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Database: UniProt
Entry: A0A093GBE5_DRYPU
LinkDB: A0A093GBE5_DRYPU
Original site: A0A093GBE5_DRYPU 
ID   A0A093GBE5_DRYPU        Unreviewed;       844 AA.
AC   A0A093GBE5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   ORFNames=N307_13313 {ECO:0000313|EMBL:KFV64202.1};
OS   Dryobates pubescens (Downy woodpecker) (Picoides pubescens).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Piciformes; Picidae; Dryobates.
OX   NCBI_TaxID=118200 {ECO:0000313|EMBL:KFV64202.1, ECO:0000313|Proteomes:UP000053875};
RN   [1] {ECO:0000313|EMBL:KFV64202.1, ECO:0000313|Proteomes:UP000053875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N307 {ECO:0000313|EMBL:KFV64202.1};
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}.
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DR   EMBL; KL215321; KFV64202.1; -; Genomic_DNA.
DR   RefSeq; XP_009894675.1; XM_009896373.1.
DR   AlphaFoldDB; A0A093GBE5; -.
DR   STRING; 118200.A0A093GBE5; -.
DR   GeneID; 104296552; -.
DR   KEGG; dpub:104296552; -.
DR   CTD; 50617; -.
DR   OrthoDB; 1967517at2759; -.
DR   Proteomes; UP000053875; 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:UP000053875};
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        776..800
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   REGION          674..712
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          51..120
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        688..712
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   844 AA;  96670 MW;  2868B527FD5191E9 CRC64;
     MASVFRSEEM SLMQLFLQVE AAYCCVAELG ELGLVQFRDL NANVNSFQRK FVNEVRRCES
     LERILRFLEN EMEDSAEIVK LEKYPETPLP REMIDMETVL EKLEAELLEA NQNQQTLKQN
     FLELTELKLL LKKTQDFFEA ETNLPDDFFS EDTSGLLELR STPAAAAAKL GFTAGVIKRE
     RMIPFERLLW RVCRGNIYLR YTEMDTTLED PVTREDVKKN VFIIFYQGEQ LKQKIRKICD
     GFRATVYPCP ESATERREML DGVNTRIEDL NTVITQTESH RQRLLHEAAA NLWSWGIKVK
     KIKAIYHILN CCNIDVTQQC VIAEIWFPVA DAGRIKRALH QGMERSGSTI APILTAIHTR
     MAPPTFNRTN KFTAGFQNIV DAYGVGNYRE MNPAPYTIIT FPFLFAVMFG DWGHGAVMLG
     FALWMVINEK SLLAQKSTNE IWNTFFSGRY LILLMGIFSM YTGFIYNDCF SKSFNLFGSS
     WHIIPMFKNK TWNKDVLLEN TVLQLDPAIP GVYSGNPYPF GIDPIWNVAS NKLTFLNSYK
     MKMSVVIGIV HMIFGVVLSL FNHIYFRKYI NIILQFIPEM IFIVSLFGYL VFMIIFKWCR
     FDVHSSQSAP SILIHFINMF LFNYSDTSNA PLYLHQKEVQ TFLVIFALIA VPWMLLIKPF
     ILRANHQKVQ RMIQSQAMSG NPGDENEVDV PETNHPKKAS QGDHGSGHGG HEDGDEEFDF
     GDTFVHQAIH TIEYCLGCIS NTASYLRLWA LSLAHAQLSE VLWTMVMHNG LSNSSWAGLI
     VMFVIFAAFA VLTVAILLVM EGLSAFLHAL RLHWVEFQNK FYVGAGHKFS PFSFRHIIDG
     TAEE
//
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