ATP9_PETHY
ID ATP9_PETHY Reviewed; 74 AA.
AC P60118; P05497; P05498;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2003, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=ATP synthase subunit 9, mitochondrial;
DE AltName: Full=Lipid-binding protein;
GN Name=ATP9;
OS Petunia hybrida (Petunia).
OG Mitochondrion.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX NCBI_TaxID=4102;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Line 3704;
RX PubMed=2877439; DOI=10.1093/nar/14.20.7995;
RA Young E.G., Hanson M.R., Dierks P.M.;
RT "Sequence and transcription analysis of the Petunia mitochondrial gene for
RT the ATP synthase proteolipid subunit.";
RL Nucleic Acids Res. 14:7995-8006(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Line 3704;
RX PubMed=17186617; DOI=10.1007/bf00329831;
RA Rothenberg M., Hanson M.R.;
RT "Different transcript abundance of two divergent ATP synthase subunit 9
RT genes in the mitochondrial genome of Petunia hybrida.";
RL Mol. Gen. Genet. 209:21-27(1987).
RN [3]
RP RNA EDITING OF TERMINATOR CODON.
RC STRAIN=Line 3704;
RX PubMed=1709830; DOI=10.1007/bf00362089;
RA Wintz H., Hanson M.R.;
RT "A termination codon is created by RNA editing in the petunia atp9
RT transcript.";
RL Curr. Genet. 19:61-64(1991).
CC -!- FUNCTION: This protein is one of the chains of the nonenzymatic
CC membrane component (F0) of mitochondrial ATPase.
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) has three main
CC subunits: a, b and c.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- RNA EDITING: Modified_positions=7 {ECO:0000269|PubMed:1709830}, 15
CC {ECO:0000269|PubMed:1709830}, 17 {ECO:0000269|PubMed:1709830}, 28
CC {ECO:0000269|PubMed:1709830}, 31 {ECO:0000269|PubMed:1709830}, 59
CC {ECO:0000269|PubMed:1709830}, 61 {ECO:0000269|PubMed:1709830}, 64
CC {ECO:0000269|PubMed:1709830}, 75 {ECO:0000269|PubMed:1709830}; Note=The
CC stop codon at position 75 is created by RNA editing.;
CC -!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000305}.
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DR EMBL; X04504; CAA28189.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X05808; CAA29251.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X05807; CAA29250.1; ALT_SEQ; Genomic_DNA.
DR PIR; S00271; LWPJA.
DR AlphaFoldDB; P60118; -.
DR SMR; P60118; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro.
DR Gene3D; 1.20.20.10; -; 1.
DR HAMAP; MF_01396; ATP_synth_c_bact; 1.
DR InterPro; IPR000454; ATP_synth_F0_csu.
DR InterPro; IPR020537; ATP_synth_F0_csu_DDCD_BS.
DR InterPro; IPR038662; ATP_synth_F0_csu_sf.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR PANTHER; PTHR10031; PTHR10031; 1.
DR Pfam; PF00137; ATP-synt_C; 1.
DR PRINTS; PR00124; ATPASEC.
DR SUPFAM; SSF81333; SSF81333; 1.
DR PROSITE; PS00605; ATPASE_C; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; CF(0); Hydrogen ion transport; Ion transport; Lipid-binding;
KW Membrane; Mitochondrion; Nucleotide-binding; RNA editing; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..74
FT /note="ATP synthase subunit 9, mitochondrial"
FT /id="PRO_0000112220"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 57
FT /note="Reversibly protonated during proton transport"
FT /evidence="ECO:0000250"
SQ SEQUENCE 74 AA; 7563 MW; 6593295037555E82 CRC64;
MLEGAKLMGA GAATIALAGA AIGIGNVFSS LIHSVARNPS LAKQLFGYAI LGFALTEAIA
LFALMMAFLI SFVF
