VATE1_RAT
ID VATE1_RAT Reviewed; 226 AA.
AC Q6PCU2;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=V-type proton ATPase subunit E 1;
DE Short=V-ATPase subunit E 1;
DE AltName: Full=Vacuolar proton pump subunit E 1;
GN Name=Atp6v1e1;
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 [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 [2]
RP PROTEIN SEQUENCE OF 53-59; 70-80; 86-99; 112-131; 139-145 AND 192-222, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
RA Lubec G., Chen W.-Q., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [3] {ECO:0007744|PDB:6VQ6, ECO:0007744|PDB:6VQ7, ECO:0007744|PDB:6VQ8, ECO:0007744|PDB:6VQ9, ECO:0007744|PDB:6VQA, ECO:0007744|PDB:6VQB, ECO:0007744|PDB:6VQI, ECO:0007744|PDB:6VQJ, ECO:0007744|PDB:6VQK}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, IDENTIFICATION
RP IN THE V-ATPASE COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=32165585; DOI=10.1126/science.aaz2924;
RA Abbas Y.M., Wu D., Bueler S.A., Robinson C.V., Rubinstein J.L.;
RT "Structure of V-ATPase from the mammalian brain.";
RL Science 367:1240-1246(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:32165585). 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:32165585).
CC {ECO:0000269|PubMed:32165585}.
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:32165585). 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:32165585). 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:32165585). 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:32165585}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:P36543}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle membrane {ECO:0000269|PubMed:32165585}; Peripheral
CC membrane protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated
CC vesicle membrane {ECO:0000269|PubMed:32165585}; Peripheral membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level).
CC {ECO:0000269|PubMed:32165585}.
CC -!- SIMILARITY: Belongs to the V-ATPase E subunit family. {ECO:0000305}.
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DR EMBL; BC059155; AAH59155.1; -; mRNA.
DR RefSeq; NP_942040.1; NM_198745.2.
DR PDB; 6VQ6; EM; 3.90 A; I/J/K=1-226.
DR PDB; 6VQ7; EM; 4.00 A; I/J/K=1-226.
DR PDB; 6VQ8; EM; 3.90 A; I/J/K=1-226.
DR PDB; 6VQ9; EM; 3.60 A; I/J/K=1-226.
DR PDB; 6VQA; EM; 3.70 A; I/J/K=1-226.
DR PDB; 6VQB; EM; 3.60 A; I/J/K=1-226.
DR PDB; 6VQI; EM; 4.30 A; I/J/K=1-226.
DR PDB; 6VQJ; EM; 5.70 A; I/J/K=1-226.
DR PDB; 6VQK; EM; 5.70 A; I/J/K=1-226.
DR PDBsum; 6VQ6; -.
DR PDBsum; 6VQ7; -.
DR PDBsum; 6VQ8; -.
DR PDBsum; 6VQ9; -.
DR PDBsum; 6VQA; -.
DR PDBsum; 6VQB; -.
DR PDBsum; 6VQI; -.
DR PDBsum; 6VQJ; -.
DR PDBsum; 6VQK; -.
DR AlphaFoldDB; Q6PCU2; -.
DR SMR; Q6PCU2; -.
DR BioGRID; 255610; 3.
DR IntAct; Q6PCU2; 6.
DR MINT; Q6PCU2; -.
DR STRING; 10116.ENSRNOP00000016495; -.
DR iPTMnet; Q6PCU2; -.
DR PhosphoSitePlus; Q6PCU2; -.
DR SwissPalm; Q6PCU2; -.
DR jPOST; Q6PCU2; -.
DR PaxDb; Q6PCU2; -.
DR PRIDE; Q6PCU2; -.
DR GeneID; 297566; -.
DR KEGG; rno:297566; -.
DR UCSC; RGD:735157; rat.
DR CTD; 529; -.
DR RGD; 735157; Atp6v1e1.
DR eggNOG; KOG1664; Eukaryota.
DR InParanoid; Q6PCU2; -.
DR OrthoDB; 1489718at2759; -.
DR PhylomeDB; Q6PCU2; -.
DR Reactome; R-RNO-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-RNO-77387; Insulin receptor recycling.
DR Reactome; R-RNO-917977; Transferrin endocytosis and recycling.
DR Reactome; R-RNO-9639288; Amino acids regulate mTORC1.
DR Reactome; R-RNO-983712; Ion channel transport.
DR PRO; PR:Q6PCU2; -.
DR Proteomes; UP000002494; Unplaced.
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:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0005902; C:microvillus; ISO:RGD.
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:0051117; F:ATPase binding; ISO:RGD.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; ISO:RGD.
DR GO; GO:1902600; P:proton transmembrane transport; ISO:RGD.
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 Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane;
KW Phosphoprotein; 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_0000282342"
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"
SQ SEQUENCE 226 AA; 26128 MW; 5DCAAC2C77F09A08 CRC64;
MALSDADVQK QIKHMMAFIE QEANEKAEEI DAKAEEEFNI EKGRLVQTQR LKIMEYYEKK
EKQIEQQKKI QMSNLMNQAR LKVLRARDDL ITDLLNEAKQ RLSKVVKDTT RYQVLLDGLV
LQGLYQLLEP RMIVRCRKQD FPLVKAAVQK AIPMYKIATK KDVDVQIDLE AYLPEDIAGG
VEIYNGDRKI KVSNTLESRL DLIAQQMMPE VRGALFGANA NRKFLD
