ID   VATL_MAIZE              Reviewed;         109 AA.
AC   Q41773; Q08074; Q41774;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   25-MAY-2022, entry version 130.
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;
DE   Flags: Fragment;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-76.
RC   STRAIN=cv. Lixis; TISSUE=Coleoptile;
RX   PubMed=8617373; DOI=10.1016/0014-5793(96)00336-5;
RA   Viereck R., Kirsch M., Loew R., Rausch T.;
RT   "Down-regulation of plant V-type H+ -ATPase genes after light-induced
RT   inhibition of growth.";
RL   FEBS Lett. 384:285-288(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 52-109.
RC   STRAIN=cv. B73; TISSUE=Leaf;
RX   PubMed=8278499; DOI=10.1104/pp.101.1.329;
RA   Keith C.S., Hoang D.O., Barrett B.M., Feigelman B., Nelson M.C., Thai H.,
RA   Baysdorfer C.;
RT   "Partial sequence analysis of 130 randomly selected maize cDNA clones.";
RL   Plant Physiol. 101:329-332(1993).
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       Note=Tonoplast.
CC   -!- TISSUE SPECIFICITY: High expression in the mesocotyl tip of etiolated
CC       seedlings compared to the base.
CC   -!- DEVELOPMENTAL STAGE: Expression is strongly linked to extension growth.
CC   -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC       {ECO:0000305}.
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DR   EMBL; X92375; CAA63119.1; -; mRNA.
DR   EMBL; X92374; CAA63118.1; -; mRNA.
DR   EMBL; M95063; AAA18550.1; -; mRNA.
DR   PIR; S65527; S65527.
DR   AlphaFoldDB; Q41773; -.
DR   SMR; Q41773; -.
DR   STRING; 4577.AC216067.3_FGP002; -.
DR   PaxDb; Q41773; -.
DR   eggNOG; KOG0232; Eukaryota.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; Q41773; baseline and differential.
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; 1.
DR   PRINTS; PR00122; VACATPASE.
DR   SUPFAM; SSF81333; SSF81333; 1.
DR   TIGRFAMs; TIGR01100; V_ATP_synt_C; 1.
PE   2: Evidence at transcript level;
KW   Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport; Vacuole.
FT   CHAIN           <1..109
FT                   /note="V-type proton ATPase 16 kDa proteolipid subunit"
FT                   /id="PRO_0000071771"
FT   TRANSMEM        <1..20
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        21..39
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        40..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        62..73
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        74..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        100..109
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   SITE            86
FT                   /note="Essential for proton translocation"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        52
FT                   /note="A -> P (in Ref. 1; CAA63119/CAA63118)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        63
FT                   /note="A -> G (in Ref. 1; CAA63119)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
SQ   SEQUENCE   109 AA;  11043 MW;  6B7518DD7A0FEB62 CRC64;
     VPVVMAGVLG IYGLIIAVII STGINPKAKP YYLFDGYAHL SSGLACGLAG LAAGMAIGIV
     GDAGVRANAQ QPKLFVGMIL ILIFAEALAL YGLIVGIILS SRAGQSRAD