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Database: UniProt
Entry: A0A162CDI3_9CRUS
LinkDB: A0A162CDI3_9CRUS
Original site: A0A162CDI3_9CRUS 
ID   A0A162CDI3_9CRUS        Unreviewed;       699 AA.
AC   A0A162CDI3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   28-JUN-2023, entry version 20.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   ORFNames=APZ42_019811 {ECO:0000313|EMBL:KZS14472.1};
OS   Daphnia magna.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC   Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX   NCBI_TaxID=35525 {ECO:0000313|EMBL:KZS14472.1, ECO:0000313|Proteomes:UP000076858};
RN   [1] {ECO:0000313|EMBL:KZS14472.1, ECO:0000313|Proteomes:UP000076858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xinb3 {ECO:0000313|EMBL:KZS14472.1,
RC   ECO:0000313|Proteomes:UP000076858};
RC   TISSUE=Complete organism {ECO:0000313|EMBL:KZS14472.1};
RA   Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT   "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL   Submitted (MAR-2016) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KZS14472.1}.
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DR   EMBL; LRGB01000944; KZS14472.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A162CDI3; -.
DR   STRING; 35525.A0A162CDI3; -.
DR   Proteomes; UP000076858; 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:SF63; V-TYPE PROTON ATPASE SUBUNIT A; 1.
DR   PANTHER; PTHR11629; VACUOLAR PROTON ATPASES; 1.
DR   Pfam; PF01496; V_ATPase_I; 2.
DR   PIRSF; PIRSF001293; ATP6V0A1; 2.
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:UP000076858};
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        200..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        364..382
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        402..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        431..451
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        482..503
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        631..655
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   REGION          516..567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          118..145
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        546..566
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   699 AA;  79987 MW;  93954D94E56DC19C CRC64;
     MQQFTLFKST QKKNVNLIEK RHDENVDFQE REDQLVPALF AEYESAYRCM SELGELGCVE
     FRDLNSEATA FQRTFSAEVT RCNEMERKLR YLEGQIVKED IKIEELLDMP AAPLPKEMVD
     LEAALDKMES ELREINVNAE EASDSAFPPI LNELPTNAKP PTYFRTNKFT HGFQALVNAY
     GIANYREVNP GLYTIITFPF LFAVMFGDGG HALIVTMFAS WMCLNEEKLS KVKGEVFGII
     FGGRYIILLM GIFSIYTGFI YHVFFAKAFN IFGSAWVVNY RSEGRPGEEY LIGEGSMESA
     MLVPDRHYDV CPNRTTSKAY NFDNATDFQS CGHYRQYPYP FGVDPVWVIA ENKIVFLNSY
     KMKLSIILGV FHMSFGVFLN LWNFTYFKRR VSILLEFLPR ILFFWPLFGY MMSLMFLKWV
     KYGANKEERE LKSDCAPSIL ITFINMMLLS YSEEKTRPPN EECKTVFMFG DDEGVTQKTL
     QIAFVLIAVL SVPVLLFGTP IQFKMKMNRM NKAKNNYSHS GSLGSSGHGD PADREPIVNS
     TLHVESGGKH DVHDGHSGDY DQNQGSNDDE HNTFGDVMIY QAIHTIEYVL ECISHTASYL
     RLWALSLAHS QLSEVLWFMV LRIGFKALPG YLGSISIFLT FAFWAGATVS ILIAMEGMSA
     FLHTLRLHWV EFQSKFYKGE GVKFHAFHFK RVTDDAKDD
//
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