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ATP synthase F(0) complex subunit C2, mitochondrial (ATP synthase lipid-binding protein) (ATP synthase membrane subunit c locus 2) (ATP synthase proteolipid P2) (ATPase protein 9) (ATPase subunit c)

 AT5G2_BOVIN             Reviewed;         143 AA.
P07926; P00839; Q54A29;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
12-SEP-2018, entry version 143.
RecName: Full=ATP synthase F(0) complex subunit C2, mitochondrial {ECO:0000305};
AltName: Full=ATP synthase lipid-binding protein;
AltName: Full=ATP synthase membrane subunit c locus 2 {ECO:0000250|UniProtKB:Q06055};
AltName: Full=ATP synthase proteolipid P2;
AltName: Full=ATPase protein 9;
AltName: Full=ATPase subunit c;
Flags: Precursor;
Name=ATP5MC2 {ECO:0000250|UniProtKB:Q06055}; Synonyms=ATP5G2;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2868890;
Gay N.J., Walker J.E.;
"Two genes encoding the bovine mitochondrial ATP synthase proteolipid
specify precursors with different import sequences and are expressed
in a tissue-specific manner.";
EMBO J. 4:3519-3524(1985).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2549952; DOI=10.1042/bj2600249;
Dyer M.R., Gay N.J., Walker J.E.;
"DNA sequences of a bovine gene and of two related pseudogenes for the
proteolipid subunit of mitochondrial ATP synthase.";
Biochem. J. 260:249-258(1989).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=12658628; DOI=10.1002/mrd.10292;
Ishiwata H., Katsuma S., Kizaki K., Patel O.V., Nakano H.,
Takahashi T., Imai K., Hirasawa A., Shiojima S., Ikawa H., Suzuki Y.,
Tsujimoto G., Izaike Y., Todoroki J., Hashizume K.;
"Characterization of gene expression profiles in early bovine
pregnancy using a custom cDNA microarray.";
Mol. Reprod. Dev. 65:9-18(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Testis;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
[5]
PROTEIN SEQUENCE OF 69-143.
TISSUE=Heart;
Sebald W., Hoppe J., Wachter E.;
"Amino acid sequence of the ATPase proteolipid from mitochondria,
chloroplasts and bacteria (wild type and mutants).";
(In) Quagliariello E., Palmieri F., Papa S., Klingenberg M. (eds.);
Function and molecular aspects of biomembrane transport, pp.63-74,
Elsevier, Amsterdam (1979).
[6]
PROTEIN SEQUENCE OF 69-78.
TISSUE=Heart;
PubMed=1827992; DOI=10.1021/bi00236a007;
Walker J.E., Lutter R., Dupuis A., Runswick M.J.;
"Identification of the subunits of F1F0-ATPase from bovine heart
mitochondria.";
Biochemistry 30:5369-5378(1991).
[7]
INVOLVEMENT IN BOVINE CEROID-LIPOFUSCINOSIS.
PubMed=1829867; DOI=10.1007/BF00405140;
Martinus R.D., Harper P.A., Jolly R.D., Bayliss S.L., Midwinter G.G.,
Shaw G.J., Palmer D.N.;
"Bovine ceroid-lipofuscinosis (Batten's disease): the major component
stored is the DCCD-reactive proteolipid, subunit C, of mitochondrial
ATP synthase.";
Vet. Res. Commun. 15:85-94(1991).
-!- 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.
-!- 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 ATP synthase
proteolipid and they specify precursors with different import
sequences but identical mature proteins.
-!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000305}.
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EMBL; X05219; CAA28846.1; -; mRNA.
EMBL; AB098947; BAC56437.1; -; mRNA.
EMBL; BC111613; AAI11614.1; -; mRNA.
PIR; S04230; S04230.
RefSeq; NP_788786.1; NM_176613.2.
RefSeq; XP_005206194.1; XM_005206137.2.
RefSeq; XP_005206195.1; XM_005206138.2.
UniGene; Bt.64851; -.
ProteinModelPortal; P07926; -.
SMR; P07926; -.
STRING; 9913.ENSBTAP00000007538; -.
PaxDb; P07926; -.
Ensembl; ENSBTAT00000007538; ENSBTAP00000007538; ENSBTAG00000005735.
GeneID; 337887; -.
KEGG; bta:337887; -.
CTD; 517; -.
VGNC; VGNC:55848; ATP5MC2.
eggNOG; KOG3025; Eukaryota.
eggNOG; COG0636; LUCA.
GeneTree; ENSGT00390000006210; -.
HOGENOM; HOG000235246; -.
HOVERGEN; HBG050605; -.
InParanoid; P07926; -.
KO; K02128; -.
OMA; HPLKMYT; -.
OrthoDB; EOG091G13J1; -.
TreeFam; TF300140; -.
Reactome; R-BTA-163210; Formation of ATP by chemiosmotic coupling.
Reactome; R-BTA-8949613; Cristae formation.
Proteomes; UP000009136; Chromosome 5.
Bgee; ENSBTAG00000005735; Expressed in 9 organ(s), highest expression level in heart.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:CAFA.
GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
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:0015986; P:ATP synthesis coupled proton transport; IBA:GO_Central.
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; Direct protein sequencing;
Hydrogen ion transport; Ion transport; Lipid-binding; Membrane;
Mitochondrion; Reference proteome; Transit peptide; Transmembrane;
Transmembrane helix; Transport.
TRANSIT 1 68 Mitochondrion.
{ECO:0000269|PubMed:1827992,
ECO:0000269|Ref.5}.
CHAIN 69 143 ATP synthase F(0) complex subunit C2,
mitochondrial.
/FTId=PRO_0000002561.
TRANSMEM 84 104 Helical. {ECO:0000255}.
TRANSMEM 119 139 Helical. {ECO:0000255}.
SITE 126 126 Reversibly protonated during proton
transport. {ECO:0000250}.
SEQUENCE 143 AA; 15029 MW; F1164485A7FA9292 CRC64;
MYTCAKFVST PSLIRRTSTV LSRSLSAVVV RRPETLTDES HSSLAVVPRP LTTSLTPSRS
FQTSAISRDI DTAAKFIGAG AATVGVAGSG AGIGTVFGSL IIGYARNPSL KQQLFSYAIL
GFALSEAMGL FCLMVAFLIL FAM


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