GLUT4_RAT
ID GLUT4_RAT Reviewed; 509 AA.
AC P19357; P97900;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Solute carrier family 2, facilitated glucose transporter member 4 {ECO:0000305};
DE AltName: Full=Glucose transporter type 4, insulin-responsive {ECO:0000303|PubMed:9059504};
DE Short=GLUT-4 {ECO:0000303|PubMed:9059504};
GN Name=Slc2a4 {ECO:0000312|RGD:2711};
GN Synonyms=Glut4 {ECO:0000303|PubMed:9059504};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TRANSPORTER ACTIVITY.
RX PubMed=2649253; DOI=10.1016/0092-8674(89)90968-9;
RA Birnbaum M.J.;
RT "Identification of a novel gene encoding an insulin-responsive glucose
RT transporter protein.";
RL Cell 57:305-315(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TRANSPORTER ACTIVITY.
RX PubMed=2645527; DOI=10.1038/338083a0;
RA James D.E., Strube M., Mueckler M.;
RT "Molecular cloning and characterization of an insulin-regulatable glucose
RT transporter.";
RL Nature 338:83-87(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=2649883; DOI=10.1073/pnas.86.8.2535;
RA Charron M.J., Brosius F.C. III, Alper S.L., Lodish H.F.;
RT "A glucose transport protein expressed predominately in insulin-responsive
RT tissues.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:2535-2539(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=9059504; DOI=10.1016/s0005-2736(96)00217-9;
RA Kasahara T., Kasahara M.;
RT "Characterization of rat Glut4 glucose transporter expressed in the yeast
RT Saccharomyces cerevisiae: comparison with Glut1 glucose transporter.";
RL Biochim. Biophys. Acta 1324:111-119(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
RX PubMed=7545962; DOI=10.1016/s0021-9258(18)46957-8;
RA Liu M.L., Olson A.L., Edgington N.P., Moye-Rowley W.S., Pessin J.E.;
RT "Myocyte enhancer factor 2 (MEF2) binding site is essential for C2C12
RT myotube-specific expression of the rat GLUT4/muscle-adipose facilitative
RT glucose transporter gene.";
RL J. Biol. Chem. 269:28514-28521(1994).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-25.
RX PubMed=7720644; DOI=10.1210/endo.136.5.7720644;
RA Olson A.L., Edgington N.P., Moye-Rowley W.S., Pessin J.E.;
RT "Characterization of 5'-heterogeneity of the rat GLUT4/muscle-adipose
RT glucose transporter gene product.";
RL Endocrinology 136:1962-1968(1995).
RN [8]
RP FUNCTION, TRANSPORTER ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=2211693; DOI=10.1016/s0021-9258(17)44734-x;
RA Holman G.D., Kozka I.J., Clark A.E., Flower C.J., Saltis J.,
RA Habberfield A.D., Simpson I.A., Cushman S.W.;
RT "Cell surface labeling of glucose transporter isoform GLUT4 by bis-mannose
RT photolabel. Correlation with stimulation of glucose transport in rat
RT adipose cells by insulin and phorbol ester.";
RL J. Biol. Chem. 265:18172-18179(1990).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=1651337; DOI=10.1083/jcb.114.4.689;
RA Haney P.M., Slot J.W., Piper R.C., James D.E., Mueckler M.;
RT "Intracellular targeting of the insulin-regulatable glucose transporter
RT (GLUT4) is isoform specific and independent of cell type.";
RL J. Cell Biol. 114:689-699(1991).
RN [10]
RP INTERACTION WITH NDUFA9.
RX PubMed=16396496; DOI=10.1021/pr0502626;
RA Foster L.J., Rudich A., Talior I., Patel N., Huang X., Furtado L.M.,
RA Bilan P.J., Mann M., Klip A.;
RT "Insulin-dependent interactions of proteins with GLUT4 revealed through
RT stable isotope labeling by amino acids in cell culture (SILAC).";
RL J. Proteome Res. 5:64-75(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND SER-488, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=26240143; DOI=10.1074/jbc.m115.657361;
RA Fazakerley D.J., Naghiloo S., Chaudhuri R., Koumanov F., Burchfield J.G.,
RA Thomas K.C., Krycer J.R., Prior M.J., Parker B.L., Murrow B.A.,
RA Stoeckli J., Meoli C.C., Holman G.D., James D.E.;
RT "Proteomic Analysis of GLUT4 Storage Vesicles Reveals Tumor Suppressor
RT Candidate 5 (TUSC5) as a Novel Regulator of Insulin Action in Adipocytes.";
RL J. Biol. Chem. 290:23528-23542(2015).
