ID   A0A1G4INX8_9SACH        Unreviewed;       807 AA.
AC   A0A1G4INX8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   22-FEB-2023, entry version 22.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   ORFNames=LAMI_0A04544G {ECO:0000313|EMBL:SCU78411.1};
OS   Lachancea mirantina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=1230905 {ECO:0000313|EMBL:SCU78411.1, ECO:0000313|Proteomes:UP000191024};
RN   [1] {ECO:0000313|EMBL:SCU78411.1, ECO:0000313|Proteomes:UP000191024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 11717 {ECO:0000313|EMBL:SCU78411.1};
RA   Devillers H.;
RL   Submitted (MAR-2016) 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}.
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DR   EMBL; LT598462; SCU78411.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4INX8; -.
DR   STRING; 1230905.A0A1G4INX8; -.
DR   OrthoDB; 1967517at2759; -.
DR   Proteomes; UP000191024; Chromosome a.
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   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:UP000191024};
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        400..425
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        446..463
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        522..540
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        552..577
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        614..634
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        712..735
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        741..764
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   REGION          650..680
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        665..680
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   807 AA;  91782 MW;  49775770F4DEB744 CRC64;
     MSDVVLKDEA IFRSAEMSLI QLYIPQEVSR DAVYGIGEIG LVQFRDLNTK VKAFQRTFVK
     EIRRLDNLQR QYRYFHSLLV KHNIKLYEEF EDEKTFSLPP STSSIDDHVD SGTLLEDRMV
     QLVEASEQLE KQKADLEQNR FVLQAGDSFF GGVGKQDSEA DMPPQSISFV TGVIPRSKVS
     SLEQILWRVL RGNLLFKRIE VPGLVYDAKL KEPVYKDAFI VFSHGALIMQ RIRKIAESLD
     ANLYDISESQ DERSEQLSKV NTSLSDVNTV LDSTTKSLET ELYALAKELD GWNKSVSREK
     ALYETLNLFN YDSNRKTLIG EGWVPTDELE DLQEHLSTLT ANLGVDVPSL IQVMETNRTP
     PTFHRTNKFT EGFQNICDCY GIATYREINP GLPTIVTFPF LFAVMFGDMG HGMLMTMAAS
     LLVIYEKQIG RMKRDEIFDM AFSGRYIVLL MGLFSIYTGF LYNDMFSKSL TIFKSGWKWP
     EHWELGETIF AKQVGTYAFG LDHAWHGTEN GLLFANSYKM KLSVLLGFIH MTYSYMFSLA
     NDIYFKNWIN IVGNFVPGLL FMQGIFGYLS ICIVYKWTID WVKDGRPAPG LLNTLINMFL
     SPGTVEEELY PHQAQLQVFL LIVALICVPC LLLIKPLHFK FTQGRHEHQP LAGSEEGVAQ
     QDQENGLLED EDDDENEGGH GEEFGDVVIH QVIHTIEFCL NCVSHTASYL RLWALSLAHA
     QLSSVLWTMT IQIAFGMTGF VGVVMTVVLF GMWFVLTCVI LVVMEGTSAM LHSLRLHWVE
     SMSKFFEGEG TPYEPFKFHC VGFEVPA
//