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Database: UniProt
Entry: A0A0R3QU71_9BILA
LinkDB: A0A0R3QU71_9BILA
Original site: A0A0R3QU71_9BILA 
ID   A0A0R3QU71_9BILA        Unreviewed;       502 AA.
AC   A0A0R3QU71;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   12-APR-2017, entry version 5.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
OS   Brugia timori.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Spirurida;
OC   Filarioidea; Onchocercidae; Brugia.
OX   NCBI_TaxID=42155 {ECO:0000313|Proteomes:UP000050602, ECO:0000313|WBParaSite:BTMF_0001127301-mRNA-1};
RN   [1] {ECO:0000313|Proteomes:UP000050602, ECO:0000313|WBParaSite:BTMF_0001127301-mRNA-1}
RP   NUCLEOTIDE SEQUENCE.
RG   Helminth Genomes Consortium;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:BTMF_0001127301-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- FUNCTION: Essential component of the vacuolar proton pump (V-
CC       ATPase), a multimeric enzyme that catalyzes the translocation of
CC       protons across the membranes. Required for assembly and activity
CC       of the V-ATPase. {ECO:0000256|RuleBase:RU361189}.
CC   -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC       {ECO:0000256|RuleBase:RU361189}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|RuleBase:RU361189}.
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DR   WBParaSite; BTMF_0001127301-mRNA-1; BTMF_0001127301-mRNA-1; BTMF_0001127301.
DR   Proteomes; UP000050602; Genome Assembly.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR   InterPro; IPR002490; V-ATPase_116kDa_su.
DR   PANTHER; PTHR11629; PTHR11629; 1.
DR   Pfam; PF01496; V_ATPase_I; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000050602};
KW   Hydrogen ion transport {ECO:0000256|RuleBase:RU361189};
KW   Ion transport {ECO:0000256|RuleBase:RU361189};
KW   Membrane {ECO:0000256|RuleBase:RU361189};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050602};
KW   Transmembrane {ECO:0000256|RuleBase:RU361189};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361189};
KW   Transport {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    406    430       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    451    469       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   COILED       97    124       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   502 AA;  58219 MW;  22A9D2C88CCF35F3 CRC64;
     MGSLYRSEQM RFCQMIVQKD AAFSCVAELG KHPYVQFKDL NANVNPFQKM YLRDIQRFEE
     LERKLRFLDA QIRKDDIEVN DDVGGDDTYE VLAPHELNQL EGTLIDLERD VINMNENNII
     LKRNYFELKE WEAILEKTDH FFEEGISDVA MHEIEAMQED SALVLRSGKE PIGFLAGVVN
     RDRVNAFEKV LWRACHKTAF IRTTDIEEEL ENPDSGEICS KSVFLIFYKG DRLRIIIEKV
     CEGFKAKLYN NCPKNSKDRH AAARDVKARI SDMRTVLGQT QEHRYKVLQA ASNSVRQWQK
     EVRMQKSVYY TLNLFTFDAI GKFFVAECWV PYVDLENVRL ALEEGVRKSG SSVRPVLNLL
     ETTEEPPTYN RVNKFTRVFQ AIVDSYGTAS YLEINPAPYT IITFPFIFSC MFGDLGHGII
     MLLVGLWMVL REKNLAARNI KDEIFNMFYG GRYIILLMGI FSIYAGFLYN DLFAKSFNLF
     GSKWRNPFPN AEIESWDSQS IL
//
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