P10870 (SNF3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
High-affinity glucose transporter SNF3

Gene names

Name:	SNF3
Ordered Locus Names:	YDL194W
ORF Names:	D1234

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	884 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	High-affinity glucose transporter. Can function as a negative regulator of glucose transport. SNF3 is involved as well in the transport of mannose and fructose. Serves as a sensor that generates an intracellular signal in the presence of low level of glucose. Inhibition of RGT1 by low levels of glucose, and hence induction of HTX2 and HTX4 expression, requires SNF3.
Subcellular location	Cell membrane; Multi-pass membrane protein Ref.1.
Induction	Glucose-repressible.
Domain	The C-terminal cytoplasmic domain seems to be important for SNF3 regulatory function.
Miscellaneous	Glucose transport is thought to be mediated by two kinetically distinct systems, a glucose-repressible high-affinity system and a constitutive low-affinity system.
Sequence similarities	Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family. [View classification]
Sequence caution	The sequence CAA58253.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Sugar transport Transport
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	detection of glucose Inferred from mutant phenotype. Source: SGD fructose transport Inferred from mutant phenotype. Source: SGD glucose transport Inferred from mutant phenotype. Source: SGD mannose transport Inferred from mutant phenotype. Source: SGD negative regulation of meiosis Inferred from mutant phenotype. Source: SGD signal transduction Traceable author statement. Source: SGD
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay Ref.5. Source: SGD
Molecular function	glucose binding Traceable author statement. Source: SGD receptor activity Traceable author statement. Source: SGD substrate-specific transmembrane transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 884	884	High-affinity glucose transporter SNF3		PRO_0000050390
Regions
	Topological domain	1 – 97	97	Cytoplasmic Potential
	Transmembrane	98 – 118	21	Helical; Name=1; Potential
	Topological domain	119 – 143	25	Extracellular Potential
	Transmembrane	144 – 164	21	Helical; Name=2; Potential
	Topological domain	165 – 178	14	Cytoplasmic Potential
	Transmembrane	179 – 199	21	Helical; Name=3; Potential
	Topological domain	200 – 202	3	Extracellular Potential
	Transmembrane	203 – 223	21	Helical; Name=4; Potential
	Topological domain	224 – 229	6	Cytoplasmic Potential
	Transmembrane	230 – 250	21	Helical; Name=5; Potential
	Topological domain	251 – 264	14	Extracellular Potential
	Transmembrane	265 – 285	21	Helical; Name=6; Potential
	Topological domain	286 – 358	73	Cytoplasmic Potential
	Transmembrane	359 – 379	21	Helical; Name=7; Potential
	Topological domain	380 – 391	12	Extracellular Potential
	Transmembrane	392 – 412	21	Helical; Name=8; Potential
	Topological domain	413 – 419	7	Cytoplasmic Potential
	Transmembrane	420 – 440	21	Helical; Name=9; Potential
	Topological domain	441 – 451	11	Extracellular Potential
	Transmembrane	452 – 472	21	Helical; Name=10; Potential
	Topological domain	473 – 488	16	Cytoplasmic Potential
	Transmembrane	489 – 509	21	Helical; Name=11; Potential
	Topological domain	510 – 521	12	Extracellular Potential
	Transmembrane	522 – 542	21	Helical; Name=12; Potential
	Topological domain	543 – 884	342	Cytoplasmic Potential
Amino acid modifications
	Modified residue	720	1	Phosphoserine Ref.8
	Modified residue	724	1	Phosphothreonine Ref.8
	Glycosylation	383	1	N-linked (GlcNAc...) Potential
Experimental info
	Mutagenesis	112	1	G → D in SNF3-142. Ref.5
	Mutagenesis	153	1	G → R in SNF3-72. Ref.5
	Mutagenesis	229	1	R → K in SNF3-1; constitutively signaling glucose receptor. Ref.5
	Mutagenesis	402	1	V → I in SNF3-39. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P10870 [UniParc]. Last modified October 3, 2006. Version 3. Checksum: 8E2A5A1A7739344F	FASTA	884	96,719
