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Database: UniProt
Entry: A0A091K2A3_COLST
LinkDB: A0A091K2A3_COLST
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ID   A0A091K2A3_COLST        Unreviewed;       845 AA.
AC   A0A091K2A3;
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=N325_11587 {ECO:0000313|EMBL:KFP30338.1};
OS   Colius striatus (Speckled mousebird).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Coliiformes; Coliidae; Colius.
OX   NCBI_TaxID=57412 {ECO:0000313|EMBL:KFP30338.1, ECO:0000313|Proteomes:UP000053615};
RN   [1] {ECO:0000313|EMBL:KFP30338.1, ECO:0000313|Proteomes:UP000053615}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N325 {ECO:0000313|EMBL:KFP30338.1};
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; KK539118; KFP30338.1; -; Genomic_DNA.
DR   RefSeq; XP_010196720.1; XM_010198418.1.
DR   AlphaFoldDB; A0A091K2A3; -.
DR   GeneID; 104555143; -.
DR   KEGG; csti:104555143; -.
DR   CTD; 50617; -.
DR   OrthoDB; 1967517at2759; -.
DR   Proteomes; UP000053615; 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:UP000053615};
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        403..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        644..662
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        777..801
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   REGION          681..713
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          51..120
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        698..713
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   845 AA;  96778 MW;  FE6D1ECBC32514C5 CRC64;
     MASFFRSEEM SLMQLFLQVE AAYCCVSELG ELGLVQFRDL NANVNSFQRK FVNEVRRCES
     LERILRFLEN EMEDNVEIVK LEKYPETPLP REMIDMEAVL EKLEAELLEA NRNQQTLKQN
     FLELMELKHL LKKTQDFFEA ETNLTDDFFS EDTSGLLELR SNPAAAAAKL GFTAGVIRRE
     RIIPFERLLW RACRGNIYLR YTEMDTPLED PVTREEVKKN VFIIFHQGEQ LKQKIKKICD
     GFRATVYPCP ESAAERREML DGVNTRIEDL NTVMTQTESH RQRLLHEAAA NLWSWGIKVK
     KIKAIYHILN CCNIDVTQQC VIAEIWFPVA DAGRIKKALH QGMERSGSAI APILTAIHTR
     MAPPTFNRTN KFTAGFQNIV DAYGVGNYRE INPAPYTIIT FPFLFAVMFG DCGHGAVMLG
     FALWMVMNEK SLLAQKSNNE IWNTFFSGRY LILLMGIFSM YTGFIYNDCF SKSFNIFGSS
     WHVIAMFKNN SWNNSVLMEN TQLQLDPAVP GVYSGNPYPF GIDPIWNIAS NKLTFLNSYK
     MKMSVVLGIV HMIFGVVLSL FNHIYFKKYI NIVLQFIPEM IFIISLFGYL VFMIIFKWCH
     FDAHSSQSAP SILIHFINMF LFNYDDSSNA PLYLHQKEVQ SFLVIFALIA VPWMLLIKPF
     ILRANYQKEQ RMIRSQAISA NPGGENEVDV PETNHSMKAS QGDHHGGGHG EHEDGGEEFN
     FGDTFVHQAI HTIEYCLGCI SNTASYLRLW ALSLAHAQLS EVLWTMVMHN GLNNSSWIGL
     IVIFIIFAAF AVLTVAILLV MEGLSAFLHA LRLHWVEFQN KFYMGAGYKF SPFSFKHIID
     GTTEE
//
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