(data stored in SCRATCH zone)

SWISSPROT: Q757T6_ASHGO

ID   Q757T6_ASHGO            Unreviewed;       160 AA.
AC   Q757T6;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 110.
DE   RecName: Full=V-type proton ATPase proteolipid subunit {ECO:0000256|RuleBase:RU363060};
GN   ORFNames=AGOS_AEL074W {ECO:0000313|EMBL:AAS52611.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS52611.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS52611.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Proton-conducting pore forming subunit of the membrane
CC       integral V0 complex of vacuolar ATPase. V-ATPase is responsible for
CC       acidifying a variety of intracellular compartments in eukaryotic cells.
CC       {ECO:0000256|RuleBase:RU363060}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000256|RuleBase:RU363060};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU363060}.
CC   -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC       {ECO:0000256|RuleBase:RU363060, ECO:0000256|SAAS:SAAS00595979}.
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DR   EMBL; AE016818; AAS52611.1; -; Genomic_DNA.
DR   RefSeq; NP_984787.1; NM_210141.1.
DR   STRING; 33169.AAS52611; -.
DR   EnsemblFungi; AAS52611; AAS52611; AGOS_AEL074W.
DR   GeneID; 4620979; -.
DR   KEGG; ago:AGOS_AEL074W; -.
DR   HOGENOM; HOG000056520; -.
DR   InParanoid; Q757T6; -.
DR   KO; K02155; -.
DR   OMA; DMFARGI; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
DR   GO; GO:0006878; P:cellular copper ion homeostasis; IEA:EnsemblFungi.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IEA:EnsemblFungi.
DR   GO; GO:0006897; P:endocytosis; IEA:EnsemblFungi.
DR   GO; GO:0006623; P:protein targeting to vacuole; IEA:EnsemblFungi.
DR   GO; GO:0007035; P:vacuolar acidification; IEA:EnsemblFungi.
DR   GO; GO:0007033; P:vacuole organization; IEA:EnsemblFungi.
DR   InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR   InterPro; IPR000245; ATPase_proteolipid_csu.
DR   InterPro; IPR011555; ATPase_proteolipid_su_C_euk.
DR   InterPro; IPR035921; F/V-ATP_Csub_sf.
DR   Pfam; PF00137; ATP-synt_C; 2.
DR   PRINTS; PR00122; VACATPASE.
DR   SUPFAM; SSF81333; SSF81333; 2.
DR   TIGRFAMs; TIGR01100; V_ATP_synt_C; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q757T6.
DR   SWISS-2DPAGE; Q757T6.
KW   Hydrogen ion transport {ECO:0000256|RuleBase:RU363060};
KW   Ion transport {ECO:0000256|RuleBase:RU363060,
KW   ECO:0000256|SAAS:SAAS00140494};
KW   Membrane {ECO:0000256|RuleBase:RU363060, ECO:0000256|SAAS:SAAS00140493};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Transmembrane {ECO:0000256|RuleBase:RU363060,
KW   ECO:0000256|SAAS:SAAS00140496};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU363060,
KW   ECO:0000256|SAAS:SAAS00140495};
KW   Transport {ECO:0000256|RuleBase:RU363060, ECO:0000256|SAAS:SAAS00140502};
KW   Vacuole {ECO:0000256|RuleBase:RU363060}.
FT   TRANSMEM        7..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363060"
FT   TRANSMEM        54..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363060"
FT   TRANSMEM        88..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363060"
FT   TRANSMEM        124..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363060"
FT   DOMAIN          15..73
FT                   /note="ATP-synt_C"
FT                   /evidence="ECO:0000259|Pfam:PF00137"
FT   DOMAIN          91..150
FT                   /note="ATP-synt_C"
FT                   /evidence="ECO:0000259|Pfam:PF00137"
SQ   SEQUENCE   160 AA;  16384 MW;  64E0B77C92A732E1 CRC64;
     MSELCPVYAP FFGAIGCAAA IVFTSFGAAY GTAKSGVSIC ATCVLRPDLL FKNIVPVIMA
     GIIAIYGLVV SVLVCYSLGQ KQALYTGFIQ LGAGLSVGLS GLAAGFAIGI VGDAGVRGNA
     QQPRLFVGMI LILIFAEVLG LYGLIVALLL NSRATQDVTC
//

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