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2.A.1.1.108
Low-affinity glucose transporter HXT1 of 570 aas and 12 TMSs. Substitutions of equivalent salt bridge-forming residues in Hxt1, Rgt2, and Glut4 are predicted to lock them in an inward-facing conformation but lead to different functional consequences. The salt bridge networks in yeast and human glucose transporters and yeast glucose receptors may play different roles in maintaining their structural and functional integrity (Kim et al. 2023).

Accession Number:P32465
Protein Name:Low-affinity glucose transporter HXT1
Length:570
Molecular Weight:63261.00
Species:Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [559292]
Number of TMSs:12
Location1 / Topology2 / Orientation3: Membrane1 / Multi-pass membrane protein2
Substrate glucose

Cross database links:

DIP: DIP-5593N
Entrez Gene ID: 856494   
Pfam: PF00083   
KEGG: sce:YHR094C   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0005624 C:membrane fraction
GO:0005886 C:plasma membrane
GO:0005353 F:fructose transmembrane transporter activity
GO:0005354 F:galactose transmembrane transporter activity
GO:0005355 F:glucose transmembrane transporter activity
GO:0015578 F:mannose transmembrane transporter activity
GO:0015146 F:pentose transmembrane transporter activity

References (9)

[1] “The HXT1 gene product of Saccharomyces cerevisiae is a new member of the family of hexose transporters.”  Lewis D.A.et.al.   2046678
[2] “Roles of multiple glucose transporters in Saccharomyces cerevisiae.”  Ko C.H.et.al.   8417358
[3] “Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII.”  Johnston M.et.al.   8091229
[4] “Global analysis of protein expression in yeast.”  Ghaemmaghami S.et.al.   14562106
[5] “A proteomics approach to understanding protein ubiquitination.”  Peng J.et.al.   12872131
[6] “A global topology map of the Saccharomyces cerevisiae membrane proteome.”  Kim H.et.al.   16847258
[7] “Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.”  Li X.et.al.   17330950
[8] “Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.”  Chi A.et.al.   17287358
[9] “A multidimensional chromatography technology for in-depth phosphoproteome analysis.”  Albuquerque C.P.et.al.   18407956

External Searches:

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence 
1:	MNSTPDLISP QKSNSSNSYE LESGRSKAMN TPEGKNESFH DNLSESQVQP AVAPPNTGKG 
61:	VYVTVSICCV MVAFGGFIFG WDTGTISGFV AQTDFLRRFG MKHHDGSHYL SKVRTGLIVS 
121:	IFNIGCAIGG IVLAKLGDMY GRRIGLIVVV VIYTIGIIIQ IASINKWYQY FIGRIISGLG 
181:	VGGITVLSPM LISEVAPSEM RGTLVSCYQV MITLGIFLGY CTNFGTKNYS NSVQWRVPLG 
241:	LCFAWALFMI GGMMFVPESP RYLVEAGRID EARASLAKVN KCPPDHPYIQ YELETIEASV 
301:	EEMRAAGTAS WGELFTGKPA MFQRTMMGIM IQSLQQLTGD NYFFYYGTIV FQAVGLSDSF 
361:	ETSIVFGVVN FFSTCCSLYT VDRFGRRNCL MWGAVGMVCC YVVYASVGVT RLWPNGQDQP 
421:	SSKGAGNCMI VFACFYIFCF ATTWAPIAYV VISECFPLRV KSKCMSIASA ANWIWGFLIS 
481:	FFTPFITGAI NFYYGYVFMG CMVFAYFYVF FFVPETKGLS LEEVNDMYAE GVLPWKSASW 
541:	VPVSKRGADY NADDLMHDDQ PFYKSLFSRK