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Database: UniProt
Entry: A0A091Q449_LEPDC
LinkDB: A0A091Q449_LEPDC
Original site: A0A091Q449_LEPDC 
ID   A0A091Q449_LEPDC        Unreviewed;       844 AA.
AC   A0A091Q449;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   ORFNames=N330_04525 {ECO:0000313|EMBL:KFQ14635.1};
OS   Leptosomus discolor (Madagascar cuckoo roller) (Cuculus discolor).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Coraciiformes; Leptosomidae; Leptosomus.
OX   NCBI_TaxID=188344 {ECO:0000313|EMBL:KFQ14635.1, ECO:0000313|Proteomes:UP000053001};
RN   [1] {ECO:0000313|EMBL:KFQ14635.1, ECO:0000313|Proteomes:UP000053001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N330 {ECO:0000313|EMBL:KFQ14635.1};
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; KK686079; KFQ14635.1; -; Genomic_DNA.
DR   RefSeq; XP_009954730.1; XM_009956428.1.
DR   AlphaFoldDB; A0A091Q449; -.
DR   GeneID; 104350554; -.
DR   KEGG; ldi:104350554; -.
DR   CTD; 50617; -.
DR   OrthoDB; 1967517at2759; -.
DR   PhylomeDB; A0A091Q449; -.
DR   Proteomes; UP000053001; 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:UP000053001};
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        639..661
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        778..800
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   REGION          681..712
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          93..120
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        690..712
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   844 AA;  96573 MW;  E8E3D54A414AE105 CRC64;
     MASVFRSEEM SLMQLFLQVE AAYCCVAELG ELGLVQFRDL NVNVNSFQRK FVNEVRRCES
     LERILCFLEN EMEDNVEIVK LEKYPETPLP REMIDMETVL EKLEAELLEA NQNQQTLKQN
     FLELMELKHL LKKTQDFFEA ETNLPDDFFS EDTSGLLELR STAAAAAAKL GFTAGVIKRE
     RMIPFERLLW RVCRGNIYLR YTEMDTPLED PVTREEVKKN VFIIFYQGEQ LKQKIKKICD
     GFRATVYPCP ESATERREML DGVNTRIEDL NTVITQTESH RQRLLHEAAA NLWSWRIKVK
     KIKAIYHILN CCNIDVTQQC VIAEIWFPVA DAARIKRALH QGMERSGSTI APILNAIHTR
     MAPPTFNRTN KFTAGFQNIV DAYGVGNYRE MNPAPYTIIT FPFLFAVMFG DCGHGAVMLG
     FALWMVINEK SLLAQKSTNE IWNTFFSGRY LILLMGIFSM YTGFIYNDCF SKSFNIFGSS
     WHIIPMFKNS TWNKDVLLDN TVLQLDPAVP GVYSGNPYPF GIDPIWNVAS NKLTFLNSYK
     MKMSVVIGIV HMIFGVVLSL FNHIYFKKYI NIILQFIPEM IFIVSLFGYL VFMIIFKWCH
     FDVHSSQSAP SILIHFINMF LFNYSDTSNA PLYLHQKEVQ SFLVIFALIA VPWMLLIKPF
     ILRANHQKAQ RTIQSQAISG NLGGENEVDA PETNHSKKAS QGDHSGGHGG HEDDDEEFNF
     GDTFVHQAIH TIEYCLGCIS NTASYLRLWA LSLAHAQLSE VLWTMVMHNG FNNSSWAGLI
     IIFIIFAAFA VLTVAILLVM EGLSAFLHAL RLHWVEFQNK FYVGAGYKFS PFSFKSIIDG
     TTEE
//
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