ATPK_PIG
ID ATPK_PIG Reviewed; 88 AA.
AC Q95339; A1XQR8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 4.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=ATP synthase subunit f, mitochondrial {ECO:0000305};
DE AltName: Full=ATP synthase membrane subunit f {ECO:0000305};
GN Name=ATP5MF {ECO:0000250|UniProtKB:P56134}; Synonyms=ATP5J2;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Small intestine;
RA Winteroe A.K., Fredholm M., Davies W.;
RT "Evaluation and characterization of a porcine small intestine cDNA
RT library.";
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Longissimus dorsi muscle;
RA Cai G., Chen Y., Wang C., Li J., Peng G., Zhang H.;
RT "Generation and analysis of cDNA sequences derived from a porcine skeletal
RT muscle library.";
RL Submitted (MAY-2006) 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 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. 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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane
CC {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ATPase F chain family. {ECO:0000305}.
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DR EMBL; Z81211; CAB03568.1; -; mRNA.
DR EMBL; DQ629139; ABK55624.1; -; mRNA.
DR RefSeq; NP_001090933.1; NM_001097464.1.
DR PDB; 6J54; EM; 3.94 A; f=2-88.
DR PDB; 6J5A; EM; 4.35 A; f=2-88.
DR PDB; 6J5I; EM; 3.34 A; f=2-88.
DR PDB; 6J5J; EM; 3.45 A; f=2-88.
DR PDB; 6J5K; EM; 6.20 A; Af/Bf/Cf/f=2-88.
DR PDB; 6ZMR; EM; 3.94 A; f=2-88.
DR PDB; 6ZNA; EM; 6.20 A; Af/Bf/Cf/f=2-88.
DR PDBsum; 6J54; -.
DR PDBsum; 6J5A; -.
DR PDBsum; 6J5I; -.
DR PDBsum; 6J5J; -.
DR PDBsum; 6J5K; -.
DR PDBsum; 6ZMR; -.
DR PDBsum; 6ZNA; -.
DR AlphaFoldDB; Q95339; -.
DR SMR; Q95339; -.
DR IntAct; Q95339; 1.
DR STRING; 9823.ENSSSCP00000008135; -.
DR PaxDb; Q95339; -.
DR PeptideAtlas; Q95339; -.
DR PRIDE; Q95339; -.
DR Ensembl; ENSSSCT00005014335; ENSSSCP00005008545; ENSSSCG00005009143.
DR Ensembl; ENSSSCT00070029288; ENSSSCP00070024407; ENSSSCG00070014902.
DR GeneID; 100037979; -.
DR KEGG; ssc:100037979; -.
DR CTD; 9551; -.
DR eggNOG; KOG4092; Eukaryota.
DR InParanoid; Q95339; -.
DR OMA; HKYVQPK; -.
DR OrthoDB; 1479342at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 3.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; ISS:UniProtKB.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IBA:GO_Central.
DR InterPro; IPR019344; F1F0-ATPsyn_F_prd.
DR PANTHER; PTHR13080; PTHR13080; 1.
DR Pfam; PF10206; WRW; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP synthesis; CF(0); Hydrogen ion transport;
KW Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P56134"
FT CHAIN 2..88
FT /note="ATP synthase subunit f, mitochondrial"
FT /id="PRO_0000194826"
FT TRANSMEM 55..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P56134"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZAF6"
FT MOD_RES 16
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P56135"
FT CONFLICT 2
FT /note="A -> T (in Ref. 2; ABK55624)"
FT /evidence="ECO:0000305"
FT HELIX 4..17
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:6J5J"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:6J5I"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 63..75
FT /evidence="ECO:0007829|PDB:6J5I"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:6J5I"
SQ SEQUENCE 88 AA; 10311 MW; 6B8A45E4B33C1A7B CRC64;
MASVVPLKDR RLLEVKLGEL PSWILMRDFT PSGIAGAFQR GYYRYYNKYV NVKKGSVAGL
SMVLAAYVVF NYCRSYKELK HERLRKYH