ATP5J_PIG
ID ATP5J_PIG Reviewed; 76 AA.
AC P13618;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=ATP synthase-coupling factor 6, mitochondrial {ECO:0000305};
DE Short=ATPase subunit F6;
DE AltName: Full=ATP synthase peripheral stalk subunit F6 {ECO:0000305};
GN Name=ATP5PF {ECO:0000250|UniProtKB:P18859}; Synonyms=ATP5J;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Intestine;
RX PubMed=2961617; DOI=10.1016/0014-5793(87)80547-1;
RA Chen Z.-W., Mutt V., Barros-Soederling J., Joernvall H.;
RT "Isolation and structural characterization of porcine coupling factor 6
RT from intestinal tissues.";
RL FEBS Lett. 226:43-46(1987).
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 F(0)
CC - containing the membrane proton channel, linked together by a central
CC stalk and a peripheral stalk. During catalysis, ATP synthesis in the
CC catalytic domain of F(1) is coupled via a rotary mechanism of the
CC central stalk subunits to proton translocation. Part of the complex
CC F(0) domain and the peripheric stalk, which acts as a stator to hold
CC the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static
CC relative to the rotary elements. Also involved in the restoration of
CC oligomycin-sensitive ATPase activity to depleted F1-F0 complexes (By
CC similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC -!- SIMILARITY: Belongs to the eukaryotic ATPase subunit F6 family.
CC {ECO:0000305}.
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DR PIR; S00212; S00212.
DR PDB; 6J5I; EM; 3.34 A; c=7-76.
DR PDB; 6J5J; EM; 3.45 A; c=7-76.
DR PDB; 6J5K; EM; 6.20 A; Ac/Bc/Cc/c=7-76.
DR PDBsum; 6J5I; -.
DR PDBsum; 6J5J; -.
DR PDBsum; 6J5K; -.
DR AlphaFoldDB; P13618; -.
DR BMRB; P13618; -.
DR SMR; P13618; -.
DR IntAct; P13618; 1.
DR STRING; 9823.ENSSSCP00000019617; -.
DR PaxDb; P13618; -.
DR PeptideAtlas; P13618; -.
DR eggNOG; KOG4634; Eukaryota.
DR HOGENOM; CLU_145649_1_0_1; -.
DR InParanoid; P13618; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; P13618; SS.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; ISS:UniProtKB.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IEA:InterPro.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro.
DR Gene3D; 1.10.246.110; -; 1.
DR InterPro; IPR008387; ATP_synth_f6_mt.
DR InterPro; IPR036204; ATP_synth_f6_sf_mt.
DR PANTHER; PTHR12441; PTHR12441; 1.
DR Pfam; PF05511; ATP-synt_F6; 1.
DR PIRSF; PIRSF002455; ATP_synthase_coupling_factor_6; 1.
DR SUPFAM; SSF111357; SSF111357; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; CF(0); Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Phosphoprotein; Reference proteome;
KW Transport.
FT CHAIN 1..76
FT /note="ATP synthase-coupling factor 6, mitochondrial"
FT /id="PRO_0000071700"
FT MOD_RES 9
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P18859"
FT MOD_RES 14
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P18859"
FT MOD_RES 47
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P97450"
FT MOD_RES 52
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P97450"
FT MOD_RES 52
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P97450"
FT MOD_RES 67
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P18859"
FT MOD_RES 67
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P97450"
FT MOD_RES 73
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P18859"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21571"
FT HELIX 8..19
FT /evidence="ECO:0007829|PDB:6J5I"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:6J5I"
FT TURN 29..32
FT /evidence="ECO:0007829|PDB:6J5J"
FT HELIX 34..48
FT /evidence="ECO:0007829|PDB:6J5I"
SQ SEQUENCE 76 AA; 8930 MW; 16F73EE42F87B874 CRC64;
NKELDPVQKL FVDKIREYRT KRQTSGGPVD AGPEYQQDLD RELFKLKQMY GKADMNTFPN
FTFEDPKFEA VEKPQS
