ATP5L_RAT
ID ATP5L_RAT Reviewed; 103 AA.
AC Q6PDU7; G3V9A9;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=ATP synthase subunit g, mitochondrial {ECO:0000305};
DE Short=ATPase subunit g;
DE AltName: Full=ATP synthase membrane subunit g {ECO:0000305};
GN Name=Atp5mg {ECO:0000312|RGD:1303259}; Synonyms=Atp5l;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
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).
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(0) domain. Minor subunit located with subunit a in the membrane.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(0) seems to have nine
CC subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). Component of an ATP
CC synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME,
CC ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C,
CC ATP5PO, ATP5MG, ATP5MK and ATP5MJ. {ECO:0000269|PubMed:17575325}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC -!- SIMILARITY: Belongs to the ATPase g subunit family. {ECO:0000305}.
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DR EMBL; CH473975; EDL95340.1; -; Genomic_DNA.
DR EMBL; BC058497; AAH58497.1; -; mRNA.
DR RefSeq; NP_997681.1; NM_212516.2.
DR AlphaFoldDB; Q6PDU7; -.
DR SMR; Q6PDU7; -.
DR BioGRID; 256666; 1.
DR CORUM; Q6PDU7; -.
DR IntAct; Q6PDU7; 1.
DR MINT; Q6PDU7; -.
DR STRING; 10116.ENSRNOP00000040969; -.
DR iPTMnet; Q6PDU7; -.
DR PhosphoSitePlus; Q6PDU7; -.
DR jPOST; Q6PDU7; -.
DR PaxDb; Q6PDU7; -.
DR PRIDE; Q6PDU7; -.
DR Ensembl; ENSRNOT00000050878; ENSRNOP00000040969; ENSRNOG00000028884.
DR GeneID; 300677; -.
DR KEGG; rno:300677; -.
DR UCSC; RGD:1303259; rat.
DR CTD; 10632; -.
DR RGD; 1303259; Atp5mg.
DR eggNOG; KOG4103; Eukaryota.
DR GeneTree; ENSGT00390000009724; -.
DR HOGENOM; CLU_152793_1_1_1; -.
DR InParanoid; Q6PDU7; -.
DR OMA; ATEVCMW; -.
DR OrthoDB; 1461139at2759; -.
DR PhylomeDB; Q6PDU7; -.
DR TreeFam; TF313978; -.
DR Reactome; R-RNO-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-RNO-8949613; Cristae formation.
DR PRO; PR:Q6PDU7; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Proteomes; UP000234681; Chromosome 8.
DR Bgee; ENSRNOG00000028884; Expressed in heart and 19 other tissues.
DR Genevisible; Q6PDU7; RN.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IDA:RGD.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046034; P:ATP metabolic process; IDA: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 InterPro; IPR006808; ATP_synth_F0_gsu_mt.
DR InterPro; IPR016702; ATP_synth_su_G_mt_met.
DR PANTHER; PTHR12386; PTHR12386; 1.
DR Pfam; PF04718; ATP-synt_G; 1.
DR PIRSF; PIRSF017835; ATP-synth_g_mitoch_animal; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP synthesis; CF(0); Hydrogen ion transport; Ion transport;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O75964"
FT CHAIN 2..103
FT /note="ATP synthase subunit g, mitochondrial"
FT /id="PRO_0000416600"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O75964"
FT MOD_RES 11
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CPQ8"
FT MOD_RES 24
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O75964"
FT MOD_RES 54
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CPQ8"
FT CONFLICT 55
FT /note="S -> N (in Ref. 2; AAH58497)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 103 AA; 11433 MW; AFB1430AED81B219 CRC64;
MAKFIRNLAD KAPSMVAAAV TYSKPRLATF WHYARVELVP PTLGEIPTAI QSMKSIIHSA
QTGNFKHLTV KEAVLNGLVA TEVWMWFYIG EIIGKRGIVG YDV
