ID A0A0C2GBV3_9BILA Unreviewed; 567 AA.
AC A0A0C2GBV3;
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};
GN ORFNames=ANCDUO_13481 {ECO:0000313|EMBL:KIH56339.1};
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:KIH56339.1, ECO:0000313|Proteomes:UP000054047};
RN [1] {ECO:0000313|EMBL:KIH56339.1, ECO:0000313|Proteomes:UP000054047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zhejiang {ECO:0000313|EMBL:KIH56339.1,
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; KN735895; KIH56339.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2GBV3; -.
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:SF58; V-TYPE PROTON ATPASE 116 KDA SUBUNIT A 3; 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 93..118
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 138..159
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 244..262
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 274..301
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 383..402
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 504..531
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
SQ SEQUENCE 567 AA; 63953 MW; 7337CF24FC0985EC CRC64;
MFSVDVTHKC LIAECWVPTV DLPLVKMALR KGTDQAGSPI QAVLNEMETH DMPPTHFKLN
KFTQGFQNIV DAYGIANYRE VNPAPWSIIS FPFLFAVMFG DSGHGIIMFL AALAFVVFEK
KLISMKIKDE VCGHLPHLIF NTFFGGRYVV LLMGIFSIYT GLLYNDIYSK SIDIFGSSWK
NPYPQKLLAE MDEHAMNTSQ TADLTWPPEY SFDSNLGPYP FGVDPIWNVA KNKLNFLNPM
KMKTSIILGI GQMAFGLILS LCNHIHNRSL VDIFFVFVPQ CFFLGCIFVY LCVMVVLKWI
FFYVNPTFIF GRLYPGSNCA PSLLIGLINM FMLKGRDPGF VQHVNSPNAT ASVIIGGKNY
TYDVYDQCYL QQWYPGQVLA EQILLGLAVV SIPIMLLVKP FYVRWLHNRG RPIPGGHGHG
GGGEEEEVVV WTRRPSRYFS FGDVMVYQAI HTIEFALGCI SHTASYLRLW ALSLAHAQLS
EVLWDMLLSI GLDMGGWGGS AAVFVLYFFF GVLSISILIL MEGLSAFLHA LRLHWVEFNS
KFYGGTGVAF EPFYFTRLIR IEEGLEQ
//