HGT1_CANAL
ID HGT1_CANAL Reviewed; 545 AA.
AC A0A1D8PCL1;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 18-JAN-2017, sequence version 1.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=High-affinity glucose transporter 1 {ECO:0000303|PubMed:10612724};
GN Name=HGT1 {ECO:0000303|PubMed:10612724}; Synonyms=HGT11;
GN OrderedLocusNames=CAALFM_C101980WA; ORFNames=orf19.4527;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP FUNCTION, AND INDUCTION.
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).
RN [5]
RP FUNCTION, AND INDUCTION.
RX PubMed=12187386; DOI=10.1007/s00239-002-2330-4;
RA Fan J., Chaturvedi V., Shen S.H.;
RT "Identification and phylogenetic analysis of a glucose transporter gene
RT family from the human pathogenic yeast Candida albicans.";
RL J. Mol. Evol. 55:336-346(2002).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH HOST COMPLEMENT
RP FACTORS FH AND C4BP AND HIV GP160.
RX PubMed=21844307; DOI=10.1093/infdis/jir455;
RA Lesiak-Markowicz I., Vogl G., Schwarzmueller T., Speth C., Lass-Floerl C.,
RA Dierich M.P., Kuchler K., Wuerzner R.;
RT "Candida albicans Hgt1p, a multifunctional evasion molecule: complement
RT inhibitor, CR3 analogue, and human immunodeficiency virus-binding
RT molecule.";
RL J. Infect. Dis. 204:802-809(2011).
CC -!- FUNCTION: High-affinity glucose transporter (PubMed:10612724,
CC PubMed:12187386). Acts as a multifunctional complement-evasion molecule
CC that causes down-regulation of complement activation by acquisition of
CC human complement factors FH and C4BP (PubMed:21844307). Functions also
CC as a human immunodeficiency virus (HIV) receptor via binding the viral
CC gp160 protein (PubMed:21844307). Modulates hyphae formation
CC (PubMed:21844307). {ECO:0000269|PubMed:10612724,
CC ECO:0000269|PubMed:21844307, ECO:0000305|PubMed:12187386}.
CC -!- SUBUNIT: Interacts with the human complement factors FH and C4BP
CC (PubMed:21844307). Binds also human immunodeficiency virus (HIV)
CC protein gp160 (PubMed:21844307). {ECO:0000269|PubMed:21844307}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expressed in presence of 2 percent glucose
CC (PubMed:12187386). Expression is induced by progesterone and drugs such
CC as cycloheximide, benomyl and chloramphenicol (PubMed:10612724).
CC {ECO:0000269|PubMed:10612724, ECO:0000269|PubMed:12187386}.
CC -!- DISRUPTION PHENOTYPE: Reduces the binding of human FH and C4Bp as well
CC as of human immunodeficiency virus (HIV) gp160 protein onto C.albicans
CC cell surface (PubMed:21844307). Reduces ability to form hyphae
CC (PubMed:21844307). {ECO:0000269|PubMed:21844307}.
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; CP017623; AOW25884.1; -; Genomic_DNA.
DR RefSeq; XP_712952.2; XM_707859.2.
DR AlphaFoldDB; A0A1D8PCL1; -.
DR SMR; A0A1D8PCL1; -.
DR STRING; 237561.A0A1D8PCL1; -.
DR GeneID; 3645420; -.
DR KEGG; cal:CAALFM_C101980WA; -.
DR VEuPathDB; FungiDB:C1_01980W_A; -.
DR eggNOG; KOG0254; Eukaryota.
DR OrthoDB; 430696at2759; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005351; F:carbohydrate:proton symporter activity; IBA:GO_Central.
DR GO; GO:0008643; P:carbohydrate 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; 2.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..545
FT /note="High-affinity glucose transporter 1"
FT /id="PRO_0000443417"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical"
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|PROSITE-ProRule:PRU00498"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
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
