ID   VATL_GOSHI              Reviewed;         165 AA.
AC   Q43434; Q43435;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=CVA16-2;
GN   and
GN   Name=CVA16-4;
OS   Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=3635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Acala SJ2; TISSUE=Ovule;
RX   PubMed=7659746; DOI=10.1104/pp.108.4.1395;
RA   Hasenfratz M.P., Tsou C.L., Wilkins T.A.;
RT   "Expression of two related vacuolar H(+)-ATPase 16-kilodalton proteolipid
RT   genes is differentially regulated in a tissue-specific manner.";
RL   Plant Physiol. 108:1395-1404(1995).
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   -!- DEVELOPMENTAL STAGE: Increases dramatically in tissues undergoing rapid
CC       expansion, particularly in anthers, ovules, and petals.
CC   -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC       {ECO:0000305}.
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DR   EMBL; U13669; AAA82976.1; -; mRNA.
DR   EMBL; U13670; AAA82977.1; -; mRNA.
DR   RefSeq; XP_016679572.1; XM_016824083.1.
DR   RefSeq; XP_016685356.1; XM_016829867.1.
DR   RefSeq; XP_016692439.1; XM_016836950.1.
DR   RefSeq; XP_016705796.1; XM_016850307.1.
DR   RefSeq; XP_016724823.1; XM_016869334.1.
DR   RefSeq; XP_016739293.1; XM_016883804.1.
DR   AlphaFoldDB; Q43434; -.
DR   SMR; Q43434; -.
DR   STRING; 3635.Q43434; -.
DR   GeneID; 107903720; -.
DR   GeneID; 107909439; -.
DR   GeneID; 107920550; -.
DR   GeneID; 107936576; -.
DR   GeneID; 107949088; -.
DR   KEGG; ghi:107903720; -.
DR   KEGG; ghi:107909439; -.
DR   KEGG; ghi:107920550; -.
DR   KEGG; ghi:107936576; -.
DR   KEGG; ghi:107949088; -.
DR   OMA; MSVCPPY; -.
DR   Proteomes; UP000189702; Chromosome 17.
DR   Proteomes; UP000189702; Chromosome 19.
DR   Proteomes; UP000189702; Chromosome 20.
DR   Proteomes; UP000189702; Chromosome 24.
DR   Proteomes; UP000189702; Chromosome 6.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
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; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport; Vacuole.
FT   CHAIN           1..165
FT                   /note="V-type proton ATPase 16 kDa proteolipid subunit"
FT                   /id="PRO_0000071768"
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         3
FT                   /note="S -> T (in CVA16-4)"
SQ   SEQUENCE   165 AA;  16659 MW;  4AA4844F9FB6BE18 CRC64;
     MSSTFSGDET APFFGFLGAA AALVFSCMGA AYGTAKSGVG VASMGVMRPE LVMKSIVPVV
     MAGVLGIYGL IIAVIISTGI NPKAKSYYLF DGYAHLSSGL ACGLAGLSAG MAIGIVGDAG
     VRANAQQPKL FVGMILILIF AEALALYGLI VGIILSSRAG QSRAE