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Database: UniProt
Entry: A0A2G5EJK7_AQUCA
LinkDB: A0A2G5EJK7_AQUCA
Original site: A0A2G5EJK7_AQUCA 
ID   A0A2G5EJK7_AQUCA        Unreviewed;       818 AA.
AC   A0A2G5EJK7;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   ORFNames=AQUCO_00700328v1 {ECO:0000313|EMBL:PIA55933.1};
OS   Aquilegia coerulea (Rocky mountain columbine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC   Aquilegia.
OX   NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA55933.1, ECO:0000313|Proteomes:UP000230069};
RN   [1] {ECO:0000313|EMBL:PIA55933.1, ECO:0000313|Proteomes:UP000230069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA   Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA   Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT   "WGS assembly of Aquilegia coerulea Goldsmith.";
RL   Submitted (SEP-2017) 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; KZ305024; PIA55933.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5EJK7; -.
DR   STRING; 218851.A0A2G5EJK7; -.
DR   InParanoid; A0A2G5EJK7; -.
DR   OrthoDB; 1967517at2759; -.
DR   Proteomes; UP000230069; 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:UP000230069};
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        422..446
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        467..484
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        547..565
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        577..600
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        636..654
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        755..776
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   COILED          94..128
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   818 AA;  92523 MW;  FD3B896060F7E238 CRC64;
     MGSVEGGCCP PMDLFRSEPM QLVQIIIPIE SAHLTVSYLG ELGLLQFKDL NAEKSPFQRT
     YAAQIKRCGE MARKLRFFRE QMTKAGFTPS ATPLTQAKID LDGLEIKLGE LEAELIEING
     NSDKLQRAYN ELVEYKLVLH KAGEFFHLAH NDATAQQREI EASHGDESSI TSPLLDQEMS
     IDPSKQVKLG FVSGLVPREK SMAFERILFR ATRGNVFLKQ AVVSEPVTDP VSGEKVDKNV
     FVVFYSGERA KNKILKICDA FGANRYPFAD DLGTQAQTVT EVSGRLSELK TTIDVGLVQR
     DNLLKTISNQ FEQWNLLVRK EKSTYHTLNM FSVDVTKKCL VAEGWCPLFA TTQLQDVLQR
     ASFDSNSQVG AILQVLHTKE SPPTYFRTNK FTTAFQEIVD AYGVAKYQEA NPGLYTVVTF
     PFLFAVMFGD WGHGICLLLA TLFFIVKEKK LSSQKLGDIT EMTFGGRYVI LMMSLFSIYT
     GLIYNEFFSV PFELFGPSAY ACRDLSCKDS TTIGLIKVRR TYPFGVDPEW HGSRSELPFL
     NSLKMKMSIL LGVAQMNLGI VLSFCNAKFF SNSVNVWFQF IPQLIFLNSL FGYLSVLIIV
     KWVTGSKADL YHVMIYMFLS PTDDLGENQL FDGQKTLQIV LLLLALVAVP WMLLPKPFIL
     KKQHQERHQG QSYQPLHRNE DSLEVEVHHD SHGHEEFEFS EVFVHQLIHT IEFVLGAVSN
     TASYLRLWAL SLAHSELSSV FYEKVLLLAW GYNNVIILII GIIVFVCATV GVLLVMETLS
     AFLHALRLHW VEFQNKFYEG DGYKFYPFSF ALLGDEEE
//
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