ATPG_PONAB
ID ATPG_PONAB Reviewed; 297 AA.
AC Q5RBS9;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
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;
DE Flags: Precursor;
GN Name=ATP5F1C {ECO:0000250|UniProtKB:P36542}; Synonyms=ATP5C1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250|UniProtKB:P05631}.
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 (By similarity). {ECO:0000250|UniProtKB:P05631}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P05631}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P05631}; Matrix side
CC {ECO:0000250|UniProtKB:P05631}.
CC -!- SIMILARITY: Belongs to the ATPase gamma chain family. {ECO:0000305}.
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DR EMBL; CR858554; CAH90781.1; -; mRNA.
DR AlphaFoldDB; Q5RBS9; -.
DR SMR; Q5RBS9; -.
DR STRING; 9601.ENSPPYP00000002405; -.
DR Ensembl; ENSPPYT00000054561; ENSPPYP00000028266; ENSPPYG00000002076.
DR eggNOG; KOG1531; Eukaryota.
DR GeneTree; ENSGT00390000006837; -.
DR HOGENOM; CLU_050669_4_0_1; -.
DR InParanoid; Q5RBS9; -.
DR OMA; MQITSAM; -.
DR Proteomes; UP000001595; Chromosome 10.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; ISS:UniProtKB.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
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 2: Evidence at transcript level;
KW Acetylation; ATP synthesis; CF(1); Hydrogen ion transport; Ion transport;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 26..297
FT /note="ATP synthase subunit gamma, mitochondrial"
FT /id="PRO_0000002687"
FT MOD_RES 39
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91VR2"
FT MOD_RES 49
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91VR2"
FT MOD_RES 55
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P36542"
FT MOD_RES 115
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91VR2"
FT MOD_RES 115
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91VR2"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36542"
FT MOD_RES 154
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P36542"
FT MOD_RES 154
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91VR2"
FT MOD_RES 197
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P36542"
FT MOD_RES 270
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91VR2"
SQ SEQUENCE 297 AA; 32867 MW; E8060FA77D3D8EFC CRC64;
MFSRAGVAGL SAWTLQPQWI QVRNMATLKD ITRRLKSIKN IQKITKSMKM VAAAKYARAE
RELKPARIYG LGSLALYEKA DIKGPEDKKK HLLIGVSSDR GLCGAIHSSI AKQMKSEVAT
LTAAGKEVML VGVGDKIRGI LYRTHSDQFL VAFKEVGRKP PTFGDASVIA LELLNSGYEF
DEGSIIFNKF RSVISYKTEE KPIFSLNTVA SADSMSIYDD IDADVLQNYQ EYNLANIIYY
SLKESTTSEQ SARMTAMDNA SKNASEMIDK LTLTFNRTRQ AVITKELIEI ISGAAAL