CC -!- FUNCTION: Insulin-regulated facilitative glucose transporter, which
CC plays a key role in removal of glucose from circulation
CC (PubMed:2649253, PubMed:2645527, PubMed:2211693). Response to insulin
CC is regulated by its intracellular localization: in the absence of
CC insulin, it is efficiently retained intracellularly within storage
CC compartments in muscle and fat cells (PubMed:2649253, PubMed:2645527,
CC PubMed:2211693). Upon insulin stimulation, translocates from these
CC compartments to the cell surface where it transports glucose from the
CC extracellular milieu into the cell (PubMed:2649253, PubMed:2645527,
CC PubMed:2211693). {ECO:0000269|PubMed:2211693,
CC ECO:0000269|PubMed:2645527, ECO:0000269|PubMed:2649253}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376,
CC ChEBI:CHEBI:4167; Evidence={ECO:0000269|PubMed:2211693,
CC ECO:0000269|PubMed:2645527, ECO:0000269|PubMed:2649253};
CC -!- SUBUNIT: Binds to DAXX. Interacts via its N-terminus with SRFBP1 (By
CC similarity). Interacts with NDUFA9 (PubMed:16396496). Interacts with
CC TRARG1; the interaction is required for proper SLC2A4 recycling after
CC insulin stimulation (By similarity). {ECO:0000250|UniProtKB:P14142,
CC ECO:0000250|UniProtKB:P14672, ECO:0000269|PubMed:16396496}.
CC -!- INTERACTION:
CC P19357; Q9QXQ0: Actn4; NbExp=3; IntAct=EBI-915426, EBI-919056;
CC P19357; P04797: Gapdh; NbExp=2; IntAct=EBI-915426, EBI-349219;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2211693};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P14142}.
CC Endomembrane system {ECO:0000269|PubMed:26240143}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P14142}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:P14142}. Note=Localizes primarily to the
CC perinuclear region, undergoing continued recycling to the plasma
CC membrane where it is rapidly reinternalized (By similarity). The
CC dileucine internalization motif is critical for intracellular
CC sequestration (By similarity). Insulin stimulation induces
CC translocation to the cell membrane (PubMed:2211693).
CC {ECO:0000250|UniProtKB:P14142, ECO:0000250|UniProtKB:P14672,
CC ECO:0000269|PubMed:2211693}.
CC -!- TISSUE SPECIFICITY: Expressed in skeletal and cardiac muscles
CC (PubMed:2649883). Expressed in brown and white adipose tissues
CC (PubMed:2649883). {ECO:0000269|PubMed:2649883}.
CC -!- DOMAIN: The dileucine internalization motif is critical for
CC intracellular sequestration. {ECO:0000250|UniProtKB:P14672}.
CC -!- PTM: Sumoylated. {ECO:0000250|UniProtKB:P14672}.
CC -!- PTM: Palmitoylated. Palmitoylation by ZDHHC7 controls the insulin-
CC dependent translocation of GLUT4 to the plasma membrane.
CC {ECO:0000250|UniProtKB:P14672}.
CC -!- DISEASE: Note=It is a candidate for certain post-receptor defects in
CC non-insulin-dependent diabetes mellitus.
CC -!- MISCELLANEOUS: Insulin-stimulated phosphorylation of TBC1D4 is required
CC for GLUT4 translocation. {ECO:0000250|UniProtKB:P14142}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. Glucose transporter subfamily.
CC {ECO:0000305}.
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DR EMBL; M25482; AAA41451.1; -; mRNA.
DR EMBL; X14771; CAA32879.1; -; mRNA.
DR EMBL; J04524; AAA41453.1; -; mRNA.
DR EMBL; D28561; BAA05911.1; -; mRNA.
DR EMBL; BC085757; AAH85757.1; -; mRNA.
DR EMBL; L36125; AAA65751.1; -; Genomic_DNA.
DR EMBL; S77784; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A32101; A32101.
DR RefSeq; NP_036883.1; NM_012751.1.
DR RefSeq; XP_006246658.1; XM_006246596.3.
DR AlphaFoldDB; P19357; -.
DR SMR; P19357; -.
DR BioGRID; 247208; 1.
DR IntAct; P19357; 634.
DR STRING; 10116.ENSRNOP00000023256; -.
DR BindingDB; P19357; -.
DR ChEMBL; CHEMBL3286066; -.
DR GlyGen; P19357; 1 site.
DR iPTMnet; P19357; -.
DR PhosphoSitePlus; P19357; -.
DR PaxDb; P19357; -.
DR PRIDE; P19357; -.
DR Ensembl; ENSRNOT00000023256; ENSRNOP00000023256; ENSRNOG00000017226.
DR GeneID; 25139; -.
DR KEGG; rno:25139; -.
DR UCSC; RGD:2711; rat.
DR CTD; 6517; -.
DR RGD; 2711; Slc2a4.
DR eggNOG; KOG0569; Eukaryota.
DR GeneTree; ENSGT00940000160688; -.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; P19357; -.
DR OMA; KVQWRFF; -.
DR OrthoDB; 749998at2759; -.
