(data stored in ACNUC16935 zone)

SWISSPROT: ALCS_EMENI

ID   ALCS_EMENI              Reviewed;         262 AA.
AC   Q460G9; C8VL21; Q5ARU9;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   30-AUG-2017, entry version 54.
DE   RecName: Full=Protein alcS;
GN   Name=alcS {ECO:0000312|EMBL:AAZ20475.1}; ORFNames=AN8981;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAZ20475.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, INDUCTION,
RP   AND DISRUPTION PHENOTYPE.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16531087; DOI=10.1016/j.fgb.2005.12.008;
RA   Flipphi M., Robellet X., Dequier E., Leschelle X., Felenbok B.,
RA   Velot C.;
RT   "Functional analysis of alcS, a gene of the alc cluster in Aspergillus
RT   nidulans.";
RL   Fungal Genet. Biol. 43:247-260(2006).
RN   [2] {ECO:0000312|EMBL:EAA64313.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3] {ECO:0000305, ECO:0000312|EMBL:CBF84523.1}
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
RN   [4] {ECO:0000305}
RP   INDUCTION.
RX   PubMed=8736527; DOI=10.1046/j.1365-2958.1996.5301061.x;
RA   Fillinger S., Felenbok B.;
RT   "A newly identified gene cluster in Aspergillus nidulans comprises
RT   five novel genes localized in the alc region that are controlled both
RT   by the specific transactivator AlcR and the general carbon-catabolite
RT   repressor CreA.";
RL   Mol. Microbiol. 20:475-488(1996).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16531087};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:16531087}. Cell
CC       septum {ECO:0000269|PubMed:16531087}.
CC   -!- INDUCTION: By ethanol and ethylacetate. Basal level and ethanol-
CC       induced expression repressed by acetate when grown on lactose. By
CC       ethyl methyl ketone (EMK). Transcriptionally regulated by
CC       transcriptional activator alcR and carbon catabolite repressor
CC       creA. {ECO:0000269|PubMed:16531087, ECO:0000269|PubMed:8736527}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Does not affect growth
CC       on ethanol, glycerol or acetate as a sole carbon source. Does not
CC       result in phenotypes related to possible secretion of ammonia.
CC       Grows normally on media with low concentrations of ethanol. No
CC       effect when screening for allylalcohol and n-propanol toxicity.
CC       AlcA and alcS double mutant has no difference in phenotype from
CC       alcA single mutant. FacA and alcS double mutant does not differ
CC       from a single facA mutant in its ability to grow on a medium with
CC       glycerol as a carbon source either alone or in presence of
CC       ethanol. {ECO:0000269|PubMed:16531087}.
CC   -!- SIMILARITY: Belongs to the acetate uptake transporter (AceTr)
CC       (TC 2.A.96) family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAA64313.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; DQ076245; AAZ20475.1; -; Genomic_DNA.
DR   EMBL; AACD01000168; EAA64313.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001307; CBF84523.1; -; Genomic_DNA.
DR   RefSeq; XP_682250.1; XM_677158.1.
DR   STRING; 162425.CADANIAP00007874; -.
DR   TCDB; 2.A.96.2.1; the acetate uptake transporter (acetr) family.
DR   EnsemblFungi; CADANIAT00007874; CADANIAP00007874; CADANIAG00007874.
DR   EnsemblFungi; EAA64313; EAA64313; AN8981.2.
DR   GeneID; 2868276; -.
DR   KEGG; ani:AN8981.2; -.
DR   HOGENOM; HOG000161878; -.
DR   InParanoid; Q460G9; -.
DR   OMA; CDLMGWR; -.
DR   OrthoDB; EOG092C569S; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   Proteomes; UP000005890; Partially assembled WGS sequence.
DR   GO; GO:0030428; C:cell septum; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:AspGD.
DR   GO; GO:0015123; F:acetate transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0019413; P:acetate biosynthetic process; IEP:AspGD.
DR   GO; GO:0006068; P:ethanol catabolic process; IEP:AspGD.
DR   GO; GO:0006847; P:plasma membrane acetate transport; IBA:GO_Central.
DR   InterPro; IPR030186; AlcS.
DR   InterPro; IPR000791; Grp1/Fun34/SatP.
DR   PANTHER; PTHR31123:SF9; PTHR31123:SF9; 1.
DR   Pfam; PF01184; Grp1_Fun34_YaaH; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; Q460G9.
DR   SWISS-2DPAGE; Q460G9.
KW   Cell membrane; Complete proteome; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    262       Protein alcS.
FT                                /FTId=PRO_0000393862.
FT   TRANSMEM     53     73       Helical. {ECO:0000255}.
FT   TRANSMEM     81    101       Helical. {ECO:0000255}.
FT   TRANSMEM    109    129       Helical. {ECO:0000255}.
FT   TRANSMEM    154    174       Helical. {ECO:0000255}.
FT   TRANSMEM    181    201       Helical. {ECO:0000255}.
FT   TRANSMEM    219    239       Helical. {ECO:0000255}.
SQ   SEQUENCE   262 AA;  28014 MW;  836C337DED2E9B17 CRC64;
     MTTEISNGEA KGHHLSTIPS SITLSAEQFE KLYLSPMMRQ QPSLARKVGN PTPLALGGFV
     ITTTPLSCCL MAWRGSSGNG IAFIGPIIFL GGLLLLITSI LEFILGNTFP CVVFGTIGGF
     WFAFAATMIP SFNAAAPYSS SATSTTAGLT SASFMNTYAF LFITMAVLML IFLLCATRTN
     VVYTLIFLSL LLVFLLLSAG YWRLGEGDAA VGDRCIKGAG ASLFVASLLG FYLLIAQLFD
     AVGLPITLPV GDMERFWPRS QK
//

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