AT5G_CAEEL
ID AT5G_CAEEL Reviewed; 116 AA.
AC Q9BKS0; P90799;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=ATP synthase c subunit {ECO:0000303|PubMed:8920929};
DE AltName: Full=ATP synthase lipid-binding protein, mitochondrial {ECO:0000305};
DE AltName: Full=ATPase protein 9 {ECO:0000305};
DE AltName: Full=ATPase subunit c {ECO:0000305};
DE Flags: Precursor;
GN ORFNames=Y82E9BR.3 {ECO:0000312|WormBase:Y82E9BR.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000312|EMBL:BAA13165.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:BAA13165.1};
RX PubMed=8920929; DOI=10.1006/bbrc.1996.1676;
RA Kawano T., Takuwa K., Nakajima T.;
RT "Molecular cloning of a cDNA for the glutamate transporter of the nematode
RT Caenorhabditis elegans.";
RL Biochem. Biophys. Res. Commun. 228:415-420(1996).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAA21841.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:BAA21841.1};
RA Kawano T.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=17223323; DOI=10.1016/j.mod.2006.11.004;
RA Kawasaki I., Hanazawa M., Gengyo-Ando K., Mitani S., Maruyama I., Iino Y.;
RT "ASB-1, a germline-specific isoform of mitochondrial ATP synthase b
RT subunit, is required to maintain the rate of germline development in
RT Caenorhabditis elegans.";
RL Mech. Dev. 124:237-251(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 F(0)
CC - containing the membrane proton channel, linked together by a central
CC stalk and a peripheral stalk. 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. Part of the complex
CC F(0) domain. Forms an homomeric c-ring of several subunits which is
CC part of the complex rotary complex (Probable). {ECO:0000305}.
CC -!- SUBUNIT: Subunit of the F-type ATPase which has 2 components, CF(1)
CC - the catalytic core - and CF(0) - the membrane proton channel.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000250|UniProtKB:Q06645}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q06645}.
CC -!- PTM: Trimethylated by ATPSCKMT at Lys-84. Methylation may be required
CC for proper incorporation of the C subunit into the ATP synthase complex
CC and mitochondrial respiration. {ECO:0000250|UniProtKB:P05496}.
CC -!- DISRUPTION PHENOTYPE: 76% embryonic lethal, 24% larval arrest.
CC {ECO:0000269|PubMed:17223323}.
CC -!- MISCELLANEOUS: Derived from a bicistronic mRNA produced by trans-
CC splicing that also produces excitatory amino acid transporter (glt-1).
CC -!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13165.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA13165.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA21841.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA21841.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D86740; BAA13165.1; ALT_FRAME; mRNA.
DR EMBL; D86741; BAA21841.1; ALT_FRAME; mRNA.
DR EMBL; BX284603; CCD73035.1; -; Genomic_DNA.
DR RefSeq; NP_001022966.1; NM_001027795.4.
DR AlphaFoldDB; Q9BKS0; -.
DR SMR; Q9BKS0; -.
DR BioGRID; 40557; 3.
DR DIP; DIP-25373N; -.
DR STRING; 6239.Y82E9BR.3.2; -.
DR EPD; Q9BKS0; -.
DR PaxDb; Q9BKS0; -.
DR PeptideAtlas; Q9BKS0; -.
DR EnsemblMetazoa; Y82E9BR.3.1; Y82E9BR.3.1; WBGene00022336.
DR EnsemblMetazoa; Y82E9BR.3.2; Y82E9BR.3.2; WBGene00022336.
DR GeneID; 175299; -.
DR UCSC; Y82E9BR.3.1; c. elegans.
DR CTD; 175299; -.
DR WormBase; Y82E9BR.3; CE27044; WBGene00022336; -.
DR eggNOG; KOG3025; Eukaryota.
DR GeneTree; ENSGT00940000176138; -.
DR HOGENOM; CLU_116822_2_0_1; -.
DR InParanoid; Q9BKS0; -.
DR OMA; ACHRPRC; -.
DR OrthoDB; 1564365at2759; -.
DR PhylomeDB; Q9BKS0; -.
DR Reactome; R-CEL-1268020; Mitochondrial protein import.
DR Reactome; R-CEL-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-CEL-8949613; Cristae formation.
DR PRO; PR:Q9BKS0; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00022336; Expressed in larva and 4 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
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; IBA:GO_Central.
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 3: Inferred from homology;
KW CF(0); Hydrogen ion transport; Ion transport; Lipid-binding; Membrane;
KW Methylation; Mitochondrion; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 25..116
FT /note="ATP synthase c subunit"
FT /id="PRO_0000399030"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 99
FT /note="Reversibly protonated during proton transport"
FT /evidence="ECO:0000250|UniProtKB:P00845"
FT MOD_RES 84
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05496"
FT CONFLICT 7..8
FT /note="AL -> FS (in Ref. 1; BAA13165 and 2; BAA21841)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 116 AA; 12108 MW; 857C762174A71F6D CRC64;
MYCQRLALPL TRSLLASRAP LALRMENAVA ARMISTTVAR KDIDSAAKYI GAGAATVGVA
GSGAGIGNVF GALVIGYARN PSLKQQLFSY AILGFALSEA MGLFCLTMGF MILFAL
