ID A0A2A2L037_9BILA Unreviewed; 381 AA.
AC A0A2A2L037;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 22-FEB-2023, entry version 14.
DE RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN ORFNames=WR25_08314 {ECO:0000313|EMBL:PAV79512.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV79512.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV79512.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV79512.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
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:PAV79512.1}.
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; LIAE01007405; PAV79512.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2L037; -.
DR STRING; 2018661.A0A2A2L037; -.
DR Proteomes; UP000218231; Unassembled WGS sequence.
DR GO; GO:0033179; C: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 PANTHER; PTHR11629:SF63; V-TYPE PROTON ATPASE SUBUNIT A; 1.
DR PANTHER; PTHR11629; VACUOLAR PROTON ATPASES; 1.
DR Pfam; PF01496; V_ATPase_I; 2.
PE 3: Inferred from homology;
KW Hydrogen ion transport {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:UP000218231};
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 37..58
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 70..93
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 127..148
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 169..190
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 308..333
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
SQ SEQUENCE 381 AA; 43722 MW; 60729D0D13D3C4A7 CRC64;
MKMKMSVLLG IAQMTFGLIL SFYNHKYFKS DLDIKFMFIP QMLFLSCIFI YLCLEIIVKW
LFFSWEGGSV LGYTYPGASC APSLLIGLIN MFMMKSRPSG FVNEKGETVP QCYLNFWYPG
QSFFEPLFVL VAIACVPVML FAKPYILWKE EKERLASGHR QLVSRIAPRR YVETVLFVVA
LMSVPVMLFV KPGLEILRHQ KAAKYQLIRQ QQSVRADMNG DEAEVVHADE QTQNHQPKSH
DGGHGHGDGP FNMGDIMVYQ AIHTIEFVLG CVSHTASYLR LWALSLAHAQ LSEVLWKMVF
AHAFSVEGYM GAIVTYVLFF IFAFLSVFIL VLMEGLSAFL HALRLHWVEF QSKFYRGEGY
PFTPFSFEKI LEEERALEEQ L
//
