SNF3_YEAST
ID SNF3_YEAST Reviewed; 884 AA.
AC P10870; D6VRF9;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Low glucose sensor SNF3 {ECO:0000305|PubMed:8901598};
DE AltName: Full=High-affinity glucose receptor SNF3 {ECO:0000303|PubMed:8901598};
DE AltName: Full=High-affinity transporter-like sensor SNF3 {ECO:0000303|PubMed:20014043};
DE AltName: Full=Sucrose nonfermenting protein 3 {ECO:0000303|PubMed:6392017};
GN Name=SNF3 {ECO:0000303|PubMed:6392017};
GN OrderedLocusNames=YDL194W {ECO:0000312|SGD:S000002353}; ORFNames=D1234;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX PubMed=3281163; DOI=10.1073/pnas.85.7.2130;
RA Celenza J.L., Marshall-Carlson L., Carlson M.;
RT "The yeast SNF3 gene encodes a glucose transporter homologous to the
RT mammalian protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:2130-2134(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8896272;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1065::aid-yea995>3.0.co;2-f;
RA Verhasselt P., Voet M., Mathys J., Volckaert G.;
RT "The sequence of 23 kb surrounding the SNF3 locus on the left arm of yeast
RT chromosome IV reveals the location of five known genes and characterizes at
RT least six new open reading frames including putative genes for ribosomal
RT protein L35 and a sugar transport protein.";
RL Yeast 12:1065-1070(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP GENE NAME.
RX PubMed=6392017; DOI=10.1093/genetics/108.4.845;
RA Neigeborn L., Carlson M.;
RT "Genes affecting the regulation of SUC2 gene expression by glucose
RT repression in Saccharomyces cerevisiae.";
RL Genetics 108:845-858(1984).
RN [6]
RP MUTAGENESIS OF GLY-112; GLY-153; ARG-229 AND VAL-402, AND SUBCELLULAR
RP LOCATION.
RX PubMed=2406560; DOI=10.1128/mcb.10.3.1105-1115.1990;
RA Marshall-Carlson L., Celenza J.L., Laurent B.C., Carlson M.;
RT "Mutational analysis of the SNF3 glucose transporter of Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 10:1105-1115(1990).
RN [7]
RP FUNCTION.
RX PubMed=8901598; DOI=10.1073/pnas.93.22.12428;
RA Oezcan S., Dover J., Rosenwald A.G., Woelfl S., Johnston M.;
RT "Two glucose transporters in Saccharomyces cerevisiae are glucose sensors
RT that generate a signal for induction of gene expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:12428-12432(1996).
RN [8]
RP FUNCTION.
RX PubMed=9046082;
RX DOI=10.1002/(sici)1097-0061(199701)13:1<9::aid-yea51>3.0.co;2-u;
RA Coons D.M., Vagnoli P., Bisson L.F.;
RT "The C-terminal domain of Snf3p is sufficient to complement the growth
RT defect of snf3 null mutations in Saccharomyces cerevisiae: SNF3 functions
RT in glucose recognition.";
RL Yeast 13:9-20(1997).
RN [9]
RP FUNCTION.
RX PubMed=9564039; DOI=10.1093/emboj/17.9.2566;
RA Ozcan S., Dover J., Johnston M.;
RT "Glucose sensing and signaling by two glucose receptors in the yeast
RT Saccharomyces cerevisiae.";
RL EMBO J. 17:2566-2573(1998).
RN [10]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP FUNCTION, AND MUTAGENESIS OF ILE-374 AND PHE-462.
RX PubMed=20014043; DOI=10.1002/yea.1737;
RA Dietvorst J., Karhumaa K., Kielland-Brandt M.C., Brandt A.;
RT "Amino acid residues involved in ligand preference of the Snf3 transporter-
RT like sensor in Saccharomyces cerevisiae.";
RL Yeast 27:131-138(2010).
