ATPD_PICAN
ID ATPD_PICAN Reviewed; 160 AA.
AC C0HK54;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 1.
DT 25-MAY-2022, entry version 9.
DE RecName: Full=ATP synthase subunit delta, mitochondrial {ECO:0000250|UniProtKB:Q12165};
DE AltName: Full=F-ATPase delta subunit {ECO:0000250|UniProtKB:Q12165};
DE Flags: Precursor;
GN Name=ATP16 {ECO:0000250|UniProtKB:Q12165};
OS Pichia angusta (Yeast) (Hansenula polymorpha).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea.
OX NCBI_TaxID=870730 {ECO:0000303|PubMed:25759169};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-29,
RP IDENTIFICATION IN ATP SYNTHASE COMPLEX, FUNCTION OF ATPASE COMPLEX,
RP SUBUNIT, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=A16 / NCYC 2310 {ECO:0000303|PubMed:25759169};
RX PubMed=25759169; DOI=10.1042/bj20150197;
RA Liu S., Charlesworth T.J., Bason J.V., Montgomery M.G., Harbour M.E.,
RA Fearnley I.M., Walker J.E.;
RT "The purification and characterization of ATP synthase complexes from the
RT mitochondria of four fungal species.";
RL Biochem. J. 468:167-175(2015).
RN [2] {ECO:0000305}
RP PARTIAL PROTEIN SEQUENCE.
RC STRAIN=A16 / NCYC 2310 {ECO:0000303|Ref.2};
RA Fearnley I.M.;
RL Submitted (AUG-2016) to UniProtKB.
RN [3] {ECO:0000305}
RP STRUCTURE BY ELECTRON MICROSCOPY (7.0 ANGSTROMS) OF MONOMERIC ATP SYNTHASE
RP COMPLEX IN COMPLEX WITH BOVINE ATPIF1, FUNCTION, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=27791192; DOI=10.1073/pnas.1615902113;
RA Vinothkumar K.R., Montgomery M.G., Liu S., Walker J.E.;
RT "Structure of the mitochondrial ATP synthase from Pichia angusta determined
RT by electron cryo-microscopy.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:12709-12714(2016).
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 (PubMed:25759169). F-type ATP synthases
CC consist of two structural domains, F(1) - containing the
CC extramembraneous catalytic core, and F(0) - containing the membrane
CC proton channel, linked together by a central stalk and a peripheral
CC stalk (PubMed:27791192). During catalysis, ATP synthesis in the
CC catalytic domain of F(1) is coupled via a rotary mechanism of the
CC central stalk subunits to proton translocation (By similarity). Part of
CC the complex F(1) domain and the central stalk which is part of the
CC complex rotary element (By similarity). Rotation of the central stalk
CC against the surrounding alpha/ATP1(3)beta/ATP2(3) subunits leads to
CC hydrolysis of ATP in three separate catalytic sites on the beta/ATP2
CC subunits (By similarity). {ECO:0000250|UniProtKB:Q6C877,
CC ECO:0000269|PubMed:25759169, ECO:0000269|PubMed:27791192}.
CC -!- SUBUNIT: F-type ATP synthases have 2 components, the catalytic core
CC F(1) and the membrane-embedded component F(0), linked together by a
CC central stalk and a peripheral stalk (PubMed:27791192). The central
CC stalk, also called rotor shaft, is often seen as part of F(1)
CC (PubMed:27791192). The peripheral stalk is seen as part of F(0). F(0)
CC contains the membrane channel next to the rotor (PubMed:27791192). F-
CC type ATP synthases form dimers but each monomer functions independently
CC in ATP generation (By similarity). The dimer consists of 18 different
CC polypeptides: ATP1 (subunit alpha, part of F(1), 3 molecules per
CC monomer), ATP2 (subunit beta, part of F(1), 3 molecules per monomer),
CC ATP3 (subunit gamma, part of the central stalk), ATP4 (subunit b, part
CC of the peripheral stalk), ATP5/OSCP (subunit 5/OSCP, part of the
CC peripheral stalk), ATP6 (subunit a, part of the peripheral stalk), ATP7
CC (subunit d, part of the peripheral stalk), ATP8 (subunit 8, part of the
CC peripheral stalk), OLI1 (subunit c, part of the rotor, 10 molecules per
CC monomer), ATP14 (subunit h, part of the peripheral stalk), ATP15
CC (subunit epsilon, part of the central stalk), ATP16 (subunit delta,
CC part of the central stalk), ATP17 (subunit f, part of the peripheral
CC stalk), ATP18 (subunit i/j, part of the peripheral stalk)
CC (PubMed:27791192, PubMed:25759169). Dimer-specific subunits are ATP19
CC (subunit k, at interface between monomers), ATP20 (subunit g, at
CC interface between monomers), TIM11 (subunit e, at interface between
CC monomers) (By similarity). Also contains subunit L (PubMed:25759169).
CC {ECO:0000250|UniProtKB:Q6C877, ECO:0000269|PubMed:25759169,
CC ECO:0000269|PubMed:27791192}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:27791192}; Peripheral membrane protein
CC {ECO:0000305|PubMed:27791192}; Matrix side
CC {ECO:0000305|PubMed:27791192}. Note=The F-type ATP synthase complex is
CC anchored in the mitochondrial inner membrane via the F(0) domain with
CC the F(1) domain and the peripheral stalk extending into the
CC mitochondrial matrix. {ECO:0000305|PubMed:27791192}.
CC -!- MASS SPECTROMETRY: Mass=14161; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:25759169};
CC -!- SIMILARITY: Belongs to the ATPase epsilon chain family. {ECO:0000305}.
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DR AlphaFoldDB; C0HK54; -.
DR SMR; C0HK54; -.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
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; 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 1: Evidence at protein level;
KW ATP synthesis; CF(1); Direct protein sequencing; Hydrogen ion transport;
KW Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Transit peptide; Transport.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25759169"
FT CHAIN 23..160
FT /note="ATP synthase subunit delta, mitochondrial"
FT /evidence="ECO:0000269|Ref.2"
FT /id="PRO_0000445313"
SQ SEQUENCE 160 AA; 16715 MW; 3B602A2C09317707 CRC64;
MFRQSLRSIA RTRTGTIGVR TYAEAVNPDV LKVSLVAPHQ AIFTNKEVSQ VNLPASSGEM
GVLANHVPTV EELAPGVVEV IESSGTASKY FVSGGFASIL PGSKLSISTV EAHPLDAFSS
ENIKSLLAEA QKNASSADET VAAEAAIEIE VLEALQAAVH
