ID   VATE1_MACFA             Reviewed;         226 AA.
AC   Q4R761;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 78.
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; ORFNames=QtsA-16227;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). 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 (By similarity).
CC       {ECO:0000250|UniProtKB:P36543}.
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 (By similarity). The V1 complex consists of three catalytic
CC       AB heterodimers that form a heterohexamer, three peripheral stalks each
CC       consisting of EG heterodimers, one central rotor including subunits D
CC       and F, and the regulatory subunits C and H (By similarity). The proton
CC       translocation complex V0 consists of the proton transport subunit a, a
CC       ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f,
CC       and the accessory subunits ATP6AP1/Ac45 and ATP6AP2/PRR (By
CC       similarity). Interacts with RABL2/RABL2A; binds preferentially to GTP-
CC       bound RABL2 (By similarity). Interacts with ALDOC (By similarity).
CC       Interacts with RAB11B (By similarity). {ECO:0000250|UniProtKB:P36543,
CC       ECO:0000250|UniProtKB:P50518}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000250|UniProtKB:P50518}; Peripheral membrane protein
CC       {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle
CC       membrane {ECO:0000250|UniProtKB:Q6PCU2}; Peripheral membrane protein
CC       {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle membrane
CC       {ECO:0000250|UniProtKB:Q6PCU2}; Peripheral membrane protein
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the V-ATPase E subunit family. {ECO:0000305}.
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DR   EMBL; AB168964; BAE01062.1; -; mRNA.
DR   RefSeq; NP_001270450.1; NM_001283521.1.
DR   AlphaFoldDB; Q4R761; -.
DR   SMR; Q4R761; -.
DR   STRING; 9541.XP_005568104.1; -.
DR   GeneID; 101866302; -.
DR   CTD; 529; -.
DR   VEuPathDB; HostDB:ENSMFAG00000032946; -.
DR   eggNOG; KOG1664; Eukaryota.
DR   OMA; AIDTQYE; -.
DR   OrthoDB; 1489718at2759; -.
DR   Proteomes; UP000233100; Chromosome 10.
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; ISS:UniProtKB.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Acetylation; Cell membrane; Cytoplasmic vesicle; Hydrogen ion transport;
KW   Ion transport; Membrane; Phosphoprotein; Reference proteome; Synapse;
KW   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_0000282341"
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;  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