AT5G2_BOVIN
ID AT5G2_BOVIN Reviewed; 143 AA.
AC P07926; P00839; Q54A29;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 162.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2868890; DOI=10.1002/j.1460-2075.1985.tb04111.x;
RA Gay N.J., Walker J.E.;
RT "Two genes encoding the bovine mitochondrial ATP synthase proteolipid
RT specify precursors with different import sequences and are expressed in a
RT tissue-specific manner.";
RL EMBO J. 4:3519-3524(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2549952; DOI=10.1042/bj2600249;
RA Dyer M.R., Gay N.J., Walker J.E.;
RT "DNA sequences of a bovine gene and of two related pseudogenes for the
RT proteolipid subunit of mitochondrial ATP synthase.";
RL Biochem. J. 260:249-258(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12658628; DOI=10.1002/mrd.10292;
RA Ishiwata H., Katsuma S., Kizaki K., Patel O.V., Nakano H., Takahashi T.,
RA Imai K., Hirasawa A., Shiojima S., Ikawa H., Suzuki Y., Tsujimoto G.,
RA Izaike Y., Todoroki J., Hashizume K.;
RT "Characterization of gene expression profiles in early bovine pregnancy
RT using a custom cDNA microarray.";
RL Mol. Reprod. Dev. 65:9-18(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 69-143.
RC TISSUE=Heart;
RA Sebald W., Hoppe J., Wachter E.;
RT "Amino acid sequence of the ATPase proteolipid from mitochondria,
RT chloroplasts and bacteria (wild type and mutants).";
RL (In) Quagliariello E., Palmieri F., Papa S., Klingenberg M. (eds.);
RL Function and molecular aspects of biomembrane transport, pp.63-74,
RL Elsevier, Amsterdam (1979).
RN [6]
RP PROTEIN SEQUENCE OF 69-78.
RC TISSUE=Heart;
RX PubMed=1827992; DOI=10.1021/bi00236a007;
RA Walker J.E., Lutter R., Dupuis A., Runswick M.J.;
RT "Identification of the subunits of F1F0-ATPase from bovine heart
RT mitochondria.";
RL Biochemistry 30:5369-5378(1991).
RN [7]
RP INVOLVEMENT IN BOVINE CEROID-LIPOFUSCINOSIS.
RX PubMed=1829867; DOI=10.1007/bf00405140;
RA Martinus R.D., Harper P.A., Jolly R.D., Bayliss S.L., Midwinter G.G.,
RA Shaw G.J., Palmer D.N.;
RT "Bovine ceroid-lipofuscinosis (Batten's disease): the major component
RT stored is the DCCD-reactive proteolipid, subunit C, of mitochondrial ATP
RT synthase.";
RL Vet. Res. Commun. 15:85-94(1991).
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). {ECO:0000269|PubMed:1829867}.
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; X05219; CAA28846.1; -; mRNA.
DR EMBL; AB098947; BAC56437.1; -; mRNA.
DR EMBL; BC111613; AAI11614.1; -; mRNA.
DR PIR; S04230; S04230.
DR RefSeq; NP_788786.1; NM_176613.2.
DR RefSeq; XP_005206194.1; XM_005206137.2.
DR RefSeq; XP_005206195.1; XM_005206138.2.
DR PDB; 6Z1R; EM; 3.29 A; K/L/M/N/O/P/Q/R=69-143.
DR PDB; 6Z1U; EM; 3.47 A; K/L/M/N/O/P/Q/R=69-143.
DR PDB; 6ZG7; EM; 3.49 A; K/L/M/N/O/P/Q/R=69-143.
DR PDB; 6ZG8; EM; 3.49 A; K/L/M/N/O/P/Q/R=69-143.
DR PDB; 6ZIK; EM; 3.66 A; K/L/M/N/O/P/Q/R=69-143.
DR PDB; 6ZIT; EM; 3.49 A; K/L/R=69-143.
DR PDB; 6ZQM; EM; 3.29 A; K/L/M/N/O/P/Q/R=69-143.
DR PDB; 6ZQN; EM; 4.00 A; K/L/M/N/O/P/Q/R=69-143.
