ATP5I_HUMAN
ID ATP5I_HUMAN Reviewed; 69 AA.
AC P56385; Q0D2L9;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 179.
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};
DE Contains:
DE RecName: Full=ATP synthase subunit e, mitochondrial, N-terminally processed;
GN Name=ATP5ME {ECO:0000312|HGNC:HGNC:846};
GN Synonyms=ATP5I {ECO:0000312|HGNC:HGNC:846}, ATP5K;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal brain;
RA Fujiwara T., Kawai A., Shimizu F., Shinomiya K., Hirano H., Okuno S.,
RA Ozaki K., Katagiri T., Takeda S., Kuga Y., Shimada Y., Nagata M.,
RA Takaichi A., Watanabe T., Horie M., Nakamura Y., Takahashi E., Hirai Y.;
RT "Molecular cloning of a human homolog of rat ATP synthase subunit e from
RT human fetal brain.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [4]
RP PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 2-16.
RC TISSUE=Leukemic T-cell;
RX PubMed=19892738; DOI=10.1073/pnas.0908958106;
RA Xu G., Shin S.B., Jaffrey S.R.;
RT "Global profiling of protease cleavage sites by chemoselective labeling of
RT protein N-termini.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
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 -!- INTERACTION:
CC P56385; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-2270000, EBI-7062247;
CC P56385; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-2270000, EBI-742688;
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC -!- SIMILARITY: Belongs to the ATPase e subunit family. {ECO:0000305}.
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DR EMBL; D50371; BAA23322.1; -; mRNA.
DR EMBL; BT006922; AAP35568.1; -; mRNA.
DR EMBL; BC003679; AAH03679.1; -; mRNA.
DR EMBL; BC105610; AAI05611.1; -; mRNA.
DR CCDS; CCDS3337.1; -.
DR RefSeq; NP_009031.1; NM_007100.3.
DR AlphaFoldDB; P56385; -.
DR SMR; P56385; -.
DR BioGRID; 107005; 98.
DR ComplexPortal; CPX-6151; Mitochondrial proton-transporting ATP synthase complex.
DR CORUM; P56385; -.
DR IntAct; P56385; 54.
DR MINT; P56385; -.
DR STRING; 9606.ENSP00000306003; -.
DR DrugBank; DB12695; Phenethyl Isothiocyanate.
DR TCDB; 3.A.2.1.15; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR iPTMnet; P56385; -.
DR PhosphoSitePlus; P56385; -.
DR SwissPalm; P56385; -.
DR BioMuta; ATP5I; -.
DR DMDM; 3023369; -.
DR EPD; P56385; -.
DR jPOST; P56385; -.
DR MassIVE; P56385; -.
DR MaxQB; P56385; -.
DR PaxDb; P56385; -.
DR PeptideAtlas; P56385; -.
DR PRIDE; P56385; -.
DR ProteomicsDB; 56918; -.
DR TopDownProteomics; P56385; -.
DR Antibodypedia; 22135; 186 antibodies from 28 providers.
DR DNASU; 521; -.
DR Ensembl; ENST00000304312.5; ENSP00000306003.4; ENSG00000169020.10.
DR GeneID; 521; -.
DR KEGG; hsa:521; -.
DR MANE-Select; ENST00000304312.5; ENSP00000306003.4; NM_007100.4; NP_009031.1.
DR UCSC; uc003gas.3; human.
DR CTD; 521; -.
DR DisGeNET; 521; -.
DR GeneCards; ATP5ME; -.
DR HGNC; HGNC:846; ATP5ME.
DR HPA; ENSG00000169020; Tissue enhanced (skeletal).
DR MIM; 601519; gene.
DR neXtProt; NX_P56385; -.
DR OpenTargets; ENSG00000169020; -.
DR PharmGKB; PA25136; -.
DR VEuPathDB; HostDB:ENSG00000169020; -.
DR eggNOG; KOG4326; Eukaryota.
DR GeneTree; ENSGT00390000005102; -.
DR HOGENOM; CLU_180903_0_0_1; -.
DR InParanoid; P56385; -.
DR OMA; GAFHQNR; -.
DR OrthoDB; 1640426at2759; -.
DR PhylomeDB; P56385; -.
DR TreeFam; TF314719; -.
DR BioCyc; MetaCyc:HS09866-MON; -.
DR PathwayCommons; P56385; -.
DR Reactome; R-HSA-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-HSA-8949613; Cristae formation.
DR SignaLink; P56385; -.
DR SIGNOR; P56385; -.
DR BioGRID-ORCS; 521; 366 hits in 1084 CRISPR screens.
DR ChiTaRS; ATP5I; human.
DR GeneWiki; ATP5I; -.
DR GenomeRNAi; 521; -.
DR Pharos; P56385; Tbio.
DR PRO; PR:P56385; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P56385; protein.
DR Bgee; ENSG00000169020; Expressed in apex of heart and 207 other tissues.
DR Genevisible; P56385; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
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); IEA:InterPro.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IC:ComplexPortal.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IDA:UniProtKB.
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 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 CHAIN 1..69
FT /note="ATP synthase subunit e, mitochondrial"
FT /id="PRO_0000434346"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 2..69
FT /note="ATP synthase subunit e, mitochondrial, N-terminally
FT processed"
FT /id="PRO_0000071684"
FT MOD_RES 34
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q06185"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29419"
SQ SEQUENCE 69 AA; 7933 MW; E4FF2B855F4535DC CRC64;
MVPPVQVSPL IKLGRYSALF LGVAYGATRY NYLKPRAEEE RRIAAEEKKK QDELKRIARE
LAEDDSILK
