VATL_AVESA
ID VATL_AVESA Reviewed; 165 AA.
AC P23957;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 25-MAY-2022, entry version 96.
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=VATP-P1;
OS Avena sativa (Oat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Poodae; Poeae; Aveninae; Avena.
OX NCBI_TaxID=4498;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Lang;
RX PubMed=1831453; DOI=10.1016/s0021-9258(18)98518-2;
RA Lai S., Watson J.C., Hansen J.N., Sze H.;
RT "Molecular cloning and sequencing of cDNAs encoding the proteolipid subunit
RT of the vacuolar H(+)-ATPase from a higher plant.";
RL J. Biol. Chem. 266:16078-16084(1991).
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 -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC {ECO:0000305}.
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DR EMBL; M73232; AAA32712.1; -; mRNA.
DR PIR; A40814; A40814.
DR AlphaFoldDB; P23957; -.
DR SMR; P23957; -.
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; 2.
DR TIGRFAMs; TIGR01100; V_ATP_synt_C; 1.
PE 2: Evidence at transcript level;
KW Hydrogen ion transport; Ion transport; Membrane; Transmembrane;
KW Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..165
FT /note="V-type proton ATPase 16 kDa proteolipid subunit"
FT /id="PRO_0000071766"
FT TOPO_DOM 1..10
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..55
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..95
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..165
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT SITE 142
FT /note="Essential for proton translocation"
FT /evidence="ECO:0000250"
FT VARIANT 78
FT /note="T -> P (in clone 12)"
FT VARIANT 89
FT /note="L -> P (in clone 12)"
FT VARIANT 164
FT /note="A -> V (in clone 93)"
SQ SEQUENCE 165 AA; 16621 MW; 900A664C6C1965BB CRC64;
MSSVFSGDET APFFGFLGAA AALVFSCMGA AYGTAKSGVG VASMGVMRPE LVMKSIVPVV
MAGVLGIYGL IIAVIISTGI NPKAKPYFLF DGYAHLSSGL ACGLAGLAAG MAIGIVGDAG
VRANAQQPKL FVGMILILIF AEALALYGLI VGIILSSRAG QSRAD
