ID A0A2T7PZE2_POMCA Unreviewed; 869 AA.
AC A0A2T7PZE2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 22-FEB-2023, entry version 15.
DE RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN ORFNames=C0Q70_01393 {ECO:0000313|EMBL:PVD38770.1};
OS Pomacea canaliculata (Golden apple snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD38770.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD38770.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD38770.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD38770.1};
RA Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA Zhang G., Qian W., Fan W.;
RT "The genome of golden apple snail Pomacea canaliculata provides insight
RT into stress tolerance and invasive adaptation.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential component of the vacuolar proton pump (V-ATPase), a
CC multimeric enzyme that catalyzes the translocation of protons across
CC the membranes. Required for assembly and activity of the V-ATPase.
CC {ECO:0000256|RuleBase:RU361189}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00009904, ECO:0000256|RuleBase:RU361189}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PVD38770.1}.
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DR EMBL; PZQS01000001; PVD38770.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7PZE2; -.
DR STRING; 400727.A0A2T7PZE2; -.
DR Proteomes; UP000245119; Miscellaneous, Linkage group lg1.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR InterPro; IPR002490; V-ATPase_116kDa_su.
DR InterPro; IPR026028; V-type_ATPase_116kDa_su_euka.
DR PANTHER; PTHR11629:SF63; V-TYPE PROTON ATPASE SUBUNIT A; 1.
DR PANTHER; PTHR11629; VACUOLAR PROTON ATPASES; 1.
DR Pfam; PF01496; V_ATPase_I; 1.
DR PIRSF; PIRSF001293; ATP6V0A1; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW ECO:0000256|RuleBase:RU361189};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU361189};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361189};
KW Reference proteome {ECO:0000313|Proteomes:UP000245119};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361189};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361189};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU361189}.
FT TRANSMEM 406..430
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 451..469
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 533..554
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 566..586
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 646..665
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 798..822
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT COILED 43..134
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 869 AA; 99895 MW; 345F316065F9BD10 CRC64;
MSIFRSEEMA LCQLFLQSEA AYACVSELGE IGIVQFKDLN PNVNAFQRKF VNEIRRCEEM
ERKLRYVEKE IRKQKLNIYD RGENPKAPAP KEMVDLEATF EKIESELREV NTNNEALKRN
SQELSELKEV MTKTQLFLHT HGEDLHSMVD DMHHETAPEE SAITTGHAAS IQLGFVAGVI
PREKMPGFER LLWFACRGNV FLRHEEIMQP LEDPVTGDPI HKSVFIIFFQ GEQLKSKVKK
ICEGFKATLY PCPEAPQERE EMLKGVNTRL YDLKTVLSQT EEHRSRVLVA AQKEIRSWMI
KVEKIKAIYH TLNMFNFDVS QNSLIAECWC PVNALDDIRA ALKTGEKISG SNVPSIIQTM
RTKKAPPTYF KTNKFTNGFQ NIVSAYGVAT YLEVNPSLYT IITFPFLFAI MFGDAGHGFI
MFLFGLWMVV TERQHMAKRS TNEIWNTFFG GRYIIMFMGL FSIYTGMIYN DVFSKSTNIF
GSSCENALEN NEMLTLDPLI SFRKHYPYPI GVDPVWQPAK NKIAFLNSLK MKLAVIIGIT
QMFFGICLSF FNHLHFRHYL SIFVEFIPEC IFLLCLFGYL VALIFLKWAT IQTEDSQCSP
ALLIHYINMF MMTYVQVPER NSTDYALKVK CSQWIIYDGQ QPLQTAFVIS AVLCIPILLL
VKPFVERAQH KKKMRMAAHL GATSRDALLQ NEITPDAVNP GFERDKTDNV SINRSSPSGD
VEAANRTHIV MEDDEEEEFD FGEVFIHQAI HTIEFCLGCI SHTASYLRLW ALSLAHAQLS
EVLWQMVFSL GLKMDMKYAG CIPVFILWFF WANLTVAVLL LMEGLSAFLH TLRLHWVEFQ
SKFYKGEGYI FQPFGFKEIL KMDSLEESK
//