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Database: UniProt
Entry: Q3SDC7_PARTE
LinkDB: Q3SDC7_PARTE
Original site: Q3SDC7_PARTE 
ID   Q3SDC7_PARTE            Unreviewed;       772 AA.
AC   Q3SDC7;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   07-JUN-2017, entry version 44.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   Name=vata4_1 {ECO:0000313|EMBL:CAI43259.1};
GN   ORFNames=GSPATT00036763001 {ECO:0000313|EMBL:CAK67980.1};
OS   Paramecium tetraurelia.
OC   Eukaryota; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888 {ECO:0000313|EMBL:CAI43259.1};
RN   [1] {ECO:0000313|EMBL:CAI43259.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Genoscope;
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAI43259.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16314392; DOI=10.1091/mbc.E05-06-0511;
RA   Wassmer T., Kissmehl R., Cohen J., Plattner H.;
RT   "Seventeen a-subunit isoforms of paramecium V-ATPase provide high
RT   specialization in localization and function.";
RL   Mol. Biol. Cell 17:917-930(2006).
RN   [3] {ECO:0000313|EMBL:CAK67980.1, ECO:0000313|Proteomes:UP000000600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK67980.1,
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.,
RA   Guigo R., Gogendeau D., Katinka M., Keller A.-M., Kissmehl R.,
RA   Klotz C., Koll F., Le Mouel A., Lepere G., Malinsky S., Nowacki M.,
RA   Nowak J.K., Plattner H., Poulain J., Ruiz F., Serrano V., Zagulski M.,
RA   Dessen P., Betermier M., Weissenbach J., Scarpelli C., Schaechter V.,
RA   Sperling L., Meyer E., Cohen J., Wincker P.;
RT   "Global trends of whole-genome duplications revealed by the ciliate
RT   Paramecium tetraurelia.";
RL   Nature 444:171-178(2006).
RN   [4] {ECO:0000313|EMBL:CAK67980.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK67980.1};
RG   Genoscope;
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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   EMBL; CR932836; CAI43259.1; -; Genomic_DNA.
DR   EMBL; CT868056; CAK67980.1; -; Genomic_DNA.
DR   RefSeq; XP_001435377.1; XM_001435340.1.
DR   STRING; 412030.XP_001435377.1; -.
DR   TCDB; 3.A.2.2.8; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR   EnsemblProtists; CAK67980; CAK67980; GSPATT00036763001.
DR   GeneID; 5021162; -.
DR   KEGG; ptm:GSPATT00036763001; -.
DR   eggNOG; KOG2189; Eukaryota.
DR   eggNOG; COG1269; LUCA.
DR   KO; K02154; -.
DR   Proteomes; UP000000600; Partially assembled 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:UP000000600};
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:UP000000600};
KW   Transmembrane {ECO:0000256|RuleBase:RU361189};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361189};
KW   Transport {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    374    403       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    415    433       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    486    507       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    519    542       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    580    602       Helical. {ECO:0000256|RuleBase:RU361189}.
SQ   SEQUENCE   772 AA;  89589 MW;  4EA571B4D4A85F69 CRC64;
     MLRSQEMSLY QLIMPRESAW AVMDQLGYMG KVEIIDHDPS IPLIARPFAN YIKRCDDLLN
     KLNLLIETAQ KLTILKQFQI SAKTSNKMCP KIHTHQYLDT LEDQINSKVN SFLELNRNHE
     QLLEQENIII DQLDILQECR IYLGDDFFVS RDSKIDYFIG TLKQDEIYQF QRMVFRVSKG
     NAFVHIKLQN SKAIYIVMFP DQGMMLKKKL QKVQESMSLN KFSLPLNLKE FDKISNELTA
     KLKEIKQLIE LTNIQLNSFI QELLKQTEGV RLIDHYNMYI SKEKELYIQL NKLKMQGNLF
     LGELWIPKKD SAQLNEVLLI VKERNRDIPG CQISQKVPHT TPPTYFVLNE FTQVFQQIVN
     TYGIARYREI NPALFTIITF PFLFGIMFGD IGHGFCLLTF GIYNIFYKFE PFHEFRYLIL
     LMGFFSFYSG WIYNDFVSLS LNLFGSCYVV DGQMTPNKPK DCTYPFGLDP AWGDNLEFDD
     SFKMKLSVII AYFHMCLGIC LSGCNFINKK DTYGFCCKFL PQILFLTATI GYMDFLIIFK
     WVKSFSPEDA PSIINTMITM VLSFGSVEGP SMWSVNSQEL IQSILIIIAV VSIPWMWFSH
     IIKGYQVFQR KNNVKIKNST SSIEGSQVIE LQLQTIQDET QQEKSLLQTH DHNDLSPDEE
     FTELIVHETI ETIEFVLGVI SNTASYLRLW ALSLAHSQLA DVFYSLILSS PMTEGSIIGA
     LLRYPIWALV SFGVLMCMDT MECFLHSLRL HWVEFQNKFY KGDGVEFHVY SL
//
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