ID X6N2N1_RETFI Unreviewed; 334 AA.
AC X6N2N1;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 22-FEB-2023, entry version 19.
DE RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN ORFNames=RFI_16694 {ECO:0000313|EMBL:ETO20520.1};
OS Reticulomyxa filosa.
OC Eukaryota; Sar; Rhizaria; Retaria; Foraminifera; Monothalamids;
OC Reticulomyxidae; Reticulomyxa.
OX NCBI_TaxID=46433 {ECO:0000313|EMBL:ETO20520.1, ECO:0000313|Proteomes:UP000023152};
RN [1] {ECO:0000313|EMBL:ETO20520.1, ECO:0000313|Proteomes:UP000023152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24332546;
RA Glockner G., Hulsmann N., Schleicher M., Noegel A.A., Eichinger L.,
RA Gallinger C., Pawlowski J., Sierra R., Euteneuer U., Pillet L.,
RA Moustafa A., Platzer M., Groth M., Szafranski K., Schliwa M.;
RT "The Genome of the Foraminiferan Reticulomyxa filosa.";
RL Curr. Biol. 0:0-0(2013).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:ETO20520.1}.
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DR EMBL; ASPP01012520; ETO20520.1; -; Genomic_DNA.
DR AlphaFoldDB; X6N2N1; -.
DR EnsemblProtists; ETO20520; ETO20520; RFI_16694.
DR OrthoDB; 1967517at2759; -.
DR Proteomes; UP000023152; 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; 1.
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:UP000023152};
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 31..52
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 99..122
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 264..288
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
SQ SEQUENCE 334 AA; 38698 MW; F9AC8F9F6BA560AC CRC64;
MKLSVIIGVS QMTFGLFLKL FNHIQENNWI SILFEFIHQL IFMLCFFGYM VFYKWCINWS
TSTLPGTPSL ITVLIKMFLS PGTIDSEVQI FPNKDFQSII QVIFLLLLVF SIPTMLCVKP
LILKSRLSKH HHDHPFDEYN QEDSKKHSEF QILPLENYQP MDDESLHQHS RHDTDHKESH
EMKEIEYFKS VSSNVQHKDA HHDYRESFGD IVIHQFIHII EYVLGTISNI ASYLRLWALS
LAPAELSEVF FDKTLRITLE STGVGAVIMN VVSAGAFLMF TCGVLLIMDV LECFFRALCL
HWVEFQNNGK ASLPYENGIL LTKCIYSKTN FDNL
//
