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MFSA_ASPFU
ID   MFSA_ASPFU              Reviewed;         542 AA.
AC   Q4WC50;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Major facilitator superfamily transporter mfsA {ECO:0000303|PubMed:16622700};
GN   Name=mfsA {ECO:0000303|PubMed:16622700}; Synonyms=stl1;
GN   ORFNames=AFUA_8G05710;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
RN   [2]
RP   IDENTIFICATION, FUNCTION, AND INDUCTION.
RX   PubMed=16622700; DOI=10.1007/s00294-006-0073-2;
RA   da Silva Ferreira M.E., Malavazi I., Savoldi M., Brakhage A.A.,
RA   Goldman M.H., Kim H.S., Nierman W.C., Goldman G.H.;
RT   "Transcriptome analysis of Aspergillus fumigatus exposed to voriconazole.";
RL   Curr. Genet. 50:32-44(2006).
RN   [3]
RP   INDUCTION.
RX   PubMed=18648542; DOI=10.1371/journal.pone.0002655;
RA   Sugui J.A., Kim H.S., Zarember K.A., Chang Y.C., Gallin J.I., Nierman W.C.,
RA   Kwon-Chung K.J.;
RT   "Genes differentially expressed in conidia and hyphae of Aspergillus
RT   fumigatus upon exposure to human neutrophils.";
RL   PLoS ONE 3:E2655-E2655(2008).
RN   [4]
RP   INDUCTION.
RX   PubMed=21264256; DOI=10.1371/journal.pone.0016016;
RA   Morton C.O., Varga J.J., Hornbach A., Mezger M., Sennefelder H., Kneitz S.,
RA   Kurzai O., Krappmann S., Einsele H., Nierman W.C., Rogers T.R.,
RA   Loeffler J.;
RT   "The temporal dynamics of differential gene expression in Aspergillus
RT   fumigatus interacting with human immature dendritic cells in vitro.";
RL   PLoS ONE 6:E16016-E16016(2011).
CC   -!- FUNCTION: Major facilitator superfamily transporter that may be
CC       involved in A.fumigatus adaptation to azoles such as vorizonazole.
CC       {ECO:0000305|PubMed:16622700}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein.
CC   -!- INDUCTION: Expression is induced upon voriconazole treatment
CC       (PubMed:16622700). Expression is up-regulated by exposure to human
CC       monocyte-derived immature dendritic cells (PubMed:21264256). Expression
CC       is also up-regulated in conidia exposed to human neutrophils
CC       (PubMed:18648542). {ECO:0000269|PubMed:16622700,
CC       ECO:0000269|PubMed:18648542, ECO:0000269|PubMed:21264256}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC       transporter (TC 2.A.1.1) family. {ECO:0000305}.
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DR   EMBL; AAHF01000013; EAL85334.1; -; Genomic_DNA.
DR   RefSeq; XP_747372.1; XM_742279.1.
DR   AlphaFoldDB; Q4WC50; -.
DR   SMR; Q4WC50; -.
DR   STRING; 746128.CADAFUBP00007968; -.
DR   EnsemblFungi; EAL85334; EAL85334; AFUA_8G05710.
DR   GeneID; 3504696; -.
DR   KEGG; afm:AFUA_8G05710; -.
DR   VEuPathDB; FungiDB:Afu8g05710; -.
DR   eggNOG; KOG0254; Eukaryota.
DR   HOGENOM; CLU_001265_30_3_1; -.
DR   InParanoid; Q4WC50; -.
DR   OMA; ENLHMEK; -.
DR   OrthoDB; 430696at2759; -.
DR   Proteomes; UP000002530; Chromosome 8.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005351; F:carbohydrate:proton symporter activity; IBA:GO_Central.
DR   GO; GO:0008643; P:carbohydrate transport; IBA:GO_Central.
DR   GO; GO:0015793; P:glycerol transmembrane transport; IBA:GO_Central.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR005828; MFS_sugar_transport-like.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR003663; Sugar/inositol_transpt.
DR   InterPro; IPR005829; Sugar_transporter_CS.
DR   Pfam; PF00083; Sugar_tr; 1.
DR   PRINTS; PR00171; SUGRTRNSPORT.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   TIGRFAMs; TIGR00879; SP; 1.
DR   PROSITE; PS50850; MFS; 1.
DR   PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..542
FT                   /note="Major facilitator superfamily transporter mfsA"
FT                   /id="PRO_0000445110"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        70..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        127..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        321..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        349..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        380..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        413..432
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        444..464
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   542 AA;  60110 MW;  4074F95FE63743F1 CRC64;
     MWTTTSGLSG RSLRLSITFA AVVGFSLFGY NQGMMAGLLN GDEFVNSFPI LKMPDNPTAG
     EKHYIDVIRG AVTSCYELGC FFGALFSMFC GNRLGRTRLI FMGASILIVG ALLTTVCYTG
     KWEVGQFVIG RVVSGIGNGM NTATIPVWQS ECSGAHNRGF LVCFEGAMIA GGTFIAYWVV
     FGISHAADSV QWRFPVALQI FFALVVATGA LMLPDSPSWF VSRGLDNEAC EVLGKIKGTS
     PDSDQVLHDF NLIKTDMEST KSEQSNWKTV FTFGKTQEFQ RLLIGCSGQF FQQFTGCNAA
     IYYSTLLFQE NLHMEKYLSL IMGGVFASVY ALATIPSFFM IERVGRRKLY LIGFLGQGLS
     FVITFACLIK ETEENSKGAA VGIFLFITFF AFTLLPLPWI YPPEINPLRT RTVGASASTC
     TNWMCNFAVV MFTPLFAGQS PWGVYLFFAL FNFVGLIFGY FFYVETAGRE LEEVDIIYAK
     AHVEGKMPFR VAHDLPKLSF EEIVQQSREL GLDTNDHVML EKKELGLSSD SAQETEEVYE
     KQ
 
 
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