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   27-MAR-2024, entry version 196.
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};
GN   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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; 75.
DR   IntAct; P10870; 2.
DR   STRING; 4932.YDL194W; -.
DR   TCDB; 2.A.1.1.17; the major facilitator superfamily (mfs).
DR   GlyCosmos; P10870; 1 site, No reported glycans.
DR   GlyGen; P10870; 1 site.
DR   iPTMnet; P10870; -.
DR   PaxDb; 4932-YDL194W; -.
DR   PeptideAtlas; P10870; -.
DR   EnsemblFungi; YDL194W_mRNA; YDL194W; YDL194W.
DR   GeneID; 851333; -.
DR   KEGG; sce:YDL194W; -.
DR   AGR; SGD:S000002353; -.
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   OrthoDB; 1058279at2759; -.
DR   BioCyc; YEAST:G3O-29579-MONOMER; -.
DR   BioGRID-ORCS; 851333; 5 hits in 10 CRISPR screens.
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: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: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   CDD; cd17356; MFS_HXT; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 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   NCBIfam; TIGR00879; SP; 1.
DR   PANTHER; PTHR48022:SF17; HIGH GLUCOSE SENSOR RGT2-RELATED; 1.
DR   PANTHER; PTHR48022; PLASTIDIC GLUCOSE TRANSPORTER 4; 1.
DR   Pfam; PF00083; Sugar_tr; 1.
DR   PRINTS; PR00171; SUGRTRNSPORT.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 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
//