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ATP synthase subunit gamma, mitochondrial (ATP synthase F1 subunit gamma) (F-ATPase gamma subunit)

 ATPG_RAT                Reviewed;         273 AA.
P35435;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 2.
23-MAY-2018, entry version 144.
RecName: Full=ATP synthase subunit gamma, mitochondrial {ECO:0000305};
AltName: Full=ATP synthase F1 subunit gamma {ECO:0000250|UniProtKB:P36542};
AltName: Full=F-ATPase gamma subunit;
Name=Atp5f1c {ECO:0000250|UniProtKB:P36542}; Synonyms=Atp5c, Atp5c1;
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] OF 4-273.
STRAIN=Sprague-Dawley; TISSUE=Liver;
Choi S.H., Thomas P.J., Lee J.E., Pedersen P.L.;
"Molecular cloning, expression and characterization of the rat liver
mitochondrial ATP synthase gamma subunit.";
Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
[2]
PROTEIN SEQUENCE OF 1-20.
Godinot C.;
Submitted (FEB-1991) to the PIR data bank.
[3]
PROTEIN SEQUENCE OF 91-101, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (JUL-2007) to UniProtKB.
[4]
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).
[5]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), SUBCELLULAR LOCATION, AND
SUBUNIT.
PubMed=9736690; DOI=10.1073/pnas.95.19.11065;
Bianchet M.A., Hullihen J., Pedersen P.L., Amzel L.M.;
"The 2.8-A structure of rat liver F1-ATPase: configuration of a
critical intermediate in ATP synthesis/hydrolysis.";
Proc. Natl. Acad. Sci. U.S.A. 95:11065-11070(1998).
-!- 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(1)
domain and the central stalk which is part of the complex rotary
element. The gamma subunit protrudes into the catalytic domain
formed of alpha(3)beta(3). Rotation of the central stalk against
the surrounding alpha(3)beta(3) subunits leads to hydrolysis of
ATP in three separate catalytic sites on the beta subunits.
-!- 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 ATP5F1, ATP5MC1, ATP5F1E, ATP5H, ATP5I, ATP5J,
ATP5J2, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C,
ATP5O, ATP5L, USMG5 and MP68. {ECO:0000269|PubMed:17575325,
ECO:0000269|PubMed:9736690}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000269|PubMed:9736690}; Peripheral membrane protein
{ECO:0000269|PubMed:9736690}; Matrix side
{ECO:0000250|UniProtKB:P05631}.
-!- SIMILARITY: Belongs to the ATPase gamma chain family.
{ECO:0000305}.
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EMBL; L19927; AAA41776.1; -; mRNA.
PIR; A33160; A33160.
UniGene; Rn.63959; -.
PDB; 1MAB; X-ray; 2.80 A; G=5-273.
PDB; 2F43; X-ray; 3.00 A; G=1-273.
PDBsum; 1MAB; -.
PDBsum; 2F43; -.
ProteinModelPortal; P35435; -.
SMR; P35435; -.
BioGrid; 250485; 1.
CORUM; P35435; -.
IntAct; P35435; 5.
MINT; P35435; -.
STRING; 10116.ENSRNOP00000049879; -.
CarbonylDB; P35435; -.
iPTMnet; P35435; -.
PhosphoSitePlus; P35435; -.
World-2DPAGE; 0004:P35435; -.
PaxDb; P35435; -.
PRIDE; P35435; -.
UCSC; RGD:620011; rat.
RGD; 620011; Atp5c1.
eggNOG; KOG1531; Eukaryota.
eggNOG; KOG2389; Eukaryota.
eggNOG; COG0224; LUCA.
HOVERGEN; HBG000933; -.
InParanoid; P35435; -.
EvolutionaryTrace; P35435; -.
PRO; PR:P35435; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005740; C:mitochondrial envelope; NAS:RGD.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:RGD.
GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic core F(1); IDA:RGD.
GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IDA:RGD.
GO; GO:0016887; F:ATPase activity; IMP:RGD.
GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
GO; GO:0046034; P:ATP metabolic process; IDA:RGD.
GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
GO; GO:0006119; P:oxidative phosphorylation; NAS:RGD.
CDD; cd12151; F1-ATPase_gamma; 1.
InterPro; IPR035968; ATP_synth_F1_ATPase_gsu.
InterPro; IPR000131; ATP_synth_F1_gsu.
InterPro; IPR023632; ATP_synth_F1_gsu_CS.
Pfam; PF00231; ATP-synt; 1.
PRINTS; PR00126; ATPASEGAMMA.
SUPFAM; SSF52943; SSF52943; 1.
TIGRFAMs; TIGR01146; ATPsyn_F1gamma; 1.
PROSITE; PS00153; ATPASE_GAMMA; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP synthesis; CF(1); Complete proteome;
Direct protein sequencing; Hydrogen ion transport; Ion transport;
Membrane; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
Reference proteome; Transport.
CHAIN 1 273 ATP synthase subunit gamma,
mitochondrial.
/FTId=PRO_0000073430.
MOD_RES 14 14 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q91VR2}.
MOD_RES 24 24 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q91VR2}.
MOD_RES 30 30 N6-acetyllysine.
{ECO:0000250|UniProtKB:P36542}.
MOD_RES 90 90 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q91VR2}.
MOD_RES 90 90 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q91VR2}.
MOD_RES 113 113 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q91VR2}.
MOD_RES 121 121 Phosphoserine.
{ECO:0000250|UniProtKB:P36542}.
MOD_RES 129 129 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P36542}.
MOD_RES 129 129 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q91VR2}.
MOD_RES 172 172 N6-acetyllysine.
{ECO:0000250|UniProtKB:P36542}.
MOD_RES 245 245 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q91VR2}.
CONFLICT 4 4 K -> R (in Ref. 1; AAA41776).
{ECO:0000305}.
HELIX 6 41 {ECO:0000244|PDB:1MAB}.
TURN 43 46 {ECO:0000244|PDB:1MAB}.
TURN 81 87 {ECO:0000244|PDB:1MAB}.
HELIX 212 232 {ECO:0000244|PDB:1MAB}.
HELIX 234 258 {ECO:0000244|PDB:1MAB}.
HELIX 261 269 {ECO:0000244|PDB:1MAB}.
SEQUENCE 273 AA; 30191 MW; BD02D3F7F7583916 CRC64;
ATLKDITRRL KSIKNIQKIT KSMKMVAAAK YARAERELKP ARVYGTGSLA LYEKAEIKGP
EDKKKHLIIG VSSDRGLCGA IHSSVAKQMK NDMAALTAAG KEVMIVGIGE KIKSILYRTH
SDQFLVSFKD VGRKPPTFGD ASVIALELLN SGYEFDEGSI IFNQFKSVIS YKTEEKPIFS
FSTVVAAENM SIYDDIDADV LQNYQEYNLA NIIYYSLKES TTSEQSARMT AMDNASKNAS
DMIDKLTLTF NRTRQAVITK ELIEIISGAA ALD


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