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Database: UniProt
Entry: Q3SDC3_PARTE
LinkDB: Q3SDC3_PARTE
Original site: Q3SDC3_PARTE 
ID   Q3SDC3_PARTE            Unreviewed;       788 AA.
AC   Q3SDC3;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   05-JUL-2017, entry version 48.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   Name=vata7_1 {ECO:0000313|EMBL:CAI43263.1};
GN   ORFNames=GSPATT00018870001 {ECO:0000313|EMBL:CAK84674.1};
OS   Paramecium tetraurelia.
OC   Eukaryota; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888 {ECO:0000313|EMBL:CAI43263.1};
RN   [1] {ECO:0000313|EMBL:CAI43263.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Genoscope;
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAI43263.1}
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:CAK84674.1, ECO:0000313|Proteomes:UP000000600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK84674.1,
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:CAK84674.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK84674.1};
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; CR932840; CAI43263.1; -; Genomic_DNA.
DR   EMBL; CT868518; CAK84674.1; -; Genomic_DNA.
DR   RefSeq; XP_001452071.1; XM_001452034.1.
DR   STRING; 412030.XP_001452071.1; -.
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; CAK84674; CAK84674; GSPATT00018870001.
DR   GeneID; 5037856; -.
DR   KEGG; ptm:GSPATT00018870001; -.
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; 2.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
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    381    405       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    434    452       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    492    513       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    525    548       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    584    603       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    717    738       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   COILED      222    249       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   788 AA;  92436 MW;  00D6068F383EB4DC CRC64;
     MFRATEIHLY KLYVEREQAF HLLTKVGQMK NVNLINCSSS AFHEHDYYKQ LKRCDDIYNK
     IGEIKHLLHL YNKQIHYCPN YEVFISNIKI TDDQAIKIEQ ELTHKVQFIL NQQANLQSIM
     EQRNKLGEEI AVLQHCKDFI YKFSGIQLGY IVGCLNTIDS HKFNRIVFRI SKENGIVKFK
     NLNNQRTLFT LVFALGKHEN LKNKLLKICE AFNVSIIQVP EESKVENKIL ELENDIANLD
     IVISTTKQEI DQQLDFFSDI QVEKVLNLDE IYDYGYCSYI CELNIILDII SATYYHLTFF
     EAKSQFLIGQ IWCEQSDIEE IKSFGVQVEI MQDINENIYE PPSLMKTNDF TYIFQELVNT
     YGIPRFDEIN PGLFTVITFP FLFGMMFGDI GHGVVLTLFG FYLLIFGQRV LKRIKLENSS
     DYLAYADFQS LYQCRYLLTL MGLFATYCGF IYNDFFSISL EYKLEKFQLG FDGKWSMSES
     HLTVMNSFKM KTAIIVGVTQ MVFGILLKGW NCLYQRKFID FIFNFLPELA FMLSTFGYMS
     FLIILKWLTN YNNNQEPPSI ITTLLNMVFT LGGIKGTEMY PHQVYYQSIL IRVAICSPII
     MLLKPEVLRI KRMFFNQRNQ QIVYNELIEQ EHGQIEQMKE EKHQLFGKLV ESRAIKEEKH
     FDYSEVYIES LIECIEFVLG AVSNTASYLR LWALSLAHSQ LSEVFFKMSL EPQLQTGSIV
     GICLTFTIYA LATFGVLMCM DTLECFLHSL RLHWVEFQSK FYKGDGHSFQ RFNYLQFLDQ
     KFQFSTRM
//
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