Full text data of ATP6V1E1
ATP6V1E1
(ATP6E, ATP6E2)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
V-type proton ATPase subunit E 1; V-ATPase subunit E 1 (V-ATPase 31 kDa subunit; p31; Vacuolar proton pump subunit E 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
V-type proton ATPase subunit E 1; V-ATPase subunit E 1 (V-ATPase 31 kDa subunit; p31; Vacuolar proton pump subunit E 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P36543
ID VATE1_HUMAN Reviewed; 226 AA.
AC P36543; A8MUE4; A8MUN4;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-1994, sequence version 1.
DT 22-JAN-2014, entry version 141.
DE RecName: Full=V-type proton ATPase subunit E 1;
DE Short=V-ATPase subunit E 1;
DE AltName: Full=V-ATPase 31 kDa subunit;
DE Short=p31;
DE AltName: Full=Vacuolar proton pump subunit E 1;
GN Name=ATP6V1E1; Synonyms=ATP6E, ATP6E2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1533641;
RA Hemken P., Guo X.-L., Wang Z.-Q., Zhang K., Gluck S.;
RT "Immunologic evidence that vacuolar H+ ATPases with heterogeneous
RT forms of Mr = 31,000 subunit have different membrane distributions in
RT mammalian kidney.";
RL J. Biol. Chem. 267:9948-9957(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8004105; DOI=10.1093/hmg/3.2.335;
RA Baud V., Mears A., Lamour V., Scamps C., McDermid A., Lipinski M.;
RT "The E subunit of vacuolar H(+)-ATPase localizes close to the
RT centromere on human chromosome 22.";
RL Hum. Mol. Genet. 3:335-339(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Osteoclastoma;
RX PubMed=8250920; DOI=10.1006/bbrc.1993.2434;
RA van Hille B., Vanek M., Richener H., Green J.R., Bilbe G.;
RT "Cloning and tissue distribution of subunits C, D, and E of the human
RT vacuolar H(+)-ATPase.";
RL Biochem. Biophys. Res. Commun. 197:15-21(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Brain, and Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 112-131, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [9]
RP INTERACTION WITH ALDOC.
RX PubMed=11399750; DOI=10.1074/jbc.M008768200;
RA Lu M., Holliday L.S., Zhang L., Dunn W.A. Jr., Gluck S.L.;
RT "Interaction between aldolase and vacuolar H+-ATPase: evidence for
RT direct coupling of glycolysis to the ATP-hydrolyzing proton pump.";
RL J. Biol. Chem. 276:30407-30413(2001).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=12036578; DOI=10.1016/S0378-1119(02)00542-5;
RA Imai-Senga Y., Sun-Wada G.H., Wada Y., Futai M.;
RT "A human gene, ATP6E1, encoding a testis-specific isoform of H(+)-
RT ATPase subunit E.";
RL Gene 289:7-12(2002).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
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.,
RA Buerckstuemmer T., 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 [13]
RP INTERACTION WITH RAB11B.
RX PubMed=20717956; DOI=10.1002/jcp.22388;
RA Oehlke O., Martin H.W., Osterberg N., Roussa E.;
RT "Rab11b and its effector Rip11 regulate the acidosis-induced traffic
RT of V-ATPase in salivary ducts.";
RL J. Cell. Physiol. 226:638-651(2011).
RN [14]
RP VARIANT [LARGE SCALE ANALYSIS] GLY-50.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase
CC essential for assembly or catalytic function. V-ATPase is
CC responsible for acidifying a variety of intracellular compartments
CC in eukaryotic cells.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a
CC peripheral catalytic V1 complex (components A to H) attached to an
CC integral membrane V0 proton pore complex (components: a, c, c',
CC c'' and d). Interacts with RABL2/RABL2A; binds preferentially to
CC GTP-bound RABL2 (By similarity). Interacts with ALDOC. Interacts
CC with RAB11B.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P36543-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P36543-2; Sequence=VSP_042925;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=P36543-3; Sequence=VSP_044589;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the V-ATPase E subunit family.
