ID A0A0N0P622_LEPSE Unreviewed; 775 AA.
AC A0A0N0P622;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 03-MAY-2023, entry version 25.
DE RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN ORFNames=ABL78_3779 {ECO:0000313|EMBL:KPI87126.1};
OS Leptomonas seymouri.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leptomonas.
OX NCBI_TaxID=5684 {ECO:0000313|EMBL:KPI87126.1, ECO:0000313|Proteomes:UP000038009};
RN [1] {ECO:0000313|EMBL:KPI87126.1, ECO:0000313|Proteomes:UP000038009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30220 {ECO:0000313|EMBL:KPI87126.1,
RC ECO:0000313|Proteomes:UP000038009};
RX PubMed=26317207;
RA Kraeva N., Butenko A., Hlavacova J., Kostygov A., Myskova J., Grybchuk D.,
RA Lestinova T., Votypka J., Volf P., Opperdoes F., Flegontov P., Lukes J.,
RA Yurchenko V.;
RT "Leptomonas seymouri: Adaptations to the Dixenous Life Cycle Analyzed by
RT Genome Sequencing, Transcriptome Profiling and Co-infection with Leishmania
RT donovani.";
RL PLoS Pathog. 11:E1005127-E1005127(2015).
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:KPI87126.1}.
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DR EMBL; LJSK01000101; KPI87126.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0P622; -.
DR EnsemblProtists; KPI87126; KPI87126; ABL78_3779.
DR VEuPathDB; TriTrypDB:Lsey_0101_0100; -.
DR OMA; WCPTNDL; -.
DR OrthoDB; 1967517at2759; -.
DR Proteomes; UP000038009; Unassembled WGS sequence.
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; 2.
DR PIRSF; PIRSF001293; ATP6V0A1; 2.
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 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 376..400
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 412..436
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 538..562
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 600..624
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 682..707
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 713..733
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT COILED 56..136
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 775 AA; 87547 MW; 3D5F2C5DF8E275CE CRC64;
MPQEACSGLW RSEDMVVLSL HMQREVAHDA VLKLGEIGMF QFLDLNKELS AFQRDFVQEV
RRCDDMERKL RFLQEEIDKA GVATIVEGGA EGETMSSLEQ KIDEVYSEVL ELNEQYQALI
EERNRSKEHL EILLRDFGGA SGDGLMMVTG VIPKDRIPLF ERLVYRATRG NSIMCTDDIE
TPFYNINANE PVYKSVFAIY FSAPRLRERL VKIAEANAAT VYQYADTEQR LNNMHASLQQ
QVDTITQTLH QSAYRQRQVL LGIAASCYEW RRAVVTEKAV FSTMNMLKFS GSTAVAQGWA
PVRACDDIRT AVAEAEYLSG AQVGTIIEEL HTKEAPPTYF KTNKITSSFQ GIVDSYGMAR
YKEANPGVFT IISFPYLFGV MYGDVGHGLI LTLFAAFLVF KEKSFEGQPL NEIFAMIFGG
RYLLLLMGFF AVYMGLLYND MFGFSIEIFT SAYRWPQLPP EGPDGVVYPS FPNGRPSVKP
TSPVAFGVDS AWSETENKLE FYNSIKMKCS VIIGVAQMMA GVFISLTNYL YFNDWVKVWF
RFVPEIAFLS FTFGYMCLLI IVKWLTTWES THDAPSLLET MTNFFLSPGT VTSQLYSGQA
AVQVVLLLLC ALCVPIMLCV IPYMEKKEHD HKMQERAAHP PADGEEEEED DFEFSEIIIH
QIIHTIEYVL GCVSNTASYL RLWALSLAHS QLSEVFWSFA FLLTVGLDGG SGVFVFVGFA
VWMAATIGVL LGMESLSAFL HALRLHWVEF NNKFYIADGY PFEPFDLAES LSKIH
//