ATP5I_PIG
ID ATP5I_PIG Reviewed; 71 AA.
AC Q9MYT8; A1XQR5;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 4.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=ATP synthase subunit e, mitochondrial {ECO:0000305};
DE Short=ATPase subunit e;
DE AltName: Full=ATP synthase membrane subunit e {ECO:0000305};
GN Name=ATP5ME {ECO:0000250|UniProtKB:P56385}; Synonyms=ATP5I;
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 [MRNA].
RC TISSUE=Skeletal muscle;
RA Maak S., Jaesert S., von Lengerken G.;
RT "Porcine ESTs differentially expressed in healthy piglets and piglets
RT suffering from congenital splay leg syndrome.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE 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
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC -!- SIMILARITY: Belongs to the ATPase e subunit family. {ECO:0000305}.
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DR EMBL; AJ278444; CAB94728.1; -; mRNA.
DR EMBL; DQ629136; ABK55621.1; -; mRNA.
DR RefSeq; NP_999080.1; NM_213915.1.
DR PDB; 6ZMR; EM; 3.94 A; e=2-71.
DR PDB; 6ZNA; EM; 6.20 A; Ae/Be/Ce/e=2-71.
DR PDBsum; 6ZMR; -.
DR PDBsum; 6ZNA; -.
DR AlphaFoldDB; Q9MYT8; -.
DR SMR; Q9MYT8; -.
DR STRING; 9823.ENSSSCP00000022175; -.
DR PaxDb; Q9MYT8; -.
DR PeptideAtlas; Q9MYT8; -.
DR PRIDE; Q9MYT8; -.
DR Ensembl; ENSSSCT00015005570; ENSSSCP00015002222; ENSSSCG00015004194.
DR Ensembl; ENSSSCT00025063133; ENSSSCP00025026879; ENSSSCG00025046462.
DR Ensembl; ENSSSCT00030102676; ENSSSCP00030047368; ENSSSCG00030073323.
DR Ensembl; ENSSSCT00035096268; ENSSSCP00035040503; ENSSSCG00035071243.
DR Ensembl; ENSSSCT00045022033; ENSSSCP00045015180; ENSSSCG00045012935.
DR Ensembl; ENSSSCT00050002950; ENSSSCP00050000959; ENSSSCG00050002355.
DR Ensembl; ENSSSCT00055017469; ENSSSCP00055013813; ENSSSCG00055008930.
DR Ensembl; ENSSSCT00060035343; ENSSSCP00060015074; ENSSSCG00060026086.
DR Ensembl; ENSSSCT00065086348; ENSSSCP00065037753; ENSSSCG00065062948.
DR Ensembl; ENSSSCT00070012708; ENSSSCP00070010455; ENSSSCG00070006634.
DR GeneID; 396950; -.
DR KEGG; ssc:396950; -.
DR CTD; 521; -.
DR eggNOG; KOG4326; Eukaryota.
DR HOGENOM; CLU_180903_0_0_1; -.
DR InParanoid; Q9MYT8; -.
DR OMA; GAFHQNR; -.
DR OrthoDB; 1640426at2759; -.
DR TreeFam; TF314719; -.
DR Reactome; R-SSC-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-SSC-8949613; Cristae formation.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 8.
DR Genevisible; Q9MYT8; 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:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:Ensembl.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IEA:Ensembl.
DR InterPro; IPR008386; ATP_synth_F0_esu_mt.
DR PANTHER; PTHR12427; PTHR12427; 1.
DR Pfam; PF05680; ATP-synt_E; 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; Transport.
FT CHAIN 1..71
FT /note="ATP synthase subunit e, mitochondrial"
FT /id="PRO_0000071686"
FT MOD_RES 34
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q06185"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29419"
FT CONFLICT 8
FT /note="S -> F (in Ref. 2; ABK55621)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="I -> T (in Ref. 1; CAB94728)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 71 AA; 8232 MW; 08E3E79499CC6432 CRC64;
MVPPVQVSPL IKLGRYSALF LGVAYGAKRY NYLKPRAEEE RRIAAEEKKK QDELKRIERE
LAEAQEDSIL K
