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Database: UniProt
Entry: G8BIQ0_CANPC
LinkDB: G8BIQ0_CANPC
Original site: G8BIQ0_CANPC 
ID   G8BIQ0_CANPC            Unreviewed;       821 AA.
AC   G8BIQ0;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   05-JUL-2017, entry version 17.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   OrderedLocusNames=CPAR2_403170 {ECO:0000313|CGD:CAL0000146171,
GN   ECO:0000313|EMBL:CCE44515.1};
OS   Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia
OS   parapsilosis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
OC   Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=578454 {ECO:0000313|Proteomes:UP000005221};
RN   [1] {ECO:0000313|Proteomes:UP000005221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L.,
RA   Agrafioti I., Arnaud M.B., Bates S., Brown A.J., Brunke S.,
RA   Costanzo M.C., Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L.,
RA   Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R.,
RA   Neiman A.M., Nikolaou E., Quail M.A., Quinn J., Santos M.C.,
RA   Schmitzberger F.F., Sherlock G., Shah P., Silverstein K.A.,
RA   Skrzypek M.S., Soll D., Staggs R., Stansfield I., Stumpf M.P.,
RA   Sudbery P.E., Srikantha T., Zeng Q., Berman J., Berriman M.,
RA   Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
RN   [2] {ECO:0000313|Proteomes:UP000005221}
RP   GENOME REANNOTATION.
RC   STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX   PubMed=22192698; DOI=10.1186/1471-2164-12-628;
RA   Guida A., Lindstaedt C., Maguire S.L., Ding C., Higgins D.G.,
RA   Corton N.J., Berriman M., Butler G.;
RT   "Using RNA-seq to determine the transcriptional landscape and the
RT   hypoxic response of the pathogenic yeast Candida parapsilosis.";
RL   BMC Genomics 12:628-628(2011).
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; HE605208; CCE44515.1; -; Genomic_DNA.
DR   EnsemblFungi; CCE44515; CCE44515; CPAR2_403170.
DR   CGD; CAL0000146171; CPAR2_403170.
DR   OrthoDB; EOG092C0YCY; -.
DR   Proteomes; UP000005221; Chromosome 4.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
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:EnsemblFungi.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:EnsemblFungi.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:EnsemblFungi.
DR   GO; GO:0016049; P:cell growth; IEA:EnsemblFungi.
DR   GO; GO:0043623; P:cellular protein complex assembly; IEA:EnsemblFungi.
DR   GO; GO:0006797; P:polyphosphate metabolic process; IEA:EnsemblFungi.
DR   GO; GO:0007035; P:vacuolar acidification; IEA:EnsemblFungi.
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:UP000005221};
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:UP000005221};
KW   Transmembrane {ECO:0000256|RuleBase:RU361189};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361189};
KW   Transport {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    408    432       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    453    470       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    530    552       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    559    583       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    624    646       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    725    744       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    756    779       Helical. {ECO:0000256|RuleBase:RU361189}.
SQ   SEQUENCE   821 AA;  94133 MW;  AAB95E2655ED25B5 CRC64;
     MSDKEEAVFR SADMSLVQIY VPTEVARETI YKIGQLDIIQ FRDLNSKVNE FQRSFVNELR
     KLDNTERQYR LFKQELDYRD IPIKLYPYEF VIPQQSDIDD LVESGQLLED RVVQLRDSVE
     TLYKNQNYLK QFKFTILAVD KFFHYQLGGH GSAIERSLLP EFDESRLLLS SATASASQFI
     SGVINRDKVG ILQQILWRIL RGNLYYHSEE LQEEIYDVKH NAYVAKNTFI IFSYGSLVHD
     RIVKVCESLD AEVYDVDKSE EARSKQLSEV KSKLEDLGTV LSESENALTS ELIAISQDLG
     KWWEIIAREK QVYKTMNRCD YDGARKLLLG EGWTPTDSIP ELTQVVKEFD QTQSIPTIVN
     VLSTNRTPPT YVRTNKFTYA FQAICDAYGT PRYKEINPGL PTIITFPFMF AIMFGDLGHG
     FIMFLAAAFL VLNEKKLSGV KKDEIFDMAY TGRYILLLMG IFSMYTGFIY NDVFSRSMDF
     FKSGWEWPEH FKVGDTLIAK EVGTYIFGMD PAWHGTENAL LFSNSYKMKL SILMGYAHMT
     YSYFFSIANY IYFDSIVDIV GNFIPGLLFM QGIFGYLSLV IVYKWTVNWA ESKYQPPGIL
     NMLISMFLSP GNVEEPFYPG QATIQIWLVV IALICVPWLL FVKPLWLKRQ LDKEAKQHAQ
     YSALPNDDEE VGGSNGSTYN NNENDDEEGD GEDHEEHSFG DIMIHQVIHT IEFCLNCVSH
     TASYLRLWAL SLAHAQLSTV LWSMTISKAF GPTGVFGVVA VVFLFAMWFT LTVCILVVME
     GTSAMLHSLR LHWVESMSKY FEGGGMPYEP FSFKGLLDSV F
//
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