	10 20 30 40 50 60 MDPNSNSSSE TLRQEKQGFL DKALQRVKGI ALRRNNSNKD HTTDDTTGSI RTPTSLQRQN 70 80 90 100 110 120 SDRQSNMTSV FTDDISTIDD NSILFSEPPQ KQSMMMSICV GVFVAVGGFL FGYDTGLINS 130 140 150 160 170 180 ITSMNYVKSH VAPNHDSFTA QQMSILVSFL SLGTFFGALT APFISDSYGR KPTIIFSTIF 190 200 210 220 230 240 IFSIGNSLQV GAGGITLLIV GRVISGIGIG AISAVVPLYQ AEATHKSLRG AIISTYQWAI 250 260 270 280 290 300 TWGLLVSSAV SQGTHARNDA SSYRIPIGLQ YVWSSFLAIG MFFLPESPRY YVLKDKLDEA 310 320 330 340 350 360 AKSLSFLRGV PVHDSGLLEE LVEIKATYDY EASFGSSNFI DCFISSKSRP KQTLRMFTGI 370 380 390 400 410 420 ALQAFQQFSG INFIFYYGVN FFNKTGVSNS YLVSFITYAV NVVFNVPGLF FVEFFGRRKV 430 440 450 460 470 480 LVVGGVIMTI ANFIVAIVGC SLKTVAAAKV MIAFICLFIA AFSATWGGVV WVISAELYPL 490 500 510 520 530 540 GVRSKCTAIC AAANWLVNFI CALITPYIVD TGSHTSSLGA KIFFIWGSLN AMGVIVVYLT 550 560 570 580 590 600 VYETKGLTLE EIDELYIKSS TGVVSPKFNK DIRERALKFQ YDPLQRLEDG KNTFVAKRNN 610 620 630 640 650 660 FDDETPRNDF RNTISGEIDH SPNQKEVHSI PERVDIPTST EILESPNKSS GMTVPVSPSL 670 680 690 700 710 720 QDVPIPQTTE PAEIRTKYVD LGNGLGLNTY NRGPPSLSSD SSEDYTEDEI GGPSSQGDQS 730 740 750 760 770 780 NRSTMNDIND YMARLIHSTS TASNTTDKFS GNQSTLRYHT ASSHSDTTEE DSNLMDLGNG 790 800 810 820 830 840 LALNAYNRGP PSILMNSSDE EANGGETSDN LNTAQDLAGM KERMAQFAQS YIDKRGGLEP 850 860 870 880 ETQSNILSTS LSVMADTNEH NNEILHSSEE NATNQPVNEN NDLK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The yeast SNF3 gene encodes a glucose transporter homologous to the mammalian protein." Celenza J.L., Marshall-Carlson L., Carlson M. Proc. Natl. Acad. Sci. U.S.A. 85:2130-2134(1988) [PubMed: 3281163] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
[2]	"The sequence of 23 kb surrounding the SNF3 locus on the left arm of yeast chromosome IV reveals the location of five known genes and characterizes at least six new open reading frames including putative genes for ribosomal protein L35 and a sugar transport protein." Verhasselt P., Voet M., Mathys J., Volckaert G. Yeast 12:1065-1070(1996) [PubMed: 8896272] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Mutational analysis of the SNF3 glucose transporter of Saccharomyces cerevisiae." Marshall-Carlson L., Celenza J.L., Laurent B.C., Carlson M. Mol. Cell. Biol. 10:1105-1115(1990) [PubMed: 2406560] [Abstract] Cited for: MUTAGENESIS OF GLY-112; GLY-153; ARG-229 AND VAL-402.
[6]	"The C-terminal domain of Snf3p is sufficient to complement the growth defect of snf3 null mutations in Saccharomyces cerevisiae: SNF3 functions in glucose recognition." Coons D.M., Vagnoli P., Bisson L.F. Yeast 13:9-20(1997) [PubMed: 9046082] [Abstract] Cited for: CHARACTERIZATION.
[7]	"A global topology map of the Saccharomyces cerevisiae membrane proteome." Kim H., Melen K., Oesterberg M., von Heijne G. Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed: 16847258] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS]. Strain: ATCC 208353 / W303-1A.
[8]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-720 AND THR-724, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J03246 Genomic DNA. Translation: AAA35060.1. X83276 Genomic DNA. Translation: CAA58253.1. Different initiation. Z74242 Genomic DNA. Translation: CAA98771.1. BK006938 Genomic DNA. Translation: DAA11669.1.
PIR	A31928.
RefSeq	NP_010087.1. NM_001180254.1.
3D structure databases
ProteinModelPortal	P10870.
ModBase	Search...
Protein-protein interaction databases
IntAct	P10870. 2 interactions.
STRING	P10870.
Protein family/group databases
TCDB	2.A.1.1.17. major facilitator superfamily (MFS).
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YDL194W; YDL194W; YDL194W.
GeneID	851333.
KEGG	sce:YDL194W.
NMPDR	fig|4932.3.peg.820.
Organism-specific databases
CYGD	YDL194w.
SGD	S000002353. SNF3.
Phylogenomic databases
eggNOG	fuNOG04879.
GeneTree	EFGT00070000008710.
HOGENOM	HBG744444.
OrthoDB	EOG44J5SK.
Gene expression databases
ArrayExpress	P10870.
Genevestigator	P10870.
GermOnline	YDL194W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR020846. MFS_dom. IPR016196. MFS_dom_general_subst_transpt. IPR005828. Sub_transporter. IPR003663. Sugar/inositol_transpt. IPR005829. Sugar_transporter_CS. [Graphical view]
KO	K08139.
Pfam	PF00083. Sugar_tr. 1 hit. [Graphical view]
PRINTS	PR00171. SUGRTRNSPORT.
SUPFAM	SSF103473. MFS_gen_substrate_transporter. 1 hit.
TIGRFAMs	TIGR00879. SP. 1 hit.
PROSITE	PS50850. MFS. 1 hit. PS00216. SUGAR_TRANSPORT_1. 1 hit. PS00217. SUGAR_TRANSPORT_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	968396.

Entry information

Entry name

SNF3_YEAST

Accession

Primary (citable) accession number: P10870
Secondary accession number(s): D6VRF9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	October 3, 2006
Last modified:	December 14, 2011
This is version 110 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program