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Database: UniProt
Entry: A0A0M8P6V0_9EURO
LinkDB: A0A0M8P6V0_9EURO
Original site: A0A0M8P6V0_9EURO 
ID   A0A0M8P6V0_9EURO        Unreviewed;       855 AA.
AC   A0A0M8P6V0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, 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=ACN38_g2462 {ECO:0000313|EMBL:KOS46566.1};
OS   Penicillium nordicum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=229535 {ECO:0000313|EMBL:KOS46566.1, ECO:0000313|Proteomes:UP000037696};
RN   [1] {ECO:0000313|EMBL:KOS46566.1, ECO:0000313|Proteomes:UP000037696}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOMC 185683 {ECO:0000313|EMBL:KOS46566.1,
RC   ECO:0000313|Proteomes:UP000037696};
RA   Nguyen H.D., Seifert K.A.;
RT   "Genome sequencing of Penicillium nordicum.";
RL   Submitted (AUG-2015) 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:KOS46566.1}.
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DR   EMBL; LHQQ01000027; KOS46566.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8P6V0; -.
DR   STRING; 229535.A0A0M8P6V0; -.
DR   OrthoDB; 1967517at2759; -.
DR   Proteomes; UP000037696; 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; 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:UP000037696};
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        462..487
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        549..567
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        579..602
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        642..661
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        758..781
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        787..811
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   COILED          100..127
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   855 AA;  97640 MW;  17403865CD805D6E CRC64;
     MAPRDTFFRS VDMSLTQLYI ANEIGREVVS ALGEVGQVQF RDLNPDTNAF QRTFTKEIRR
     LDNVERQLRY FHKQMEKATI PMRSSSDFSD TLAAPLASEI DELADRSESL EQRIVSLNDS
     YETLKKREVE LSEWRWVLRE AGGFFDRAHT QTEDIRQSFD NDEAPLLRDV EHHAPRQNGD
     TQGQQSFSEM NIGFVSGVIP RDRIGAFERI LWRTLRGNLY MNQSEIPEPI IDPMTNVEVH
     KNVFVIFAHG KNILAKIRKI SESLNASLYG VDENSELRRD QIHEVNTRLG DVGNVLRNTK
     NTLDAELSQI ARSLAAWMII VKKEKAVYDT LNKFSYDQAR KTLIAEAWCP TNSLALIKST
     LQDVNDRAGL TVPTIVNQIR TNKTPPTFVR TNKFTEGFQT IVNAYGIPKY SEVNPGLYTV
     VTFPFLFAVM FGDCGHGALM TMAASAMIFW EKKLARTKLD ELTYMAFYGR YIMLMMGLFS
     IYTGFIYNDI FSKSFTIFPS QWQWPEDIKA GEMVEATLKE GYRYPIGLDW NWHEADNSLL
     FSNSMKMKMS VLLGWCHMTY ALCLQYVNGR HFKSKVDIWG NFVPGLLFFQ SIFGYLVLTI
     LYKWTVNWQE KGVNPPGLLN MLIFMFLSPG TVEEQLYPGQ SAVQILLLLV AVAQVPIMLF
     LKPFWLRYEH NRARALGYRG LGENSRVSAL DADGDLDGGP GRDSLASDGE GVAMLSQDID
     DSEEHEEFDF GDLMIHQVIH TIEFCLNCIS HTASYLRLWA LSLAHQQLSI VLWTMTIGSA
     FQQENPVTRV IMVVVSFYLW FVLTLCILCA MEGTSAMLHS LRLHWVEAMS KHFVGEGIPF
     LPFSFKTLLE EDPVD
//
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