ID ATP5I_RAT Reviewed; 71 AA.
AC P29419;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 27-MAR-2024, entry version 148.
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:0000312|RGD:621377}; Synonyms=Atp5i;
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 [MRNA], AND PROTEIN SEQUENCE OF 2-71.
RC TISSUE=Liver;
RX PubMed=1463732; DOI=10.1021/bi00164a022;
RA Higuti T., Kuroiwa K., Kawamura Y., Yoshihara Y.;
RT "Complete amino acid sequence of subunit e of rat liver mitochondrial H(+)-
RT ATP synthase.";
RL Biochemistry 31:12451-12454(1992).
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 PROTEIN SEQUENCE OF 2-45.
RC TISSUE=Liver;
RX PubMed=1429613; DOI=10.1016/s0021-9258(18)41722-x;
RA Higuti T., Yoshihara Y., Kuroiwa K., Kawamura Y., Toda H., Sakiyama F.;
RT "A simple, rapid method for purification of epsilon-subunit, coupling
RT factor 6, subunit d, and subunit e from rat liver H(+)-ATP synthase and
RT determination of the complete amino acid sequence of epsilon-subunit.";
RL J. Biol. Chem. 267:22658-22661(1992).
RN [4]
RP PROTEIN SEQUENCE OF 16-28 AND 60-71, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
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).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 ATP5MPL. {ECO:0000269|PubMed:17575325}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC -!- SIMILARITY: Belongs to the ATPase e subunit family. {ECO:0000305}.
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DR EMBL; D13121; BAA02423.1; -; mRNA.
DR EMBL; BC058449; AAH58449.1; -; mRNA.
DR PIR; A44246; A44246.
DR RefSeq; NP_536729.1; NM_080481.1.
DR AlphaFoldDB; P29419; -.
DR SMR; P29419; -.
DR BioGRID; 250811; 2.
DR CORUM; P29419; -.
DR IntAct; P29419; 2.
DR MINT; P29419; -.
DR STRING; 10116.ENSRNOP00000000072; -.
DR GlyGen; P29419; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P29419; -.
DR PhosphoSitePlus; P29419; -.
DR SwissPalm; P29419; -.
DR jPOST; P29419; -.
DR PaxDb; 10116-ENSRNOP00000000072; -.
DR GeneID; 140608; -.
DR KEGG; rno:140608; -.
DR UCSC; RGD:621377; rat.
DR AGR; RGD:621377; -.
DR CTD; 521; -.
DR RGD; 621377; Atp5me.
DR VEuPathDB; HostDB:ENSRNOG00000000064; -.
DR eggNOG; KOG4326; Eukaryota.
DR HOGENOM; CLU_180903_0_0_1; -.
DR InParanoid; P29419; -.
DR OrthoDB; 5361366at2759; -.
DR PhylomeDB; P29419; -.
DR TreeFam; TF314719; -.
DR Reactome; R-RNO-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-RNO-8949613; Cristae formation.
DR PRO; PR:P29419; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000000064; Expressed in quadriceps femoris and 20 other cell types or tissues.
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:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; ISO:RGD.
DR InterPro; IPR008386; ATP_synth_F0_esu_mt.
DR PANTHER; PTHR12427; ATP SYNTHASE E CHAIN, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12427:SF1; ATP SYNTHASE SUBUNIT E, MITOCHONDRIAL; 1.
DR Pfam; PF05680; ATP-synt_E; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP synthesis; CF(0); Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Phosphoprotein; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1429613,
FT ECO:0000269|PubMed:1463732"
FT CHAIN 2..71
FT /note="ATP synthase subunit e, mitochondrial"
FT /id="PRO_0000071688"
FT MOD_RES 34
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q06185"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 71 AA; 8255 MW; 0377253CE2B422D2 CRC64;
MVPPVQVSPL IKFGRYSALI LGMAYGAKRY SYLKPRAEEE RRIAAEEKKR LDELKRIERE
LAEAEDVSIF K
//