DR PhylomeDB; P19357; -.
DR TreeFam; TF313762; -.
DR Reactome; R-RNO-189200; Cellular hexose transport.
DR PRO; PR:P19357; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000017226; Expressed in skeletal muscle tissue and 17 other tissues.
DR Genevisible; P19357; RN.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005905; C:clathrin-coated pit; IDA:RGD.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0012505; C:endomembrane system; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0070062; C:extracellular exosome; ISO:RGD.
DR GO; GO:0032593; C:insulin-responsive compartment; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0005771; C:multivesicular body; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0042383; C:sarcolemma; IDA:ARUK-UCL.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:RGD.
DR GO; GO:0030315; C:T-tubule; IDA:RGD.
DR GO; GO:0005802; C:trans-Golgi network; ISO:RGD.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; ISO:RGD.
DR GO; GO:0012506; C:vesicle membrane; ISO:RGD.
DR GO; GO:0055056; F:D-glucose transmembrane transporter activity; IDA:RGD.
DR GO; GO:0005355; F:glucose transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015304; F:glucose uniporter activity; IDA:UniProtKB.
DR GO; GO:0015149; F:hexose transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0010021; P:amylopectin biosynthetic process; ISO:RGD.
DR GO; GO:0050873; P:brown fat cell differentiation; ISO:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; IDA:RGD.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
DR GO; GO:0071470; P:cellular response to osmotic stress; ISO:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISO:RGD.
DR GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
DR GO; GO:0046323; P:glucose import; IMP:BHF-UCL.
DR GO; GO:0044381; P:glucose import in response to insulin stimulus; IDA:UniProtKB.
DR GO; GO:1904659; P:glucose transmembrane transport; IDA:UniProtKB.
DR GO; GO:0007611; P:learning or memory; IDA:ARUK-UCL.
DR GO; GO:0007616; P:long-term memory; IMP:ARUK-UCL.
DR GO; GO:0015749; P:monosaccharide transmembrane transport; IBA:GO_Central.
DR GO; GO:0031550; P:positive regulation of brain-derived neurotrophic factor receptor signaling pathway; IMP:ARUK-UCL.
DR GO; GO:0098694; P:regulation of synaptic vesicle budding from presynaptic endocytic zone membrane; IDA:SynGO.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0007614; P:short-term memory; IMP:ARUK-UCL.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR002441; Glc_transpt_4.
DR InterPro; IPR045263; GLUT.
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 PANTHER; PTHR23503; PTHR23503; 1.
DR Pfam; PF00083; Sugar_tr; 1.
DR PRINTS; PR01193; GLUCTRSPORT4.
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; Cytoplasm; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Reference proteome; Sugar transport; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation.
FT CHAIN 1..509
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 4"
FT /id="PRO_0000050366"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..81
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..111
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..142
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..201
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..287
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..323
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 345..353
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 375..384
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 406..417
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 439..445
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..466
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 467..509
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 7..13
FT /note="Interaction with SRFBP1"
FT /evidence="ECO:0000250|UniProtKB:P14672"
FT MOTIF 489..490
FT /note="Dileucine internalization motif"
FT /evidence="ECO:0000255"
FT BINDING 177
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 298..299
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 304
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 333
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 396
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 404
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 274
FT /note="Phosphoserine; by SGK1"
FT /evidence="ECO:0000250|UniProtKB:P14672"
FT MOD_RES 486
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14142"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT LIPID 223
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P14672"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 349
FT /note="R -> Q (in Ref. 1; AAA41451)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 509 AA; 54896 MW; DA50321E99E4CA90 CRC64;
MPSGFQQIGS EDGEPPQQRV TGTLVLAVFS AVLGSLQFGY NIGVINAPQK VIEQSYNATW
LGRQGPGGPD SIPQGTLTTL WALSVAIFSV GGMISSFLIG IISQWLGRKR AMLANNVLAV
LGGALMGLAN AAASYEILIL GRFLIGAYSG LTSGLVPMYV GEIAPTHLRG ALGTLNQLAI
VIGILVAQVL GLESMLGTAT LWPLLLAITV LPALLQLLLL PFCPESPRYL YIIRNLEGPA
RKSLKRLTGW ADVSDALAEL KDEKRKLERE RPLSLLQLLG SRTHRQPLII AVVLQLSQQL
SGINAVFYYS TSIFELAGVE QPAYATIGAG VVNTVFTLVS VLLVERAGRR TLHLLGLAGM
CGCAILMTVA LLLLERVPSM SYVSIVAIFG FVAFFEIGPG PIPWFIVAEL FSQGPRPAAM
AVAGFSNWTC NFIVGMGFQY VADAMGPYVF LLFAVLLLGF FIFTFLRVPE TRGRTFDQIS
ATFRRTPSLL EQEVKPSTEL EYLGPDEND
