VATL_CHRCT
ID VATL_CHRCT Reviewed; 164 AA.
AC Q43362; O04754;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 94.
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=VAP;
OS Chrysotila carterae (Marine alga) (Syracosphaera carterae).
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Isochrysidales;
OC Isochrysidaceae; Chrysotila.
OX NCBI_TaxID=13221;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=136;
RA Corstjens P.L.A.M., Araki Y., Westbroek P., Gonzalez E.L.;
RT "A gene encoding the 16 kD proteolipid subunit of a vacuolar-type H(+)-
RT ATPase from Pleurochrysis carterae strain 136.";
RL (er) Plant Gene Register PGR96-038(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=136;
RA Corstjens P.L.A.M., Gonzalez E.L.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U48365; AAB67833.1; -; mRNA.
DR EMBL; U53182; AAB67834.1; -; mRNA.
DR EMBL; U81519; AAB58498.1; -; Transcribed_RNA.
DR AlphaFoldDB; Q43362; -.
DR SMR; Q43362; -.
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..164
FT /note="V-type proton ATPase 16 kDa proteolipid subunit"
FT /id="PRO_0000071775"
FT TOPO_DOM 1..10
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..53
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..96
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..164
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT SITE 143
FT /note="Essential for proton translocation"
FT /evidence="ECO:0000250"
SQ SEQUENCE 164 AA; 16252 MW; B9723D4A2CF8A964 CRC64;
MSDLCPPTAP FFGFMGAAVA LIFANLGAAY GTAKSGVGVS SMGVMKPDLV MKSIIPVVMA
GVLGIYGLII AVIIGNGVKG PEGGKPQYSS FTGFAHLAAG LACGLSGMAA GIAIGIVGDA
GVRASAQQAK LYVGMVLILI FAEALGLYGL IVGLILTSKE APCS
