ATPG_RAT
ID ATPG_RAT Reviewed; 273 AA.
AC P35435;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=ATP synthase subunit gamma, mitochondrial {ECO:0000305};
DE AltName: Full=ATP synthase F1 subunit gamma {ECO:0000250|UniProtKB:P36542};
DE AltName: Full=F-ATPase gamma subunit;
GN Name=Atp5f1c {ECO:0000250|UniProtKB:P36542}; Synonyms=Atp5c, Atp5c1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-273.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RA Choi S.H., Thomas P.J., Lee J.E., Pedersen P.L.;
RT "Molecular cloning, expression and characterization of the rat liver
RT mitochondrial ATP synthase gamma subunit.";
RL Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 1-20.
RA Godinot C.;
RL Submitted (FEB-1991) to the PIR data bank.
RN [3]
RP PROTEIN SEQUENCE OF 91-101, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE ATP SYNTHASE
RP COMPLEX.
RX PubMed=17575325; DOI=10.1074/mcp.m700097-mcp200;
RA Meyer B., Wittig I., Trifilieff E., Karas M., Schaegger H.;
RT "Identification of two proteins associated with mammalian ATP synthase.";
RL Mol. Cell. Proteomics 6:1690-1699(2007).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=9736690; DOI=10.1073/pnas.95.19.11065;
RA Bianchet M.A., Hullihen J., Pedersen P.L., Amzel L.M.;
RT "The 2.8-A structure of rat liver F1-ATPase: configuration of a critical
RT intermediate in ATP synthesis/hydrolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:11065-11070(1998).
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
CC F(0) - containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation. Part of the complex
CC F(1) domain and the central stalk which is part of the complex rotary
CC element. The gamma subunit protrudes into the catalytic domain formed
CC of alpha(3)beta(3). Rotation of the central stalk against the
CC surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in
CC three separate catalytic sites on the beta subunits.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a, b and c. Component of an ATP synthase complex composed of
CC ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-
CC ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and
CC ATP5MJ. {ECO:0000269|PubMed:17575325, ECO:0000269|PubMed:9736690}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:9736690}; Peripheral membrane protein
CC {ECO:0000269|PubMed:9736690}; Matrix side
CC {ECO:0000250|UniProtKB:P05631}.
CC -!- SIMILARITY: Belongs to the ATPase gamma chain family. {ECO:0000305}.
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DR EMBL; L19927; AAA41776.1; -; mRNA.
DR PIR; A33160; A33160.
DR PDB; 1MAB; X-ray; 2.80 A; G=5-273.
DR PDB; 2F43; X-ray; 3.00 A; G=1-273.
DR PDBsum; 1MAB; -.
DR PDBsum; 2F43; -.
DR AlphaFoldDB; P35435; -.
DR SMR; P35435; -.
DR BioGRID; 250485; 6.
DR CORUM; P35435; -.
DR IntAct; P35435; 7.
DR MINT; P35435; -.
DR STRING; 10116.ENSRNOP00000049879; -.
DR CarbonylDB; P35435; -.
DR iPTMnet; P35435; -.
DR World-2DPAGE; 0004:P35435; -.
DR jPOST; P35435; -.
DR PaxDb; P35435; -.
DR PRIDE; P35435; -.
DR UCSC; RGD:620011; rat.
DR RGD; 620011; Atp5f1c.
DR eggNOG; KOG1531; Eukaryota.
DR eggNOG; KOG2389; Eukaryota.
DR InParanoid; P35435; -.
DR Reactome; R-RNO-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-RNO-8949613; Cristae formation.
DR EvolutionaryTrace; P35435; -.
DR PRO; PR:P35435; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:RGD.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
DR GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1); IDA:RGD.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IDA:RGD.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0046034; P:ATP metabolic process; IDA:RGD.
DR GO; GO:0071732; P:cellular response to nitric oxide; IEP:RGD.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; ISO:RGD.
DR CDD; cd12151; F1-ATPase_gamma; 1.
DR InterPro; IPR035968; ATP_synth_F1_ATPase_gsu.
DR InterPro; IPR000131; ATP_synth_F1_gsu.
DR InterPro; IPR023632; ATP_synth_F1_gsu_CS.
DR PANTHER; PTHR11693; PTHR11693; 1.
DR Pfam; PF00231; ATP-synt; 1.
DR PRINTS; PR00126; ATPASEGAMMA.
DR SUPFAM; SSF52943; SSF52943; 1.
DR TIGRFAMs; TIGR01146; ATPsyn_F1gamma; 1.
DR PROSITE; PS00153; ATPASE_GAMMA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP synthesis; CF(1); Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Phosphoprotein; Reference proteome;
KW Transport.
FT CHAIN 1..273
FT /note="ATP synthase subunit gamma, mitochondrial"
FT /id="PRO_0000073430"
FT MOD_RES 14
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91VR2"
FT MOD_RES 24
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91VR2"
FT MOD_RES 30
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P36542"
FT MOD_RES 90
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91VR2"
FT MOD_RES 90
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91VR2"
FT MOD_RES 113
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91VR2"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36542"
FT MOD_RES 129
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P36542"
FT MOD_RES 129
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91VR2"
FT MOD_RES 172
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P36542"
FT MOD_RES 245
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91VR2"
FT CONFLICT 4
FT /note="K -> R (in Ref. 1; AAA41776)"
FT /evidence="ECO:0000305"
FT HELIX 6..41
FT /evidence="ECO:0007829|PDB:1MAB"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:1MAB"
FT TURN 81..87
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 212..232
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 234..258
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 261..269
FT /evidence="ECO:0007829|PDB:1MAB"
SQ 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