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DR EMBL; X76228; CAA53814.1; -; mRNA.
DR EMBL; X71491; CAA50592.1; -; mRNA.
DR EMBL; CR456385; CAG30271.1; -; mRNA.
DR EMBL; AK294623; BAG57804.1; -; mRNA.
DR EMBL; AK315941; BAH14312.1; -; mRNA.
DR EMBL; AC004019; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC006285; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC007666; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004443; AAH04443.1; -; mRNA.
DR PIR; S60562; S60562.
DR RefSeq; NP_001034455.1; NM_001039366.1.
DR RefSeq; NP_001034456.1; NM_001039367.1.
DR RefSeq; NP_001687.1; NM_001696.3.
DR UniGene; Hs.517338; -.
DR ProteinModelPortal; P36543; -.
DR SMR; P36543; 2-217.
DR IntAct; P36543; 7.
DR MINT; MINT-5002575; -.
DR STRING; 9606.ENSP00000253413; -.
DR TCDB; 3.A.2.2.4; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR PhosphoSite; P36543; -.
DR DMDM; 549207; -.
DR UCD-2DPAGE; P36543; -.
DR PaxDb; P36543; -.
DR PRIDE; P36543; -.
DR DNASU; 529; -.
DR Ensembl; ENST00000253413; ENSP00000253413; ENSG00000131100.
DR Ensembl; ENST00000399796; ENSP00000382694; ENSG00000131100.
DR Ensembl; ENST00000399798; ENSP00000382696; ENSG00000131100.
DR GeneID; 529; -.
DR KEGG; hsa:529; -.
DR UCSC; uc002zms.1; human.
DR CTD; 529; -.
DR GeneCards; GC22M018074; -.
DR HGNC; HGNC:857; ATP6V1E1.
DR HPA; CAB009528; -.
DR HPA; CAB018699; -.
DR HPA; HPA029196; -.
DR MIM; 108746; gene.
DR neXtProt; NX_P36543; -.
DR PharmGKB; PA25158; -.
DR eggNOG; COG1390; -.
DR HOGENOM; HOG000202506; -.
DR HOVERGEN; HBG002309; -.
DR InParanoid; P36543; -.
DR KO; K02150; -.
DR OMA; TIRCRKQ; -.
DR OrthoDB; EOG70PC01; -.
DR PhylomeDB; P36543; -.
DR BioCyc; MetaCyc:HS05489-MONOMER; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR GeneWiki; ATP6V1E1; -.
DR GenomeRNAi; 529; -.
DR NextBio; 2197; -.
DR PRO; PR:P36543; -.
DR ArrayExpress; P36543; -.
DR Bgee; P36543; -.
DR CleanEx; HS_ATP6V1E1; -.
DR Genevestigator; P36543; -.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0016469; C:proton-transporting two-sector ATPase complex; TAS:ProtInc.
DR GO; GO:0033178; C:proton-transporting two-sector ATPase complex, catalytic domain; IEA:InterPro.
DR GO; GO:0008553; F:hydrogen-exporting ATPase activity, phosphorylative mechanism; IEA:Ensembl.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:Ensembl.
DR GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
DR GO; GO:0051701; P:interaction with host; TAS:Reactome.
DR GO; GO:0090382; P:phagosome maturation; TAS:Reactome.
DR GO; GO:0015992; P:proton transport; TAS:ProtInc.
DR GO; GO:0033572; P:transferrin transport; TAS:Reactome.
DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
DR InterPro; IPR002842; ATPase_V1/A1-cplx_esu.
DR Pfam; PF01991; vATP-synt_E; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Hydrogen ion transport; Hydrolase;
KW Ion transport; Phosphoprotein; Polymorphism; Reference proteome;
KW Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 226 V-type proton ATPase subunit E 1.