CC -!- FUNCTION: High-affinity low glucose sensor that is part of the
CC sensor/receptor-repressor (SSR) glucose-signaling pathway, which
CC detects extracellular glucose and induces expression of glucose
CC transporters that bring glucose into the cell (PubMed:8901598,
CC PubMed:9564039). The transporter-like sensor generates an intracellular
CC signal in the presence of low levels of glucose to promote low glucose-
CC induced expression of HXT2 (PubMed:9564039). Binding of glucose to the
CC SNF3 transmembrane domain activates a downstream signaling cascade,
CC leading to phosphorylation of the RGT1 corepressors MTH1 and STD1,
CC targeting them for SCF(Grr1)-dependent ubiquitination and degradation.
CC Depletion of the corepressors robs RGT1 of its ability to repress
CC expression of HXT genes, leading to accumulation of glucose
CC transporters in the plasma membrane (By similarity). SNF3 is involved
CC as well in the transport of mannose and fructose (PubMed:20014043).
CC Even though SNF3 is similar to glucose transporters, it appears to be
CC unable to transport glucose (PubMed:9564039).
CC {ECO:0000250|UniProtKB:Q12300, ECO:0000269|PubMed:20014043,
CC ECO:0000269|PubMed:8901598, ECO:0000269|PubMed:9564039}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2406560,
CC ECO:0000269|PubMed:3281163}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:3281163}.
CC -!- INDUCTION: Glucose-repressible.
CC -!- DOMAIN: The C-terminal cytoplasmic domain seems to be important for
CC SNF3 regulatory function. {ECO:0000305|PubMed:9046082}.
CC -!- PTM: Phosphorylated in the C-terminal tail on Yck consensus sites in a
CC yeast casein kinases YCK1 and YCK2 (Yck)-dependent manner. This
CC phosphorylation is required for interaction with HXT corepressors MTH1
CC and STD1 and ultimately HXT expression. {ECO:0000250|UniProtKB:Q12300}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA58253.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; J03246; AAA35060.1; -; Genomic_DNA.
DR EMBL; X83276; CAA58253.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z74242; CAA98771.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11669.1; -; Genomic_DNA.
DR PIR; A31928; A31928.
DR RefSeq; NP_010087.1; NM_001180254.1.
DR AlphaFoldDB; P10870; -.
DR SMR; P10870; -.
DR BioGRID; 31851; 74.
DR IntAct; P10870; 2.
DR STRING; 4932.YDL194W; -.
DR TCDB; 2.A.1.1.17; the major facilitator superfamily (mfs).
DR iPTMnet; P10870; -.
DR PaxDb; P10870; -.
DR PRIDE; P10870; -.
DR EnsemblFungi; YDL194W_mRNA; YDL194W; YDL194W.
DR GeneID; 851333; -.
DR KEGG; sce:YDL194W; -.
DR SGD; S000002353; SNF3.
DR VEuPathDB; FungiDB:YDL194W; -.
DR eggNOG; KOG0254; Eukaryota.
DR GeneTree; ENSGT00940000176821; -.
DR HOGENOM; CLU_001265_42_0_1; -.
DR InParanoid; P10870; -.
DR OMA; NDYMAQL; -.
DR BioCyc; YEAST:G3O-29579-MON; -.
DR PRO; PR:P10870; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P10870; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
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; IDA:SGD.
DR GO; GO:0005351; F:carbohydrate:proton symporter activity; IBA:GO_Central.
DR GO; GO:0005536; F:glucose binding; TAS:SGD.
DR GO; GO:0008643; P:carbohydrate transport; IBA:GO_Central.
DR GO; GO:0051594; P:detection of glucose; IMP:SGD.
DR GO; GO:0015755; P:fructose transmembrane transport; IMP:SGD.
DR GO; GO:0010255; P:glucose mediated signaling pathway; IMP:SGD.
DR GO; GO:1904659; P:glucose transmembrane transport; IMP:SGD.
DR GO; GO:0015761; P:mannose transmembrane transport; IMP:SGD.
