VA0E2_RAT
ID VA0E2_RAT Reviewed; 81 AA.
AC Q5EB76;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=V-type proton ATPase subunit e 2;
DE Short=V-ATPase subunit e 2;
DE AltName: Full=Vacuolar proton pump subunit e 2;
GN Name=Atp6v0e2;
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=Brain;
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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
RN [3] {ECO:0007744|PDB:6VQ6, ECO:0007744|PDB:6VQ7, ECO:0007744|PDB:6VQ8, ECO:0007744|PDB:6VQC, ECO:0007744|PDB:6VQG, ECO:0007744|PDB:6VQH}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 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 V0 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).
CC {ECO:0000269|PubMed:32165585}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle
CC membrane {ECO:0000269|PubMed:32165585}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle
CC membrane {ECO:0000269|PubMed:32165585}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level).
CC {ECO:0000269|PubMed:32165585}.
CC -!- SIMILARITY: Belongs to the V-ATPase e1/e2 subunit family.
CC {ECO:0000305}.
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DR EMBL; BC089958; AAH89958.1; -; mRNA.
DR RefSeq; NP_001002253.1; NM_001002253.1.
DR PDB; 6VQ6; EM; 3.90 A; e=1-81.
DR PDB; 6VQ7; EM; 4.00 A; e=1-81.
DR PDB; 6VQ8; EM; 3.90 A; e=1-81.
DR PDB; 6VQC; EM; 3.80 A; e=1-81.
DR PDB; 6VQG; EM; 4.20 A; e=1-81.
DR PDB; 6VQH; EM; 4.40 A; e=1-81.
DR PDBsum; 6VQ6; -.
DR PDBsum; 6VQ7; -.
DR PDBsum; 6VQ8; -.
DR PDBsum; 6VQC; -.
DR PDBsum; 6VQG; -.
DR PDBsum; 6VQH; -.
DR AlphaFoldDB; Q5EB76; -.
DR SMR; Q5EB76; -.
DR IntAct; Q5EB76; 1.
DR STRING; 10116.ENSRNOP00000010853; -.
DR GlyGen; Q5EB76; 1 site, 4 N-linked glycans (1 site).
DR iPTMnet; Q5EB76; -.
DR PhosphoSitePlus; Q5EB76; -.
DR PaxDb; Q5EB76; -.
DR Ensembl; ENSRNOT00000010853; ENSRNOP00000010853; ENSRNOG00000008218.
DR GeneID; 436582; -.
DR KEGG; rno:436582; -.
DR UCSC; RGD:1303238; rat.
DR CTD; 155066; -.
DR RGD; 1303238; Atp6v0e2.
DR eggNOG; KOG3500; Eukaryota.
DR GeneTree; ENSGT00940000162476; -.
DR HOGENOM; CLU_170555_0_0_1; -.
DR InParanoid; Q5EB76; -.
DR OMA; YLQYYWE; -.
DR OrthoDB; 1613627at2759; -.
DR PhylomeDB; Q5EB76; -.
DR TreeFam; TF300290; -.
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:Q5EB76; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000008218; Expressed in frontal cortex and 19 other tissues.
DR Genevisible; Q5EB76; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; ISS:UniProtKB.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; ISO:RGD.
DR GO; GO:1902600; P:proton transmembrane transport; ISO:RGD.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR InterPro; IPR008389; ATPase_V0-cplx_e1/e2_su.
DR InterPro; IPR017385; ATPase_V0-cplx_e1/e2_su_met.
DR PANTHER; PTHR12263; PTHR12263; 1.
DR Pfam; PF05493; ATP_synt_H; 1.
DR PIRSF; PIRSF038097; V-ATP_synth_e1/e2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasmic vesicle; Glycoprotein; Hydrogen ion transport;
KW Ion transport; Membrane; Reference proteome; Synapse; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..81
FT /note="V-type proton ATPase subunit e 2"
FT /id="PRO_0000270201"
FT TOPO_DOM 1..7
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..81
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
SQ SEQUENCE 81 AA; 9198 MW; E84EC3CB4304BB45 CRC64;
MTAHSFALPV IIFTTFWGLI GIAGPWFVPK GPNRGVIITM LVATAVCCYL FWLIAILAQL
NPLFGPQLKN ETIWYVRFLW E