DR PDB; 7AJB; EM; 9.20 A; AK/AL/AM/AN/AO/AP/AQ/AR/K/L/M/N/O/P/Q/R=69-143.
DR PDB; 7AJC; EM; 11.90 A; AK/AL/AM/AN/AO/AP/AQ/AR/K/L/M/N/O/P/Q/R=69-143.
DR PDB; 7AJD; EM; 9.00 A; AK/AL/AM/AN/AO/AP/AQ/AR/K/L/M/N/O/P/Q/R=69-143.
DR PDB; 7AJE; EM; 9.40 A; AK/AL/AM/AN/AO/AP/AQ/AR/K/L/M/N/O/P/Q/R=69-143.
DR PDB; 7AJF; EM; 8.45 A; AK/AL/AM/AN/AO/AP/AQ/AR/K/L/M/N/O/P/Q/R=69-143.
DR PDB; 7AJG; EM; 10.70 A; AK/AL/AM/AN/AO/AP/AQ/AR/K/L/M/N/O/P/Q/R=69-143.
DR PDB; 7AJH; EM; 9.70 A; AK/AL/AM/AN/AO/AP/AQ/AR/K/L/M/N/O/P/Q/R=69-143.
DR PDB; 7AJI; EM; 11.40 A; AK/AL/AM/AN/AO/AP/AQ/AR/K/L/M/N/O/P/Q/R=69-143.
DR PDB; 7AJJ; EM; 13.10 A; AK/AL/AM/AN/AO/AP/AQ/AR/K/L/M/N/O/P/Q/R=69-143.
DR PDBsum; 6Z1R; -.
DR PDBsum; 6Z1U; -.
DR PDBsum; 6ZG7; -.
DR PDBsum; 6ZG8; -.
DR PDBsum; 6ZIK; -.
DR PDBsum; 6ZIT; -.
DR PDBsum; 6ZQM; -.
DR PDBsum; 6ZQN; -.
DR PDBsum; 7AJB; -.
DR PDBsum; 7AJC; -.
DR PDBsum; 7AJD; -.
DR PDBsum; 7AJE; -.
DR PDBsum; 7AJF; -.
DR PDBsum; 7AJG; -.
DR PDBsum; 7AJH; -.
DR PDBsum; 7AJI; -.
DR PDBsum; 7AJJ; -.
DR AlphaFoldDB; P07926; -.
DR SMR; P07926; -.
DR STRING; 9913.ENSBTAP00000007538; -.
DR PaxDb; P07926; -.
DR PRIDE; P07926; -.
DR GeneID; 337887; -.
DR KEGG; bta:337887; -.
DR CTD; 517; -.
DR eggNOG; KOG3025; Eukaryota.
DR HOGENOM; CLU_116822_1_0_1; -.
DR InParanoid; P07926; -.
DR OrthoDB; 1564365at2759; -.
DR TreeFam; TF300140; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:CAFA.
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 1: Evidence at protein level;
KW 3D-structure; CF(0); Direct protein sequencing; Hydrogen ion transport;
KW Ion transport; Lipid-binding; Membrane; Methylation; Mitochondrion;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..68
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:1827992, ECO:0000269|Ref.5"
FT CHAIN 69..143
FT /note="ATP synthase F(0) complex subunit C2, mitochondrial"
FT /id="PRO_0000002561"
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"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:6ZG7"
FT HELIX 74..82
FT /evidence="ECO:0007829|PDB:6ZG7"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:6ZG7"
FT HELIX 86..106
FT /evidence="ECO:0007829|PDB:6ZG7"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:6ZG7"
FT HELIX 111..140
FT /evidence="ECO:0007829|PDB:6ZG7"
SQ SEQUENCE 143 AA; 15029 MW; F1164485A7FA9292 CRC64;
MYTCAKFVST PSLIRRTSTV LSRSLSAVVV RRPETLTDES HSSLAVVPRP LTTSLTPSRS
FQTSAISRDI DTAAKFIGAG AATVGVAGSG AGIGTVFGSL IIGYARNPSL KQQLFSYAIL
GFALSEAMGL FCLMVAFLIL FAM