FT /FTId=PRO_0000117295.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 56 56 Phosphotyrosine (By similarity).
FT VAR_SEQ 12 33 Missing (in isoform 2).
FT /FTId=VSP_042925.
FT VAR_SEQ 93 122 Missing (in isoform 3).
FT /FTId=VSP_044589.
FT VARIANT 50 50 R -> G (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_036565.
FT CONFLICT 32 32 A -> R (in Ref. 3; CAA50592).
FT CONFLICT 86 86 A -> G (in Ref. 1; no nucleotide entry).
SQ SEQUENCE 226 AA; 26145 MW; DFD0D44E6D9AEA17 CRC64;
MALSDADVQK QIKHMMAFIE QEANEKAEEI DAKAEEEFNI EKGRLVQTQR LKIMEYYEKK
EKQIEQQKKI QMSNLMNQAR LKVLRARDDL ITDLLNEAKQ RLSKVVKDTT RYQVLLDGLV
LQGLYQLLEP RMIVRCRKQD FPLVKAAVQK AIPMYKIATK NDVDVQIDQE SYLPEDIAGG
VEIYNGDRKI KVSNTLESRL DLIAQQMMPE VRGALFGANA NRKFLD
//
ID VATE1_HUMAN Reviewed; 226 AA.
AC P36543; A8MUE4; A8MUN4;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-1994, sequence version 1.
DT 22-JAN-2014, entry version 141.
DE RecName: Full=V-type proton ATPase subunit E 1;
DE Short=V-ATPase subunit E 1;
DE AltName: Full=V-ATPase 31 kDa subunit;
DE Short=p31;
DE AltName: Full=Vacuolar proton pump subunit E 1;
GN Name=ATP6V1E1; Synonyms=ATP6E, ATP6E2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1533641;
RA Hemken P., Guo X.-L., Wang Z.-Q., Zhang K., Gluck S.;
RT "Immunologic evidence that vacuolar H+ ATPases with heterogeneous
RT forms of Mr = 31,000 subunit have different membrane distributions in
RT mammalian kidney.";
RL J. Biol. Chem. 267:9948-9957(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8004105; DOI=10.1093/hmg/3.2.335;
RA Baud V., Mears A., Lamour V., Scamps C., McDermid A., Lipinski M.;
RT "The E subunit of vacuolar H(+)-ATPase localizes close to the
RT centromere on human chromosome 22.";
RL Hum. Mol. Genet. 3:335-339(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Osteoclastoma;
RX PubMed=8250920; DOI=10.1006/bbrc.1993.2434;
RA van Hille B., Vanek M., Richener H., Green J.R., Bilbe G.;
RT "Cloning and tissue distribution of subunits C, D, and E of the human
RT vacuolar H(+)-ATPase.";
RL Biochem. Biophys. Res. Commun. 197:15-21(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Brain, and Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 112-131, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [9]
RP INTERACTION WITH ALDOC.
RX PubMed=11399750; DOI=10.1074/jbc.M008768200;
RA Lu M., Holliday L.S., Zhang L., Dunn W.A. Jr., Gluck S.L.;
RT "Interaction between aldolase and vacuolar H+-ATPase: evidence for
RT direct coupling of glycolysis to the ATP-hydrolyzing proton pump.";
RL J. Biol. Chem. 276:30407-30413(2001).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=12036578; DOI=10.1016/S0378-1119(02)00542-5;
RA Imai-Senga Y., Sun-Wada G.H., Wada Y., Futai M.;
RT "A human gene, ATP6E1, encoding a testis-specific isoform of H(+)-
RT ATPase subunit E.";
RL Gene 289:7-12(2002).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
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.,
RA Buerckstuemmer T., 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 [13]
RP INTERACTION WITH RAB11B.
