ID A0A0C2FDU2_9BILA Unreviewed; 367 AA.
AC A0A0C2FDU2;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
DE Flags: Fragment;
GN ORFNames=ANCDUO_23225 {ECO:0000313|EMBL:KIH46720.1};
OS Ancylostoma duodenale.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH46720.1, ECO:0000313|Proteomes:UP000054047};
RN [1] {ECO:0000313|EMBL:KIH46720.1, ECO:0000313|Proteomes:UP000054047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zhejiang {ECO:0000313|EMBL:KIH46720.1,
RC ECO:0000313|Proteomes:UP000054047};
RA Mitreva M.;
RT "Draft genome of the parsitic nematode Ancylostoma duodenale.";
RL Submitted (DEC-2013) 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; KN768629; KIH46720.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2FDU2; -.
DR Proteomes; UP000054047; Unassembled WGS sequence.
DR GO; GO:0033179; C: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 PANTHER; PTHR11629:SF73; V-TYPE PROTON ATPASE 116 KDA SUBUNIT A 2; 1.
DR PANTHER; PTHR11629; VACUOLAR PROTON ATPASES; 1.
DR Pfam; PF01496; V_ATPase_I; 1.
PE 3: Inferred from homology;
KW Hydrogen ion transport {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:UP000054047};
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 39..59
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 71..96
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 169..191
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 301..325
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 346..363
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KIH46720.1"
SQ SEQUENCE 367 AA; 41406 MW; A6D85810CD52FAD5 CRC64;
INPEYSYQHA DGPYPFGVDP IWNIAENKLN FLNSMKMKLS VIAGIAQMTF GVILSFFNYR
FFKSKIDIYT VFIPQMLFMT CIFIYLCLQI VLKWIFFWVK SEVIFGQLYP GSHCAPSLLI
GLINMFMFKD RPAGFVQFDK PINASANEYE ELDACYLSQW YPGQSMIEAI LVIIAVLCIP
IMLFGKPVHF IMEQKKKKKA MGSNISVRAN VASDDSEIII NGGNKKEEAE HAAGGGGGHG
HDEAFGDVMV HQAIHTIEYV LGCVSHTASY LRLWALSLAH AQLSEVLWHM VLVNSFILDG
VAGYIALYVI FFAFGVLTFS ILVLMEGLSA FLHALRLHWV EFQSKFYLGL GYAFVPYSFK
QALQETN
//
