VATE1_BOVIN
ID VATE1_BOVIN Reviewed; 226 AA.
AC P11019; Q3T009;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 131.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=2896353; DOI=10.1073/pnas.85.9.3004;
RA Hirsch S., Strauss A., Masood K., Lee S., Sukhatme V., Gluck S.;
RT "Isolation and sequence of a cDNA clone encoding the 31-kDa subunit of
RT bovine kidney vacuolar H+-ATPase.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:3004-3008(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0007744|PDB:6XBW, ECO:0007744|PDB:6XBY}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.37 ANGSTROMS), FUNCTION, IDENTIFICATION
RP IN THE V-ATPASE COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=32764564; DOI=10.1038/s41467-020-17762-9;
RA Wang R., Long T., Hassan A., Wang J., Sun Y., Xie X.S., Li X.;
RT "Cryo-EM structures of intact V-ATPase from bovine brain.";
RL Nat. Commun. 11:3921-3921(2020).
CC -!- FUNCTION: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase),
CC a multisubunit enzyme composed of a peripheral complex (V1) that
CC hydrolyzes ATP and a membrane integral complex (V0) that translocates
CC protons (PubMed:32764564). V-ATPase is responsible for acidifying and
CC maintaining the pH of intracellular compartments and in some cell
CC types, is targeted to the plasma membrane, where it is responsible for
CC acidifying the extracellular environment (PubMed:32764564).
CC {ECO:0000269|PubMed:32764564}.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme made up of two
CC complexes: the ATP-hydrolytic V1 complex and the proton translocation
CC V0 complex (PubMed:32764564). The V1 complex consists of three
CC catalytic AB heterodimers that form a heterohexamer, three peripheral
CC stalks each consisting of EG heterodimers, one central rotor including
CC subunits D and F, and the regulatory subunits C and H
CC (PubMed:32764564). The proton translocation complex V0 consists of the
CC proton transport subunit a, a ring of proteolipid subunits c9c'',
CC rotary subunit d, subunits e and f, and the accessory subunits
CC ATP6AP1/Ac45 and ATP6AP2/PRR (PubMed:32764564). Interacts with
CC RABL2/RABL2A; binds preferentially to GTP-bound RABL2 (By similarity).
CC Interacts with ALDOC (By similarity). Interacts with RAB11B (By
CC similarity). {ECO:0000250|UniProtKB:P36543,
CC ECO:0000250|UniProtKB:P50518, ECO:0000269|PubMed:32764564}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:P36543}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle membrane {ECO:0000250|UniProtKB:Q6PCU2}; Peripheral
CC membrane protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated
CC vesicle membrane {ECO:0000269|PubMed:32764564}; Peripheral membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level).
CC {ECO:0000269|PubMed:32764564}.
CC -!- SIMILARITY: Belongs to the V-ATPase E subunit family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J03244; AAA30562.1; -; mRNA.
DR EMBL; BC102616; AAI02617.1; -; mRNA.
DR PIR; A31335; A31335.
DR RefSeq; NP_777235.1; NM_174810.2.
DR PDB; 6XBW; EM; 3.37 A; I/J/K=1-226.
DR PDB; 6XBY; EM; 3.79 A; I/J/K=1-226.
DR PDB; 7KHR; EM; 3.62 A; I/J/K=1-226.
DR PDBsum; 6XBW; -.
DR PDBsum; 6XBY; -.
DR PDBsum; 7KHR; -.
DR AlphaFoldDB; P11019; -.
DR SMR; P11019; -.
DR CORUM; P11019; -.
DR STRING; 9913.ENSBTAP00000037526; -.
DR PaxDb; P11019; -.
DR PeptideAtlas; P11019; -.
DR PRIDE; P11019; -.
DR Ensembl; ENSBTAT00000037702; ENSBTAP00000037526; ENSBTAG00000014238.
DR GeneID; 287017; -.
DR KEGG; bta:287017; -.
DR CTD; 529; -.
DR VEuPathDB; HostDB:ENSBTAG00000014238; -.
DR VGNC; VGNC:26322; ATP6V1E1.
DR eggNOG; KOG1664; Eukaryota.
DR GeneTree; ENSGT00390000002730; -.
DR InParanoid; P11019; -.
DR OMA; AIDTQYE; -.
DR OrthoDB; 1489718at2759; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000014238; Expressed in Ammon's horn and 101 other tissues.
DR ExpressionAtlas; P11019; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IDA:UniProtKB.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
DR GO; GO:0045851; P:pH reduction; IC:UniProtKB.
DR GO; GO:1902600; P:proton transmembrane transport; IC:UniProtKB.
DR Gene3D; 3.30.2320.30; -; 1.
DR HAMAP; MF_00311; ATP_synth_E_arch; 1.
DR InterPro; IPR038495; ATPase_E_C.
DR InterPro; IPR002842; ATPase_V1_Esu.
DR PANTHER; PTHR45715; PTHR45715; 1.
DR Pfam; PF01991; vATP-synt_E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell membrane; Cytoplasmic vesicle;
KW Hydrogen ion transport; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Synapse; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P36543"
FT CHAIN 2..226
FT /note="V-type proton ATPase subunit E 1"
FT /id="PRO_0000117294"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P36543"
FT MOD_RES 56
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P50518"
FT CONFLICT 181
FT /note="V -> D (in Ref. 2; AAI02617)"
FT /evidence="ECO:0000305"
FT HELIX 7..25
FT /evidence="ECO:0007829|PDB:6XBW"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 29..107
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 110..127
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 141..158
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 196..206
FT /evidence="ECO:0007829|PDB:6XBW"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:6XBW"
SQ SEQUENCE 226 AA; 26139 MW; 58D183C70C035898 CRC64;
MALSDADVQK QIKHMMAFIE QEANEKAEEI DAKAEEEFNI EKGRLVQTQR LKIMEYYEKK
EKQIEQQKKI QMSNLMNQAR LKVLRARDDL ITDLLNEAKQ RLSKVVKDTT RYQVLLDGLV
LQGLYQLLEP RMIVRCRKQD FPLVKAAVQK AIPVYKVATK RDVDVQIDQE AYLPEEIAGG
VEIYNGDRKI KVSNTLESRL DLIAQQMMPE VRGALFGANA NRKFLD