RX PubMed=20717956; DOI=10.1002/jcp.22388;
RA Oehlke O., Martin H.W., Osterberg N., Roussa E.;
RT "Rab11b and its effector Rip11 regulate the acidosis-induced traffic
RT of V-ATPase in salivary ducts.";
RL J. Cell. Physiol. 226:638-651(2011).
RN [14]
RP VARIANT [LARGE SCALE ANALYSIS] GLY-50.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase
CC essential for assembly or catalytic function. V-ATPase is
CC responsible for acidifying a variety of intracellular compartments
CC in eukaryotic cells.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a
CC peripheral catalytic V1 complex (components A to H) attached to an
CC integral membrane V0 proton pore complex (components: a, c, c',
CC c'' and d). Interacts with RABL2/RABL2A; binds preferentially to
CC GTP-bound RABL2 (By similarity). Interacts with ALDOC. Interacts
CC with RAB11B.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P36543-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P36543-2; Sequence=VSP_042925;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=P36543-3; Sequence=VSP_044589;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the V-ATPase E subunit family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; X76228; CAA53814.1; -; mRNA.
DR EMBL; X71491; CAA50592.1; -; mRNA.
DR EMBL; CR456385; CAG30271.1; -; mRNA.
DR EMBL; AK294623; BAG57804.1; -; mRNA.
DR EMBL; AK315941; BAH14312.1; -; mRNA.
DR EMBL; AC004019; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC006285; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC007666; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004443; AAH04443.1; -; mRNA.
DR PIR; S60562; S60562.
DR RefSeq; NP_001034455.1; NM_001039366.1.
DR RefSeq; NP_001034456.1; NM_001039367.1.
DR RefSeq; NP_001687.1; NM_001696.3.
DR UniGene; Hs.517338; -.
DR ProteinModelPortal; P36543; -.
DR SMR; P36543; 2-217.
DR IntAct; P36543; 7.
DR MINT; MINT-5002575; -.
DR STRING; 9606.ENSP00000253413; -.
DR TCDB; 3.A.2.2.4; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR PhosphoSite; P36543; -.
DR DMDM; 549207; -.
DR UCD-2DPAGE; P36543; -.
DR PaxDb; P36543; -.
DR PRIDE; P36543; -.
DR DNASU; 529; -.
DR Ensembl; ENST00000253413; ENSP00000253413; ENSG00000131100.
DR Ensembl; ENST00000399796; ENSP00000382694; ENSG00000131100.
DR Ensembl; ENST00000399798; ENSP00000382696; ENSG00000131100.
DR GeneID; 529; -.
DR KEGG; hsa:529; -.
DR UCSC; uc002zms.1; human.
DR CTD; 529; -.
DR GeneCards; GC22M018074; -.
DR HGNC; HGNC:857; ATP6V1E1.
DR HPA; CAB009528; -.
DR HPA; CAB018699; -.
DR HPA; HPA029196; -.
DR MIM; 108746; gene.
DR neXtProt; NX_P36543; -.
DR PharmGKB; PA25158; -.
DR eggNOG; COG1390; -.
DR HOGENOM; HOG000202506; -.
DR HOVERGEN; HBG002309; -.
DR InParanoid; P36543; -.
DR KO; K02150; -.
DR OMA; TIRCRKQ; -.
DR OrthoDB; EOG70PC01; -.
DR PhylomeDB; P36543; -.
DR BioCyc; MetaCyc:HS05489-MONOMER; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR GeneWiki; ATP6V1E1; -.
DR GenomeRNAi; 529; -.
DR NextBio; 2197; -.
DR PRO; PR:P36543; -.
DR ArrayExpress; P36543; -.
DR Bgee; P36543; -.
DR CleanEx; HS_ATP6V1E1; -.
DR Genevestigator; P36543; -.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0016469; C:proton-transporting two-sector ATPase complex; TAS:ProtInc.
DR GO; GO:0033178; C:proton-transporting two-sector ATPase complex, catalytic domain; IEA:InterPro.
