ID   A0A093IXA0_EURHL        Unreviewed;       842 AA.
AC   A0A093IXA0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   ORFNames=N326_02499 {ECO:0000313|EMBL:KFW04252.1};
OS   Eurypyga helias (Sunbittern) (Ardea helias).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Eurypygimorphae; Eurypygiformes;
OC   Eurypygidae; Eurypyga.
OX   NCBI_TaxID=54383 {ECO:0000313|EMBL:KFW04252.1, ECO:0000313|Proteomes:UP000054232};
RN   [1] {ECO:0000313|EMBL:KFW04252.1, ECO:0000313|Proteomes:UP000054232}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N326 {ECO:0000313|EMBL:KFW04252.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KK565846; KFW04252.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093IXA0; -.
DR   Proteomes; UP000054232; 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:SF26; V-TYPE PROTON ATPASE 116 KDA SUBUNIT A 4; 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:UP000054232};
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        398..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        447..466
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        545..566
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        572..596
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        641..662
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        773..798
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   REGION          672..710
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          51..120
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        688..710
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   842 AA;  96299 MW;  E3CD83DC82E6DB8B CRC64;
     MASVFRSEEM SLMQLFLQVE AAYCCVAELG ELGLAQFRDL NVNVNSFQRK FVNEVRRCES
     LERILRFLEN EMEDNVEIVK LEKYPETPLP REMIDMETVL EKLEAELLEA NQNQQTLKQN
     FLELTELKHL LKKTQDFFEA ETNLPDDFFS EDTSGLLELR STPAAAAAKL GFTAGVIKRE
     RMIPFERLLW RACRGNIYLR YTEMDTPLED PVTREEVKKN VFIIFYQGEQ LKQKIKKICD
     GFRATVYPCP ESATERREML DGVNTRIEDL NTVITQTESH RQRLLREAAA SLWSWGIKVK
     KIKAIYHILN CCNIDVTQQC VIAEIWFPVA DAGRIKRALH QGMERSGSTI APILTAIHTR
     MAPPTFNRTN KFTAGFQNIV DAYGVGSYRE MNPAPYTIIT FPFLFAVMFG DCGHGAVMLG
     FALWMVINEK SLLAQKSTNE IWNTFFSGRY LILLMGIFSM YTGFIYNDCF SKSLNIFGSS
     WHIIPMFKNS TWTKDVLLDN MVLQLDPAVP GVYSGNPYPF GIDPIWNVAS NKLTFLNSYK
     MKMSVVIGIV HMIFGVMLSL FNHIYFKKYM NIVLQFIPEM IFIISLFGYL VFMIIFKWCH
     FDVHSSQSAP SILIHFINMF LFNYSDTSNA PLYLHQKEVQ SFLVIFALIA VPWMLLIKPF
     LLRANHQKAQ RMSQAISENP GGENELEVPE TNHSKKASKG DHSGGHGGHE DDDEEFNFGD
     IFVHQAIHTI EYCLGCISNT ASYLRLWALS LAHAQLSEVL WTMVMHNGFN NSGWAGLIVI
     FIIFAAFAVL TVAILLVMEG LSAFLHALRL HWVEFQNKFY VGAGYKFSPF SFKHIIDGSA
     ED
//