AT5G2_SHEEP
ID AT5G2_SHEEP Reviewed; 143 AA.
AC Q06056;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=ATP synthase F(0) complex subunit C2, mitochondrial {ECO:0000305};
DE AltName: Full=ATP synthase lipid-binding protein;
DE AltName: Full=ATP synthase membrane subunit c locus 2 {ECO:0000250|UniProtKB:Q06055};
DE AltName: Full=ATP synthase proteolipid P2;
DE AltName: Full=ATPase protein 9;
DE AltName: Full=ATPase subunit c;
DE Flags: Precursor;
GN Name=ATP5MC2 {ECO:0000250|UniProtKB:Q06055}; Synonyms=ATP5G2;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8328973; DOI=10.1042/bj2930065;
RA Medd S.M., Walker J.E., Jolly R.D.;
RT "Characterization of the expressed genes for subunit c of mitochondrial ATP
RT synthase in sheep with ceroid lipofuscinosis.";
RL Biochem. J. 293:65-73(1993).
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. A homomeric c-ring of probably 10 subunits is part of the
CC complex rotary element.
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. Interacts with DNAJC30; interaction is direct.
CC {ECO:0000250|UniProtKB:Q06055}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane
CC protein.
CC -!- PTM: Trimethylated by ATPSCKMT at Lys-111. Methylation is required for
CC proper incorporation of the C subunit into the ATP synthase complex and
CC mitochondrial respiration. {ECO:0000250|UniProtKB:Q06055}.
CC -!- DISEASE: Note=This protein is the major protein stored in the storage
CC bodies of animals or humans affected with ceroid lipofuscinosis (Batten
CC disease).
CC -!- MISCELLANEOUS: There are three genes which encode the ATP synthase
CC proteolipid and they specify precursors with different import sequences
CC but identical mature proteins.
CC -!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000305}.
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DR EMBL; X69905; CAA49530.1; -; mRNA.
DR PIR; S34069; S34069.
DR RefSeq; NP_001009468.1; NM_001009468.1.
DR RefSeq; XP_012015298.1; XM_012159908.2.
DR AlphaFoldDB; Q06056; -.
DR SMR; Q06056; -.
DR STRING; 9940.ENSOARP00000017601; -.
DR Ensembl; ENSOART00020028434; ENSOARP00020023569; ENSOARG00020018477.
DR Ensembl; ENSOART00020028541; ENSOARP00020023657; ENSOARG00020018507.
DR GeneID; 443542; -.
DR KEGG; oas:443542; -.
DR CTD; 517; -.
DR eggNOG; KOG3025; Eukaryota.
DR OrthoDB; 1564365at2759; -.
DR Proteomes; UP000002356; Unplaced.
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: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 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..68
FT /note="Mitochondrion"
FT CHAIN 69..143
FT /note="ATP synthase F(0) complex subunit C2, mitochondrial"
FT /id="PRO_0000002565"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 126
FT /note="Reversibly protonated during proton transport"
FT /evidence="ECO:0000250"
FT MOD_RES 111
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q06055"
SQ SEQUENCE 143 AA; 15043 MW; F103A48A47E09292 CRC64;
MYTCAKFVST PSLIRRTSTL LSRSLSAVVV RRPETLTDES HSSLAVVPRP LTTSLTPSRS
FQTSAISRDI DTAAKFIGAG AATVGVAGSG AGIGTVFGSL IIGYARNPSL KQQLFSYAIL
GFALSEAMGL FCLMVAFLIL FAM