DR GO; GO:0008553; F:hydrogen-exporting ATPase activity, phosphorylative mechanism; IEA:Ensembl.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:Ensembl.
DR GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
DR GO; GO:0051701; P:interaction with host; TAS:Reactome.
DR GO; GO:0090382; P:phagosome maturation; TAS:Reactome.
DR GO; GO:0015992; P:proton transport; TAS:ProtInc.
DR GO; GO:0033572; P:transferrin transport; TAS:Reactome.
DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
DR InterPro; IPR002842; ATPase_V1/A1-cplx_esu.
DR Pfam; PF01991; vATP-synt_E; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Hydrogen ion transport; Hydrolase;
KW Ion transport; Phosphoprotein; Polymorphism; Reference proteome;
KW Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 226 V-type proton ATPase subunit E 1.
FT /FTId=PRO_0000117295.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 56 56 Phosphotyrosine (By similarity).
FT VAR_SEQ 12 33 Missing (in isoform 2).
FT /FTId=VSP_042925.
FT VAR_SEQ 93 122 Missing (in isoform 3).
FT /FTId=VSP_044589.
FT VARIANT 50 50 R -> G (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_036565.
FT CONFLICT 32 32 A -> R (in Ref. 3; CAA50592).
FT CONFLICT 86 86 A -> G (in Ref. 1; no nucleotide entry).
SQ SEQUENCE 226 AA; 26145 MW; DFD0D44E6D9AEA17 CRC64;
MALSDADVQK QIKHMMAFIE QEANEKAEEI DAKAEEEFNI EKGRLVQTQR LKIMEYYEKK
EKQIEQQKKI QMSNLMNQAR LKVLRARDDL ITDLLNEAKQ RLSKVVKDTT RYQVLLDGLV
LQGLYQLLEP RMIVRCRKQD FPLVKAAVQK AIPMYKIATK NDVDVQIDQE SYLPEDIAGG
VEIYNGDRKI KVSNTLESRL DLIAQQMMPE VRGALFGANA NRKFLD
//
MIM
108746
*RECORD*
*FIELD* NO
108746
*FIELD* TI
*108746 ATPase, H+ TRANSPORTING, LYSOSOMAL, 31-KD, V1 SUBUNIT E; ATP6V1E
;;ATPase, H+ TRANSPORTING, LYSOSOMAL, SUBUNIT E; ATP6E;;
read moreVACUOLAR PROTON PUMP, 31-KD SUBUNIT
*FIELD* TX
DESCRIPTION
The vacuolar-type H(+)-ATPase (V-ATPase) is responsible for the
acidification of endosomes, lysosomes, and other intracellular
organelles. It is also involved in hydrogen ion transport across the
plasma membrane into the extracellular space. The V-ATPase is a
multisubunit complex with cytosolic and transmembrane domains. The
cytosolic catalytic domain consists of 3 A subunits and 3 B subunits,
which bind and hydrolyze ATP, as well as regulatory accessory subunits
including C (603097), D (607028), and E.
CLONING
Van Hille et al. (1993) cloned subunit E from an osteoclastoma cDNA
library with probes developed by PCR from the bovine cDNA sequence. The
deduced 242-amino acid protein has a calculated molecular mass of about
26 kD and shares 99% homology with the bovine sequence. Northern blot
analysis revealed ubiquitous and comparable expression of a 1.6-kb
transcript.
Baud et al. (1994) isolated heterogeneous nuclear RNA from somatic cell
hybrids selected for their chromosome 22 content. Inter-Alu PCR
amplification yielded a series of human DNA fragments that detected
evolutionarily conserved sequences. The gene fragment closest to the
centromere, designated XEN61, was found to be present in 4 copies in 6
patients with the cat eye syndrome (115470), a disorder of known partial
trisomy of 22pter-q11.2. A fetal brain cDNA clone was identified with
XEN61 and completely sequenced. The deduced protein was the E subunit of
vacuolar H(+)-ATPase. This 31-kD component of a proton pump is essential
in eukaryotic cells because it both controls acidification of the
vacuolar system and provides it with its main protonmotive force. RT-PCR
experiments indicated that the corresponding mRNA is widely transcribed.
