AT5G1_BOVIN
ID AT5G1_BOVIN Reviewed; 136 AA.
AC P32876; P00839; Q3SZC8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 156.
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 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 [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 62-136.
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 [4]
RP PROTEIN SEQUENCE OF 62-71.
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 [5]
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).
RN [6]
RP IDENTIFICATION IN THE ATP SYNTHASE COMPLEX.
RX PubMed=17570365; DOI=10.1016/j.febslet.2007.05.079;
RA Chen R., Runswick M.J., Carroll J., Fearnley I.M., Walker J.E.;
RT "Association of two proteolipids of unknown function with ATP synthase from
RT bovine heart mitochondria.";
RL FEBS Lett. 581:3145-3148(2007).
RN [7]
RP IDENTIFICATION IN THE ATP SYNTHASE COMPLEX.
RX PubMed=25851905; DOI=10.1074/jbc.m115.645283;
RA Lee J., Ding S., Walpole T.B., Holding A.N., Montgomery M.G.,
RA Fearnley I.M., Walker J.E.;
RT "Organization of Subunits in the Membrane Domain of the Bovine F-ATPase
RT Revealed by Covalent Cross-linking.";
RL J. Biol. Chem. 290:13308-13320(2015).
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. Interacts
CC with TMEM70 (homooligomer form); this interaction facilitates the
CC oligomer formation of subunit c/ATP5MC1 (c-ring) and the c-ring
CC membrane insertion and also protects ATP5MC1 against intramitochondrial
CC proteolysis (By similarity). {ECO:0000250|UniProtKB:P05496,
CC ECO:0000269|PubMed:17570365, ECO:0000269|PubMed:25851905}.
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; X05218; CAA28845.1; -; mRNA.
DR EMBL; BC102952; AAI02953.1; -; mRNA.
DR PIR; A24578; LWBOA.
DR RefSeq; NP_788822.1; NM_176649.3.
DR RefSeq; XP_005220574.1; XM_005220517.1.
DR RefSeq; XP_005220575.1; XM_005220518.3.
DR RefSeq; XP_005220576.1; XM_005220519.3.
DR PDB; 2XND; X-ray; 3.50 A; J/K/L/M/N/O/P/Q=63-134.
DR PDB; 5ARA; EM; 6.70 A; J/K/L/M/N/O/P/Q=63-134.
DR PDB; 5ARE; EM; 7.40 A; J/K/L/M/N/O/P/Q=63-134.
DR PDB; 5ARH; EM; 7.20 A; J/K/L/M/N/O/P/Q=63-134.
DR PDB; 5ARI; EM; 7.40 A; J/K/L/M/N/O/P/Q=63-134.
DR PDB; 5FIJ; EM; 7.40 A; J/K/L/M/N/O/P/Q=63-134.
DR PDB; 5FIK; EM; 6.40 A; J/K/L/M/N/O/P/Q=63-134.
DR PDB; 5FIL; EM; 7.10 A; J/K/L/M/N/O/P/Q=63-134.
DR PDB; 6ZBB; EM; 3.61 A; K/L/M/N/O/P/Q/R=62-136.
DR PDB; 6ZIQ; EM; 4.33 A; M/N/O=62-136.
DR PDB; 6ZPO; EM; 4.00 A; K/L/M/N/O/P/Q/R=62-136.
DR PDBsum; 2XND; -.
DR PDBsum; 5ARA; -.
DR PDBsum; 5ARE; -.
DR PDBsum; 5ARH; -.
DR PDBsum; 5ARI; -.
DR PDBsum; 5FIJ; -.
DR PDBsum; 5FIK; -.
DR PDBsum; 5FIL; -.
DR PDBsum; 6ZBB; -.
DR PDBsum; 6ZIQ; -.
DR PDBsum; 6ZPO; -.
DR AlphaFoldDB; P32876; -.
DR SMR; P32876; -.
DR CORUM; P32876; -.
DR DIP; DIP-59387N; -.
DR IntAct; P32876; 5.
DR STRING; 9913.ENSBTAP00000024402; -.
DR PaxDb; P32876; -.
DR Ensembl; ENSBTAT00000024402; ENSBTAP00000024402; ENSBTAG00000018339.
DR GeneID; 338053; -.
DR KEGG; bta:338053; -.
DR CTD; 516; -.
DR VEuPathDB; HostDB:ENSBTAG00000018339; -.
DR VGNC; VGNC:103014; ATP5MC1.
DR eggNOG; KOG3025; Eukaryota.
DR GeneTree; ENSGT00940000159720; -.
DR HOGENOM; CLU_116822_1_0_1; -.
DR InParanoid; P32876; -.
DR OMA; ACHRPRC; -.
DR OrthoDB; 1564365at2759; -.
DR TreeFam; TF300140; -.
DR Reactome; R-BTA-1268020; Mitochondrial protein import.
DR Reactome; R-BTA-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-BTA-8949613; Cristae formation.
DR EvolutionaryTrace; P32876; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000018339; Expressed in cardiac ventricle and 106 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; IDA:UniProtKB.
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..61
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:1827992, ECO:0000269|Ref.3"
FT CHAIN 62..136
FT /note="ATP synthase F(0) complex subunit C1, mitochondrial"
FT /id="PRO_0000002556"
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 TURN 64..73
FT /evidence="ECO:0007829|PDB:2XND"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:2XND"
FT HELIX 80..96
FT /evidence="ECO:0007829|PDB:2XND"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:2XND"
FT HELIX 103..107
FT /evidence="ECO:0007829|PDB:2XND"
FT HELIX 112..131
FT /evidence="ECO:0007829|PDB:2XND"
SQ SEQUENCE 136 AA; 14223 MW; 242199E80C02FA65 CRC64;
MQTTGALLIS PALIRSCTRG LIRPVSASFL SRPEIQSVQP SYSSGPLQVA RREFQTSVVS
RDIDTAAKFI GAGAATVGVA GSGAGIGTVF GSLIIGYARN PSLKQQLFSY AILGFALSEA
MGLFCLMVAF LILFAM
