ID   VATL_KALDA              Reviewed;         165 AA.
AC   Q96473;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=V-type proton ATPase 16 kDa proteolipid subunit;
DE            Short=V-ATPase 16 kDa proteolipid subunit;
DE   AltName: Full=V-type H(+)-ATPase 16 kDa subunit;
DE   AltName: Full=Vacuolar proton pump 16 kDa proteolipid subunit;
OS   Kalanchoe daigremontiana (Devil's backbone) (Bryophyllum daigremontianum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Saxifragales; Crassulaceae; Kalanchoe.
OX   NCBI_TaxID=23013;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RX   PubMed=8756609; DOI=10.1007/bf00021806;
RA   Bartholomew D.M., Rees D.J.G., Rambaut A., Smith J.A.C.;
RT   "Isolation and sequence analysis of a cDNA encoding the c subunit of a
RT   vacuolar-type H(+)-ATPase from the CAM plant Kalanchoe daigremontiana.";
RL   Plant Mol. Biol. 31:435-442(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       Necessary for the crassulacean acid metabolism.
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: Higher expression in leaves, followed by roots and
CC       weakly in flowers. Expression in leaves is light-dependent.
CC   -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC       {ECO:0000305}.
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DR   EMBL; U16244; AAC49473.1; -; mRNA.
DR   AlphaFoldDB; Q96473; -.
DR   SMR; Q96473; -.
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_0000071769"
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"
SQ   SEQUENCE   165 AA;  16645 MW;  4B14844F9FB6BE18 CRC64;
     MSSTFSGDET APFFGFLGAA AALVFSCMGA AYGTAKSGVG VASMGVMRPE LVMKSIVPVV
     MAGVLGIYGL IIAVIISTGI NPKAKSYYLF DGYAHLSSGL ACGLAGLSAG MAIGIVGDAG
     VRANAQQPKL FVGMILILIF AEALALYGLI VGIILSSRAG QSRAD