MAPPING
Puech et al. (1997) did comparative mapping of the human 22q11 region in
the mouse using 7 genes that had been ordered unambiguously by physical
mapping: cen--ATP6E--IDD (600594)--CLTD (601273)--TMVCF (602101)--GP1BB
(138720)--COMT (116790)--ARVCF (602269)--tel. The region containing
these genes was estimated to span about 1.5 Mb. Five of the 7 genes
(Idd, Gp1bb, Tmvcf, Arvcf, and Comt) were found to be located on mouse
chromosome 16. Atp6e mapped to the distal region of mouse chromosome 6.
In addition to MMU16 and MMU6, some loci from the 22q region were found
to be located on MMU10. Furthermore the genes that are located on mouse
chromosome 16 show a quite different relative organization from that in
humans. Puech et al. (1997) interpreted these results showing that
instability of the 22q11 region is not restricted to humans but may have
been present throughout evolution. The results underscore the importance
of detailed comparative mapping of genes in mice and humans as a
prerequisite for the development of mouse models of human diseases
involving chromosomal rearrangements, such as velocardiofacial syndrome
(192430) and DiGeorge syndrome (188400).
*FIELD* RF
1. Baud, V.; Mears, A. J.; Lamour, V.; Scamps, C.; Duncan, A. M. V.;
McDermid, H. E.; Lipinski, M.: The E subunit of vacuolar H(+)-ATPase
localizes close to the centromere on human chromosome 22. Hum. Molec.
Genet. 3: 335-339, 1994.
2. Puech, A.; Saint-Jore, B.; Funke, B.; Gilbert, D. J.; Sirotkin,
H.; Copeland, N. G.; Jenkins, N. A.; Kucherlapati, R.; Morrow, B.;
Skoultchi, A. I.: Comparative mapping of the human 22q11 chromosomal
region and the orthologous region in mice reveals complex changes
in gene organization. Proc. Nat. Acad. Sci. 94: 14608-14613, 1997.
3. van Hille, B.; Vanek, M.; Richener, H.; Green, J. R.; Bilbe, G.
: Cloning and tissue distribution of subunits C, D, and E of the human
vacuolar H(+)-ATPase. Biochem. Biophys. Res. Commun. 97: 15-21,
1993.
*FIELD* CN
Patricia A. Hartz - updated: 6/11/2002
Victor A. McKusick - updated: 2/6/1998
*FIELD* CD
Victor A. McKusick: 5/2/1994
*FIELD* ED
carol: 06/11/2002
carol: 6/11/2002
psherman: 10/8/1998
mark: 2/15/1998
terry: 2/6/1998
carol: 5/2/1994
*RECORD*
*FIELD* NO
108746
*FIELD* TI
*108746 ATPase, H+ TRANSPORTING, LYSOSOMAL, 31-KD, V1 SUBUNIT E; ATP6V1E
;;ATPase, H+ TRANSPORTING, LYSOSOMAL, SUBUNIT E; ATP6E;;
read moreVACUOLAR PROTON PUMP, 31-KD SUBUNIT
*FIELD* TX
DESCRIPTION
The vacuolar-type H(+)-ATPase (V-ATPase) is responsible for the
acidification of endosomes, lysosomes, and other intracellular
organelles. It is also involved in hydrogen ion transport across the
plasma membrane into the extracellular space. The V-ATPase is a
multisubunit complex with cytosolic and transmembrane domains. The
cytosolic catalytic domain consists of 3 A subunits and 3 B subunits,
which bind and hydrolyze ATP, as well as regulatory accessory subunits
including C (603097), D (607028), and E.
