref. 3; AA sequence).
{ECO:0000305}.
SEQUENCE 168 AA; 17595 MW; C8628F8BF266F849 CRC64;
MLPAALLRHP GLRRLVLQAR TYAQAAASPA PAAGPGQMSF TFASPTQVFF DGANVRQVDV
PTLTGAFGIL ASHVPTLQVL RPGLVMVHAE DGTTTKYFVS SGSVTVNADS SVQLLAEEVV
TLDMLDLGAA RANLEKAQSE LSGAADEAAR AEIQIRIEAN EALVKALE


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