VATL_ENTHI
ID VATL_ENTHI Reviewed; 177 AA.
AC Q24810;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=V-type proton ATPase 16 kDa proteolipid subunit;
DE Short=V-ATPase 16 kDa proteolipid subunit;
DE AltName: Full=Vacuolar proton pump 16 kDa proteolipid subunit;
GN Name=VMA3;
OS Entamoeba histolytica.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=5759;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 30459 / HM-1:IMSS;
RX PubMed=8039932; DOI=10.1128/iai.62.8.3572-3575.1994;
RA Descoteaux S., Yu Y., Samuelson J.;
RT "Cloning of Entamoeba genes encoding proteolipids of putative vacuolar
RT proton-translocating ATPases.";
RL Infect. Immun. 62:3572-3575(1994).
CC -!- FUNCTION: Proton-conducting pore forming subunit of the membrane
CC integral V0 complex of vacuolar ATPase. V-ATPase is responsible for
CC acidifying a variety of intracellular compartments in eukaryotic cells.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC catalytic V1 complex (main components: subunits A, B, C, D, E, and F)
CC attached to an integral membrane V0 proton pore complex (main
CC component: the proteolipid protein; which is present as a hexamer that
CC forms the proton-conducting pore).
CC -!- SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC {ECO:0000305}.
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DR EMBL; U01057; AAA21450.1; -; Genomic_DNA.
DR AlphaFoldDB; Q24810; -.
DR SMR; Q24810; -.
DR STRING; 5759.rna_EHI_059840-1; -.
DR VEuPathDB; AmoebaDB:EHI5A_153590; -.
DR VEuPathDB; AmoebaDB:EHI8A_149890; -.
DR VEuPathDB; AmoebaDB:EHI_059840; -.
DR VEuPathDB; AmoebaDB:KM1_213470; -.
DR eggNOG; KOG0232; Eukaryota.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR Gene3D; 1.20.120.610; -; 1.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR000245; ATPase_proteolipid_csu.
DR InterPro; IPR011555; ATPase_proteolipid_su_C_euk.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR Pfam; PF00137; ATP-synt_C; 2.
DR PRINTS; PR00122; VACATPASE.
DR SUPFAM; SSF81333; SSF81333; 1.
DR TIGRFAMs; TIGR01100; V_ATP_synt_C; 1.
PE 3: Inferred from homology;
KW Hydrogen ion transport; Ion transport; Membrane; Transmembrane;
KW Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..177
FT /note="V-type proton ATPase 16 kDa proteolipid subunit"
FT /id="PRO_0000071755"
FT TOPO_DOM 1..19
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..100
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..177
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT SITE 147
FT /note="Essential for proton translocation"
FT /evidence="ECO:0000250"
SQ SEQUENCE 177 AA; 18132 MW; 32521191B721FB52 CRC64;
MLMSILLRSV TELCPVYPPF FGSMGITASI VFTVFGGAYG TAKSSVGISS VGVMKPEFIV
RSVAPVVFAG IIGLYGLIVC ILLFINVTKS EYSLNRAFLD LGAGLTCGLC GLASGMAIGI
SGDCGVRGAA QQPKLFVGML ICLIFSEALA LYGFIVALIM ASTGENSCVA TASSSSA