CLONING
Van Hille et al. (1993) cloned subunit E from an osteoclastoma cDNA
library with probes developed by PCR from the bovine cDNA sequence. The
deduced 242-amino acid protein has a calculated molecular mass of about
26 kD and shares 99% homology with the bovine sequence. Northern blot
analysis revealed ubiquitous and comparable expression of a 1.6-kb
transcript.
Baud et al. (1994) isolated heterogeneous nuclear RNA from somatic cell
hybrids selected for their chromosome 22 content. Inter-Alu PCR
amplification yielded a series of human DNA fragments that detected
evolutionarily conserved sequences. The gene fragment closest to the
centromere, designated XEN61, was found to be present in 4 copies in 6
patients with the cat eye syndrome (115470), a disorder of known partial
trisomy of 22pter-q11.2. A fetal brain cDNA clone was identified with
XEN61 and completely sequenced. The deduced protein was the E subunit of
vacuolar H(+)-ATPase. This 31-kD component of a proton pump is essential
in eukaryotic cells because it both controls acidification of the
vacuolar system and provides it with its main protonmotive force. RT-PCR
experiments indicated that the corresponding mRNA is widely transcribed.
MAPPING
Puech et al. (1997) did comparative mapping of the human 22q11 region in
the mouse using 7 genes that had been ordered unambiguously by physical
mapping: cen--ATP6E--IDD (600594)--CLTD (601273)--TMVCF (602101)--GP1BB
(138720)--COMT (116790)--ARVCF (602269)--tel. The region containing
these genes was estimated to span about 1.5 Mb. Five of the 7 genes
(Idd, Gp1bb, Tmvcf, Arvcf, and Comt) were found to be located on mouse
chromosome 16. Atp6e mapped to the distal region of mouse chromosome 6.
In addition to MMU16 and MMU6, some loci from the 22q region were found
to be located on MMU10. Furthermore the genes that are located on mouse
chromosome 16 show a quite different relative organization from that in
humans. Puech et al. (1997) interpreted these results showing that
instability of the 22q11 region is not restricted to humans but may have
been present throughout evolution. The results underscore the importance
of detailed comparative mapping of genes in mice and humans as a
prerequisite for the development of mouse models of human diseases
involving chromosomal rearrangements, such as velocardiofacial syndrome
(192430) and DiGeorge syndrome (188400).
*FIELD* RF
1. Baud, V.; Mears, A. J.; Lamour, V.; Scamps, C.; Duncan, A. M. V.;
McDermid, H. E.; Lipinski, M.: The E subunit of vacuolar H(+)-ATPase
localizes close to the centromere on human chromosome 22. Hum. Molec.
Genet. 3: 335-339, 1994.
2. Puech, A.; Saint-Jore, B.; Funke, B.; Gilbert, D. J.; Sirotkin,
H.; Copeland, N. G.; Jenkins, N. A.; Kucherlapati, R.; Morrow, B.;
Skoultchi, A. I.: Comparative mapping of the human 22q11 chromosomal
region and the orthologous region in mice reveals complex changes
in gene organization. Proc. Nat. Acad. Sci. 94: 14608-14613, 1997.
3. van Hille, B.; Vanek, M.; Richener, H.; Green, J. R.; Bilbe, G.
: Cloning and tissue distribution of subunits C, D, and E of the human
vacuolar H(+)-ATPase. Biochem. Biophys. Res. Commun. 97: 15-21,
1993.
*FIELD* CN
Patricia A. Hartz - updated: 6/11/2002
Victor A. McKusick - updated: 2/6/1998
*FIELD* CD
Victor A. McKusick: 5/2/1994
*FIELD* ED
carol: 06/11/2002
carol: 6/11/2002
psherman: 10/8/1998
mark: 2/15/1998
terry: 2/6/1998
carol: 5/2/1994