DR GO; GO:0045835; P:negative regulation of meiotic nuclear division; IMP:SGD.
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; IPR037792; Rgt2/Snf3.
DR InterPro; IPR003663; Sugar/inositol_transpt.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR PANTHER; PTHR48022:SF16; PTHR48022:SF16; 1.
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.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..884
FT /note="Low glucose sensor SNF3"
FT /id="PRO_0000050390"
FT TOPO_DOM 1..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 98..118
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..143
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 144..164
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 179..199
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..202
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 203..223
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 230..250
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..264
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 265..285
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..358
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 359..379
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 380..391
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 392..412
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 413..419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 420..440
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 441..451
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 452..472
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..488
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 489..509
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 510..521
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 522..542
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 543..884
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
FT REGION 30..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..725
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 112
FT /note="G->D: In SNF3-142."
FT /evidence="ECO:0000269|PubMed:2406560"
FT MUTAGEN 153
FT /note="G->R: In SNF3-72."
FT /evidence="ECO:0000269|PubMed:2406560"
FT MUTAGEN 229
FT /note="R->K: In SNF3-1; constitutively signaling glucose
FT receptor."
FT /evidence="ECO:0000269|PubMed:2406560"
FT MUTAGEN 374
FT /note="I->V: Decreases responsiveness to mannose and
FT fructose."
FT /evidence="ECO:0000269|PubMed:20014043"
FT MUTAGEN 402
FT /note="V->I: In SNF3-39."
FT /evidence="ECO:0000269|PubMed:2406560"
FT MUTAGEN 462
FT /note="F->Y: Decreases responsiveness to fructose."
FT /evidence="ECO:0000269|PubMed:20014043"
SQ SEQUENCE 884 AA; 96719 MW; 8E2A5A1A7739344F CRC64;
MDPNSNSSSE TLRQEKQGFL DKALQRVKGI ALRRNNSNKD HTTDDTTGSI RTPTSLQRQN
SDRQSNMTSV FTDDISTIDD NSILFSEPPQ KQSMMMSICV GVFVAVGGFL FGYDTGLINS
ITSMNYVKSH VAPNHDSFTA QQMSILVSFL SLGTFFGALT APFISDSYGR KPTIIFSTIF
IFSIGNSLQV GAGGITLLIV GRVISGIGIG AISAVVPLYQ AEATHKSLRG AIISTYQWAI
TWGLLVSSAV SQGTHARNDA SSYRIPIGLQ YVWSSFLAIG MFFLPESPRY YVLKDKLDEA
AKSLSFLRGV PVHDSGLLEE LVEIKATYDY EASFGSSNFI DCFISSKSRP KQTLRMFTGI
ALQAFQQFSG INFIFYYGVN FFNKTGVSNS YLVSFITYAV NVVFNVPGLF FVEFFGRRKV
LVVGGVIMTI ANFIVAIVGC SLKTVAAAKV MIAFICLFIA AFSATWGGVV WVISAELYPL
GVRSKCTAIC AAANWLVNFI CALITPYIVD TGSHTSSLGA KIFFIWGSLN AMGVIVVYLT
VYETKGLTLE EIDELYIKSS TGVVSPKFNK DIRERALKFQ YDPLQRLEDG KNTFVAKRNN
FDDETPRNDF RNTISGEIDH SPNQKEVHSI PERVDIPTST EILESPNKSS GMTVPVSPSL
QDVPIPQTTE PAEIRTKYVD LGNGLGLNTY NRGPPSLSSD SSEDYTEDEI GGPSSQGDQS
NRSTMNDIND YMARLIHSTS TASNTTDKFS GNQSTLRYHT ASSHSDTTEE DSNLMDLGNG
LALNAYNRGP PSILMNSSDE EANGGETSDN LNTAQDLAGM KERMAQFAQS YIDKRGGLEP
ETQSNILSTS LSVMADTNEH NNEILHSSEE NATNQPVNEN NDLK
