VATL_MESCR
ID VATL_MESCR Reviewed; 165 AA.
AC P68161; Q39437;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 68.
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=VMAC1;
OS Mesembryanthemum crystallinum (Common ice plant) (Cryophytum crystallinum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Aizoaceae; Mesembryanthemum;
OC Mesembryanthemum subgen. Cryophytum.
OX NCBI_TaxID=3544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8653119; DOI=10.1046/j.1365-313x.1996.9050729.x;
RA Tsiantis M.S., Bartholomew D.M., Smith J.A.;
RT "Salt regulation of transcript levels for the c subunit of a leaf vacuolar
RT H(+)-ATPase in the halophyte Mesembryanthemum crystallinum.";
RL Plant J. 9:729-736(1996).
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; X94999; CAA64455.1; -; mRNA.
DR AlphaFoldDB; P68161; -.
DR SMR; P68161; -.
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_0000071772"
FT TOPO_DOM 1..12
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..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"
SQ SEQUENCE 165 AA; 16684 MW; 821F2471E9B97509 CRC64;
MSTVFNGDET APFFGFLGAA AALVFSCMGA AYGTAKSGVG VASMGVMRPE LVMKSIVPVV
MAGVLGIYGL IIAVIISTGI NPKAKSYYLF DGYAHLSSGL ACGLAGLSAG MAIGIVGDAG
VRANAQQPKL FVGMILILIF AEALALYGLI VGIILSSRAG QSRAD
