AT5G1_SHEEP
ID AT5G1_SHEEP Reviewed; 136 AA.
AC P17605;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=ATP synthase F(0) complex subunit C1, mitochondrial {ECO:0000305};
DE AltName: Full=ATP synthase lipid-binding protein;
DE AltName: Full=ATP synthase membrane subunit c locus 1 {ECO:0000250|UniProtKB:P05496};
DE AltName: Full=ATP synthase proteolipid P1;
DE AltName: Full=ATPase protein 9;
DE AltName: Full=ATPase subunit c;
DE Flags: Precursor;
GN Name=ATP5MC1 {ECO:0000250|UniProtKB:P05496}; Synonyms=ATP5G1;
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).
RN [2]
RP PROTEIN SEQUENCE OF 62-136.
RX PubMed=2141977; DOI=10.1042/bj2680751;
RA Fearnley I.M., Walker J.E., Martinus R.D., Jolly R.D., Kirkland K.B.,
RA Shaw G.J., Palmer D.N.;
RT "The sequence of the major protein stored in ovine ceroid lipofuscinosis is
RT identical with that of the dicyclohexylcarbodiimide-reactive proteolipid of
RT mitochondrial ATP synthase.";
RL Biochem. J. 268:751-758(1990).
RN [3]
RP PROTEIN SEQUENCE OF 62-101.
RX PubMed=2522438; DOI=10.1016/s0021-9258(18)83610-9;
RA Palmer D.N., Martinus R.D., Cooper S.M., Midwinter G.G., Reid J.C.,
RA Jolly R.D.;
RT "Ovine ceroid lipofuscinosis. The major lipopigment protein and the lipid-
RT binding subunit of mitochondrial ATP synthase have the same NH2-terminal
RT sequence.";
RL J. Biol. Chem. 264:5736-5740(1989).
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: Homooligomer (By similarity). F-type ATPases have 2
CC components, CF(1) - the catalytic core - and CF(0) - the membrane
CC proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1),
CC delta(1), epsilon(1). CF(0) has three main subunits: a, b and c.
CC Component of an ATP synthase complex composed of ATP5PB, ATP5MC1,
CC ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A,
CC ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and ATP5MJ (By
CC similarity). Interacts with TMEM70 (homooligomer form); this
CC interaction facilitates the oligomer formation of subunit c/ATP5MC1 (c-
CC ring) and the c-ring membrane insertion and also protects ATP5MC1
CC against intramitochondrial proteolysis (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P05496}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane
CC protein.
CC -!- PTM: Trimethylated by ATPSCKMT at Lys-104. Methylation is required for
CC proper incorporation of the C subunit into the ATP synthase complex and
CC mitochondrial respiration. {ECO:0000250|UniProtKB:P05496}.
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; X69904; CAA49529.1; -; mRNA.
DR PIR; S34068; S31769.
DR RefSeq; NP_001009396.1; NM_001009396.1.
DR RefSeq; XP_012040502.1; XM_012185112.2.
DR PDB; 6TT7; EM; 3.50 A; 1/2/3/4/5/6/7/8=1-136.
DR PDB; 6ZA9; EM; 3.76 A; 1/2/3/4/5/6/7/8=1-136.
DR PDBsum; 6TT7; -.
DR PDBsum; 6ZA9; -.
DR AlphaFoldDB; P17605; -.
DR SMR; P17605; -.
DR STRING; 9940.ENSOARP00000007127; -.
DR Ensembl; ENSOART00000007234; ENSOARP00000007127; ENSOARG00000006653.
DR Ensembl; ENSOART00020035109; ENSOARP00020029005; ENSOARG00020022590.
DR GeneID; 443410; -.
DR KEGG; oas:443410; -.
DR CTD; 516; -.
DR eggNOG; KOG3025; Eukaryota.
DR HOGENOM; CLU_116822_1_0_1; -.
DR OMA; CMGFCIL; -.
DR OrthoDB; 1564365at2759; -.
DR Proteomes; UP000002356; Chromosome 11.
DR Bgee; ENSOARG00000006653; Expressed in heart right ventricle and 53 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; ISS:UniProtKB.
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 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..61
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2141977,
FT ECO:0000269|PubMed:2522438"
FT CHAIN 62..136
FT /note="ATP synthase F(0) complex subunit C1, mitochondrial"
FT /id="PRO_0000002560"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 119
FT /note="Reversibly protonated during proton transport"
FT /evidence="ECO:0000250"
FT MOD_RES 104
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05496"
FT HELIX 63..74
FT /evidence="ECO:0007829|PDB:6TT7"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:6TT7"
FT HELIX 79..97
FT /evidence="ECO:0007829|PDB:6TT7"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:6TT7"
FT HELIX 104..133
FT /evidence="ECO:0007829|PDB:6TT7"
SQ SEQUENCE 136 AA; 14192 MW; 3135C9FD0DA84BCE CRC64;
MQTTGALLIS PALIRSCTRG LIRPVSASFL SRPEIPSVQP SYSSGPLQVA RREFQTSVVS
RDIDTAAKFI GAGAATVGVA GSGAGIGTVF GSLIIGYARN PSLKQQLFSY AILGFALSEA
MGLFCLMVAF LILFAM
