ATP5L_BOVIN
ID ATP5L_BOVIN Reviewed; 103 AA.
AC Q28852; Q3T0C5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 140.
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:0000250|UniProtKB:O75964}; Synonyms=ATP5L;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-103, AND MASS
RP SPECTROMETRY.
RC TISSUE=Heart;
RX PubMed=8011660; DOI=10.1021/bi00191a026;
RA Collinson I.R., Runswick M.J., Buchanan S.K., Fearnley I.M., Skehel J.M.,
RA van Raaij M.J., Griffiths D.E., Walker J.E.;
RT "F0 membrane domain of ATP synthase from bovine heart mitochondria:
RT purification, subunit composition, and reconstitution with F1-ATPase.";
RL Biochemistry 33:7971-7978(1994).
RN [2]
RP SEQUENCE REVISION TO 93.
RA Collinson I.R., Runswick M.J., Buchanan S.K., Fearnley I.M., Skehel J.M.,
RA van Raaij M.J., Griffiths D.E., Walker J.E.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION IN THE ATP SYNTHASE COMPLEX.
RX PubMed=17570365; DOI=10.1016/j.febslet.2007.05.079;
RA Chen R., Runswick M.J., Carroll J., Fearnley I.M., Walker J.E.;
RT "Association of two proteolipids of unknown function with ATP synthase from
RT bovine heart mitochondria.";
RL FEBS Lett. 581:3145-3148(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:17570365}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC -!- MASS SPECTROMETRY: Mass=11328.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8011660};
CC -!- SIMILARITY: Belongs to the ATPase g subunit family. {ECO:0000305}.
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DR EMBL; S70448; AAB31108.3; -; mRNA.
DR EMBL; BC102455; AAI02456.1; -; mRNA.
DR PIR; B54211; B54211.
DR RefSeq; NP_001019721.4; NM_001024550.4.
DR PDB; 6ZBB; EM; 3.61 A; g=2-103.
DR PDB; 6ZIQ; EM; 4.33 A; g=2-103.
DR PDB; 6ZIT; EM; 3.49 A; g=2-103.
DR PDB; 6ZIU; EM; 6.02 A; g=2-103.
DR PDB; 6ZPO; EM; 4.00 A; g=2-103.
DR PDB; 6ZQM; EM; 3.29 A; g=2-103.
DR PDB; 6ZQN; EM; 4.00 A; g=2-103.
DR PDB; 7AJB; EM; 9.20 A; Ag/g=2-103.
DR PDB; 7AJC; EM; 11.90 A; Ag/g=2-103.
DR PDB; 7AJD; EM; 9.00 A; Ag/g=2-103.
DR PDB; 7AJE; EM; 9.40 A; Ag/g=2-103.
DR PDB; 7AJF; EM; 8.45 A; Ag/g=2-103.
DR PDB; 7AJG; EM; 10.70 A; Ag/g=2-103.
DR PDB; 7AJH; EM; 9.70 A; Ag/g=2-103.
DR PDB; 7AJI; EM; 11.40 A; Ag/g=2-103.
DR PDB; 7AJJ; EM; 13.10 A; Ag/g=2-103.
DR PDBsum; 6ZBB; -.
DR PDBsum; 6ZIQ; -.
DR PDBsum; 6ZIT; -.
DR PDBsum; 6ZIU; -.
DR PDBsum; 6ZPO; -.
DR PDBsum; 6ZQM; -.
DR PDBsum; 6ZQN; -.
DR PDBsum; 7AJB; -.
DR PDBsum; 7AJC; -.
DR PDBsum; 7AJD; -.
DR PDBsum; 7AJE; -.
DR PDBsum; 7AJF; -.
DR PDBsum; 7AJG; -.
DR PDBsum; 7AJH; -.
DR PDBsum; 7AJI; -.
DR PDBsum; 7AJJ; -.
DR AlphaFoldDB; Q28852; -.
DR SMR; Q28852; -.
DR IntAct; Q28852; 1.
DR MINT; Q28852; -.
DR STRING; 9913.ENSBTAP00000009643; -.
DR PaxDb; Q28852; -.
DR PeptideAtlas; Q28852; -.
DR GeneID; 515696; -.
DR KEGG; bta:515696; -.
DR CTD; 10632; -.
DR eggNOG; KOG4103; Eukaryota.
DR HOGENOM; CLU_152793_1_1_1; -.
DR InParanoid; Q28852; -.
DR OrthoDB; 1461139at2759; -.
DR TreeFam; TF313978; -.
DR Proteomes; UP000009136; Unplaced.
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); IBA:GO_Central.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
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 3D-structure; Acetylation; ATP synthesis; CF(0); Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O75964,
FT ECO:0000269|PubMed:8011660"
FT CHAIN 2..103
FT /note="ATP synthase subunit g, mitochondrial"
FT /id="PRO_0000071690"
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 35
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CPQ8"
FT MOD_RES 54
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CPQ8"
FT CONFLICT 3
FT /note="E -> Q (in Ref. 3; AAI02456)"
FT /evidence="ECO:0000305"
FT HELIX 23..36
FT /evidence="ECO:0007829|PDB:6ZIT"
FT HELIX 45..61
FT /evidence="ECO:0007829|PDB:6ZIT"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:6ZIT"
FT HELIX 70..94
FT /evidence="ECO:0007829|PDB:6ZIT"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:6ZIT"
SQ SEQUENCE 103 AA; 11417 MW; 9E2A9089ADEAC56B CRC64;
MAEFVRNLAE KAPALVNAAV TYSKPRLATF WYYAKVELVP PTPAEIPTAI QSLKKIINSA
KTGSFKQLTV KEALLNGLVA TEVWMWFYVG EIIGKRGIIG YDV
