HGT1_CANAX
ID HGT1_CANAX Reviewed; 545 AA.
AC O74713;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=High-affinity glucose transporter;
GN Name=HGT1;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10261 / CBS 2718 / NBRC 1061 / FMJ 1011;
RX PubMed=10612724; DOI=10.1111/j.1574-6968.2000.tb08866.x;
RA Varma A., Singh B.B., Karnani N., Lichtenberg-Frate H., Hofer M.,
RA Magee B.B., Prasad R.;
RT "Molecular cloning and functional characterisation of a glucose
RT transporter, CaHGT1, of Candida albicans.";
RL FEMS Microbiol. Lett. 182:15-21(2000).
CC -!- FUNCTION: High-affinity glucose transporter.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
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; Y16834; CAA76406.1; -; Genomic_DNA.
DR AlphaFoldDB; O74713; -.
DR SMR; O74713; -.
DR MoonProt; O74713; -.
DR CGD; CAL0000200616; HGT1.
DR VEuPathDB; FungiDB:C1_01980W_A; -.
DR VEuPathDB; FungiDB:CAWG_01184; -.
DR GO; GO:1903561; C:extracellular vesicle; IDA:CGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:CGD.
DR GO; GO:0005886; C:plasma membrane; IDA:CGD.
DR GO; GO:0005355; F:glucose transmembrane transporter activity; IGI:CGD.
DR GO; GO:0034605; P:cellular response to heat; IMP:CGD.
DR GO; GO:0036244; P:cellular response to neutral pH; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0036168; P:filamentous growth of a population of unicellular organisms in response to heat; IMP:CGD.
DR GO; GO:0036178; P:filamentous growth of a population of unicellular organisms in response to neutral pH; IMP:CGD.
DR GO; GO:1904659; P:glucose transmembrane transport; IGI:CGD.
DR GO; GO:0045916; P:negative regulation of complement activation; IMP:CGD.
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; 2.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Membrane; Sugar transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..545
FT /note="High-affinity glucose transporter"
FT /id="PRO_0000050417"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..71
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..124
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..156
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..191
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..290
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..316
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..344
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 366..394
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..432
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 433..453
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 454..459
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 481..545
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 524..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 545 AA; 60670 MW; A9A0FD77DC70780E CRC64;
MSSKIERIFS GPALKINTYL DKLPKIYNVF FIASISTIAG MMFGFDISSM SAFIGAEHYM
RYFNSPGSDI QGFITSSMAL GSFFGSIASS FVSEPFGRRL SLLTCAFFWM VGAAIQSSVQ
NRAQLIIGRI ISGIGVGFGS AVAPVYGAEL APRKIRGLIG GMFQFFVTLG IMIMFYLSFG
LGHINGVASF RIAWGLQIVP GLCLFLGCFF IPESPRWLAK QGQWEAAEEI VAKIQAHGDR
ENPDVLIEIS EIKDQLLLEE SSKQIGYATL FTKKYIQRTF TAIFAQIWQQ LTGMNVMMYY
IVYIFQMAGY SGNSNLVASS IQYVINTCVT VPALYFIDKV GRRPLLIGGA TMMMAFQFGL
AGILGQYSIP WPDSGNDSVN IRIPEDNKSA SKGAIACCYL FVASFAFTWG VGIWVYCAEI
WGDNRVAQRG NAISTSANWI LNFAIAMYTP TGFKNISWKT YIIYGVFCFA MATHVYFGFP
ETKGKRLEEI GQMWEERVPA WRSRSWQPTV PIASDAELAR KMEVEHEEDK LMNEDSNSES
RENQA
