ID A0D4Z5_PARTE Unreviewed; 378 AA.
AC A0D4Z5;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN ORFNames=GSPATT00013559001 {ECO:0000313|EMBL:CAK78112.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK78112.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK78112.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK78112.1,
RC ECO:0000313|Proteomes:UP000000600};
RX PubMed=17086204; DOI=10.1038/nature05230;
RG Genoscope;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(2006).
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; CT868296; CAK78112.1; -; Genomic_DNA.
DR RefSeq; XP_001445509.1; XM_001445472.1.
DR AlphaFoldDB; A0D4Z5; -.
DR STRING; 5888.A0D4Z5; -.
DR EnsemblProtists; CAK78112; CAK78112; GSPATT00013559001.
DR GeneID; 5031294; -.
DR KEGG; ptm:GSPATT00013559001; -.
DR eggNOG; KOG2189; Eukaryota.
DR HOGENOM; CLU_732505_0_0_1; -.
DR InParanoid; A0D4Z5; -.
DR OMA; HERMEMN; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central.
DR GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR InterPro; IPR002490; V-ATPase_116kDa_su.
DR PANTHER; PTHR11629:SF63; V-TYPE PROTON ATPASE SUBUNIT A; 1.
DR PANTHER; PTHR11629; VACUOLAR PROTON ATPASES; 1.
DR Pfam; PF01496; V_ATPase_I; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrogen ion transport {ECO:0000256|RuleBase:RU361189};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU361189}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000000600};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU361189}.
FT COILED 84..130
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 378 AA; 44073 MW; 8770E89E24AE20E4 CRC64;
MSFFRSETMA YYQIIVPKES AWNVFNEMGK LSMVQVVDMS PDEPHVNRPF YQYIRRADEV
ISKLNVLEVE MLKYKIKNLK CSDYQQFLEK MSQYTKDISQ SEDKWFDLIE STLDEKYSQL
IEQIQNLEQI SVRKNTLFEH KAVLIKSKEV LGPTYYTKGR NVAINPQIGG IPEQQKVAQP
LYNLNYLVGV VDRLEANRFK RMVFRASKGN AWIVMSDIEY SRIDASLESG NLDSDKSAAK
NLEKQRTVFL IVYTGGGQDF LRAKLNKICD SFNCAKFVLP DDPQLLVQKT LELDRSLDEC
DNLLRLTAGK IKELLLEYAQ IQPQLKISLL EMSKLIMVKE KALYTNLNYL YQKERIYIGF
FWAPKHIEAE LHHTDYTN
//