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ATP synthase F(0) complex subunit C1, mitochondrial (ATP synthase lipid-binding protein) (ATP synthase membrane subunit c locus 1) (ATP synthase proteolipid P1) (ATPase protein 9) (ATPase subunit c)

 AT5G1_RAT               Reviewed;         136 AA.
Q06645;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
10-OCT-2018, entry version 131.
RecName: Full=ATP synthase F(0) complex subunit C1, mitochondrial {ECO:0000305};
AltName: Full=ATP synthase lipid-binding protein;
AltName: Full=ATP synthase membrane subunit c locus 1 {ECO:0000312|RGD:61933};
AltName: Full=ATP synthase proteolipid P1;
AltName: Full=ATPase protein 9;
AltName: Full=ATPase subunit c;
Flags: Precursor;
Name=Atp5mc1 {ECO:0000312|RGD:61933}; Synonyms=Atp5g1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8448208; DOI=10.1016/0167-4781(93)90219-4;
Higuti T., Kuroiwa K., Kawamura Y., Morimoto K., Tsujita H.;
"Molecular cloning and sequence of cDNAs for the import precursors of
oligomycin sensitivity conferring protein, ATPase inhibitor protein,
and subunit c of H(+)-ATP synthase in rat mitochondria.";
Biochim. Biophys. Acta 1172:311-314(1993).
[2]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE ATP
SYNTHASE COMPLEX.
PubMed=17575325; DOI=10.1074/mcp.M700097-MCP200;
Meyer B., Wittig I., Trifilieff E., Karas M., Schaegger H.;
"Identification of two proteins associated with mammalian ATP
synthase.";
Mol. Cell. Proteomics 6:1690-1699(2007).
-!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP
synthase or Complex V) produces ATP from ADP in the presence of a
proton gradient across the membrane which is generated by electron
transport complexes of the respiratory chain. F-type ATPases
consist of two structural domains, F(1) - containing the
extramembraneous catalytic core and F(0) - containing the membrane
proton channel, linked together by a central stalk and a
peripheral stalk. During catalysis, ATP synthesis in the catalytic
domain of F(1) is coupled via a rotary mechanism of the central
stalk subunits to proton translocation. Part of the complex F(0)
domain. A homomeric c-ring of probably 10 subunits is part of the
complex rotary element.
-!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
core - and CF(0) - the membrane proton channel. CF(1) has five
subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0)
has three main subunits: a, b and c. Component of an ATP synthase
complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME,
ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D,
ATP5F1C, ATP5PO, ATP5MG, ATP5MD and MP68.
{ECO:0000269|PubMed:17575325}.
-!- SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane
protein.
-!- DISEASE: Note=This protein is the major protein stored in the
storage bodies of animals or humans affected with ceroid
lipofuscinosis (Batten disease).
-!- MISCELLANEOUS: There are three genes which encode the
mitochondrial ATP synthase proteolipid and they specify precursors
with different import sequences. They are expressed in a tissue-
specific manner.
-!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000305}.
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EMBL; D13123; BAA02425.1; -; mRNA.
PIR; JS0740; JS0740.
RefSeq; NP_059007.1; NM_017311.1.
RefSeq; XP_006247250.1; XM_006247188.3.
RefSeq; XP_006247251.1; XM_006247189.1.
UniGene; Rn.3357; -.
ProteinModelPortal; Q06645; -.
SMR; Q06645; -.
CORUM; Q06645; -.
STRING; 10116.ENSRNOP00000009815; -.
PaxDb; Q06645; -.
PRIDE; Q06645; -.
Ensembl; ENSRNOT00000009815; ENSRNOP00000009815; ENSRNOG00000007235.
GeneID; 29754; -.
KEGG; rno:29754; -.
UCSC; RGD:61933; rat.
CTD; 516; -.
RGD; 61933; Atp5mc1.
eggNOG; KOG3025; Eukaryota.
eggNOG; COG0636; LUCA.
GeneTree; ENSGT00390000006210; -.
HOGENOM; HOG000235246; -.
HOVERGEN; HBG050605; -.
InParanoid; Q06645; -.
KO; K02128; -.
OMA; IRCCTRD; -.
OrthoDB; EOG091G13J1; -.
PhylomeDB; Q06645; -.
TreeFam; TF300140; -.
Reactome; R-RNO-1268020; Mitochondrial protein import.
Reactome; R-RNO-163210; Formation of ATP by chemiosmotic coupling.
Reactome; R-RNO-8949613; Cristae formation.
PRO; PR:Q06645; -.
Proteomes; UP000002494; Chromosome 10.
Bgee; ENSRNOG00000007235; Expressed in 10 organ(s), highest expression level in heart.
Genevisible; Q06645; RN.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IDA:RGD.
GO; GO:0005739; C:mitochondrion; NAS:RGD.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IBA:GO_Central.
GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
GO; GO:0046034; P:ATP metabolic process; IDA:RGD.
GO; GO:0015986; P:ATP synthesis coupled proton transport; IBA:GO_Central.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
Gene3D; 1.20.20.10; -; 1.
HAMAP; MF_01396; ATP_synth_c_bact; 1.
InterPro; IPR000454; ATP_synth_F0_csu.
InterPro; IPR020537; ATP_synth_F0_csu_DDCD_BS.
InterPro; IPR038662; ATP_synth_F0_csu_sf.
InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
InterPro; IPR035921; F/V-ATP_Csub_sf.
PANTHER; PTHR10031; PTHR10031; 1.
Pfam; PF00137; ATP-synt_C; 1.
PRINTS; PR00124; ATPASEC.
SUPFAM; SSF81333; SSF81333; 1.
PROSITE; PS00605; ATPASE_C; 1.
1: Evidence at protein level;
CF(0); Complete proteome; Hydrogen ion transport; Ion transport;
Lipid-binding; Membrane; Mitochondrion; Reference proteome;
Transit peptide; Transmembrane; Transmembrane helix; Transport.
TRANSIT 1 61 Mitochondrion.
CHAIN 62 136 ATP synthase F(0) complex subunit C1,
mitochondrial.
/FTId=PRO_0000002559.
TRANSMEM 77 97 Helical. {ECO:0000255}.
TRANSMEM 112 132 Helical. {ECO:0000255}.
SITE 119 119 Reversibly protonated during proton
transport. {ECO:0000250}.
SEQUENCE 136 AA; 14244 MW; 91060591516D6AF6 CRC64;
MQTTKALLIS PVLIRSCTRG LIRPVSASLL SRPEAPSKKP SCCSSPLQVA RREFQTSVIS
RDIDTAAKFI GAGAATVGVA GSGAGIGTVF GSLIIGYARN PSLKQQLFSY AILGFALSEA
MGLFCLMVAF LILFAM


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