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Database: UniProt
Entry: A0A158PA15_ANGCA
LinkDB: A0A158PA15_ANGCA
Original site: A0A158PA15_ANGCA 
ID   A0A158PA15_ANGCA        Unreviewed;       857 AA.
AC   A0A158PA15;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   15-FEB-2017, entry version 4.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
OS   Angiostrongylus cantonensis (Rat lungworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Strongylida; Metastrongyloidea; Angiostrongylidae; Angiostrongylus.
OX   NCBI_TaxID=6313 {ECO:0000313|WBParaSite:ACAC_0000888201-mRNA-1};
RN   [1] {ECO:0000313|Proteomes:UP000035642, ECO:0000313|WBParaSite:ACAC_0000888201-mRNA-1}
RP   NUCLEOTIDE SEQUENCE.
RA   Suarez D.L., Cauthen A.N.;
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:ACAC_0000888201-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) 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}.
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DR   WBParaSite; ACAC_0000888201-mRNA-1; ACAC_0000888201-mRNA-1; ACAC_0000888201.
DR   Proteomes; UP000035642; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000220; C:vacuolar 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   InterPro; IPR026028; V-type_ATPase_116kDa_su_euka.
DR   PANTHER; PTHR11629; PTHR11629; 1.
DR   Pfam; PF01496; V_ATPase_I; 1.
DR   PIRSF; PIRSF001293; ATP6V0A1; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000035642};
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:UP000035642};
KW   Transmembrane {ECO:0000256|RuleBase:RU361189};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361189};
KW   Transport {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    401    425       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    446    464       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    531    549       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    570    593       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    662    685       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    798    822       Helical. {ECO:0000256|RuleBase:RU361189}.
SQ   SEQUENCE   857 AA;  98975 MW;  EF34D35D9F90F059 CRC64;
     MGSLARSEEM RFCQLIVEKE AAFNCVAELG KQPYVQFKDL NPDVNPFQRT FVRDIRRYDE
     MERKLRFLES QITKNHIIIT GRLDRGDYNI MPTAELNQLE TTLTDLERDV KNMNDSDSQL
     MMNYMELKEW DAVLDRTDEF LQGGMDDQAA EELETQEEEY GKVEKAPIGY SVGVIRRERL
     PAFERVLWRA CHHAVYLRSS PIDEDLEDEN DEKCQKAVFI LFYKGDRLRS IVEKVCDGFK
     AKLMKSCPNT FKDRQSARTD VRARLQDLRT VLGQTKEHRY RVLQAAANNH NDWLRQVRMQ
     KTVYHHLNLF TFDRIGRFFV AECWVPRVHL EEVKAALERG AKASGSAMQP VLNVLDTPEE
     PPTYNRTNKF TEVFQSIVDS YGIATYRELN PAPFTIISFP FIFSCMFGDL GHGLLMFLAG
     LYFVVREKNL IDRNIKDEIF GMFFGGRYII LLMGLFSMYA GFIYNDIFAK SFNIFGTSWL
     NPYRKIHFES VQMDPEYSYQ HAYGPYLFGM DPVWNIAENK LNFLNSLKMK LSVIAGIAQM
     TFGVVLSLFN YRYEFFKSKI DIYTVFIPQM LFMSCIFIYL CLQVIVKWIF FWVKEDMIFG
     QFYPGSHCAP SLLIGLINMF MFKDRPAGFV ELKVMNGTTP EYTELDACYL SQWYPGQSTV
     EAILVLIAVL CVPVMLFGKP IHFILEQKKK KNEMGSNISV RANMVADESE IVINGEHKKQ
     AGEHGEPEEE AFGDVMVHQA IHTIEYVLGC VSHTASYLRL WALSLAHAQL SEVLWHMVLV
     QAFSLDGVAG YIATYVIFFF FGVLTFSILV LMEGLSAFLH ALRLHWVEFQ SKFYLGLGYG
     FVPYSFKTAL QAAEIGN
//
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