VGLU2_RAT
ID VGLU2_RAT Reviewed; 582 AA.
AC Q9JI12;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Vesicular glutamate transporter 2 {ECO:0000250|UniProtKB:Q9P2U8};
DE Short=VGluT2 {ECO:0000303|PubMed:11698620};
DE AltName: Full=Differentiation-associated BNPI {ECO:0000250|UniProtKB:Q9P2U8};
DE AltName: Full=Differentiation-associated Na(+)-dependent inorganic phosphate cotransporter {ECO:0000303|PubMed:11551935};
DE AltName: Full=Solute carrier family 17 member 6;
GN Name=Slc17a6 {ECO:0000312|RGD:620531};
GN Synonyms=Dnpi {ECO:0000303|PubMed:11551935}, Vglut2;
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].
RA Mashima H., Kojima I.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11551935; DOI=10.1074/jbc.m106244200;
RA Hayashi M., Otsuka M., Morimoto R., Hirota S., Yatsushiro S., Takeda J.,
RA Yamamoto A., Moriyama Y.;
RT "Differentiation-associated Na+-dependent inorganic phosphate cotransporter
RT (DNPI) is a vesicular glutamate transporter in endocrine glutamatergic
RT systems.";
RL J. Biol. Chem. 276:43400-43406(2001).
RN [3]
RP FUNCTION, TRANSPORTER ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11698619; DOI=10.1523/jneurosci.21-22-j0001.2001;
RA Herzog E., Bellenchi G.C., Gras C., Bernard V., Ravassard P., Bedet C.,
RA Gasnier B., Giros B., El Mestikawy S.;
RT "The existence of a second vesicular glutamate transporter specifies
RT subpopulations of glutamatergic neurons.";
RL J. Neurosci. 21:RC181-RC181(2001).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11698620; DOI=10.1523/jneurosci.21-22-j0002.2001;
RA Takamori S., Rhee J.S., Rosenmund C., Jahn R.;
RT "Identification of differentiation-associated brain-specific phosphate
RT transporter as a second vesicular glutamate transporter (VGLUT2).";
RL J. Neurosci. 21:RC182-RC182(2001).
RN [5]
RP FUNCTION, TRANSPORTER ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11502256; DOI=10.1016/s0896-6273(01)00344-0;
RA Fremeau R.T. Jr., Troyer M.D., Pahner I., Nygaard G.O., Tran C.H.,
RA Reimer R.J., Bellocchio E.E., Fortin D., Storm-Mathisen J., Edwards R.H.;
RT "The expression of vesicular glutamate transporters defines two classes of
RT excitatory synapse.";
RL Neuron 31:247-260(2001).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17110340; DOI=10.1016/j.cell.2006.10.030;
RA Takamori S., Holt M., Stenius K., Lemke E.A., Groenborg M., Riedel D.,
RA Urlaub H., Schenck S., Bruegger B., Ringler P., Mueller S.A., Rammner B.,
RA Graeter F., Hub J.S., De Groot B.L., Mieskes G., Moriyama Y., Klingauf J.,
RA Grubmueller H., Heuser J., Wieland F., Jahn R.;
RT "Molecular anatomy of a trafficking organelle.";
RL Cell 127:831-846(2006).
RN [7]
RP FUNCTION, TRANSPORTER ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF HIS-128; ARG-184 AND GLU-191.
RX PubMed=17046815; DOI=10.1074/jbc.m607670200;
RA Juge N., Yoshida Y., Yatsushiro S., Omote H., Moriyama Y.;
RT "Vesicular glutamate transporter contains two independent transport
RT machineries.";
RL J. Biol. Chem. 281:39499-39506(2006).
RN [8]
RP FUNCTION, TRANSPORTER ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=18080752; DOI=10.1007/s11064-007-9546-z;
RA Mackenzie B., Illing A.C., Morris M.E.K., Varoqui H., Erickson J.D.;
RT "Analysis of a vesicular glutamate transporter (VGLUT2) supports a cell-
RT leakage mode in addition to vesicular packaging.";
RL Neurochem. Res. 33:238-247(2008).
RN [9]
RP FUNCTION, AND TRANSPORTER ACTIVITY.
RX PubMed=25433636; DOI=10.1016/j.neuron.2014.11.008;
RA Preobraschenski J., Zander J.F., Suzuki T., Ahnert-Hilger G., Jahn R.;
RT "Vesicular glutamate transporters use flexible anion and cation binding
RT sites for efficient accumulation of neurotransmitter.";
RL Neuron 84:1287-1301(2014).
RN [10]
RP FUNCTION, TRANSPORTER ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=27133463; DOI=10.1016/j.neuron.2016.03.026;
RA Eriksen J., Chang R., McGregor M., Silm K., Suzuki T., Edwards R.H.;
RT "Protons Regulate Vesicular Glutamate Transporters through an Allosteric
RT Mechanism.";
RL Neuron 90:768-780(2016).
RN [11]
RP FUNCTION, AND TRANSPORTER ACTIVITY.
RX PubMed=29642010; DOI=10.1016/j.celrep.2018.03.055;
RA Preobraschenski J., Cheret C., Ganzella M., Zander J.F., Richter K.,
RA Schenck S., Jahn R., Ahnert-Hilger G.;
RT "Dual and Direction-Selective Mechanisms of Phosphate Transport by the
RT Vesicular Glutamate Transporter.";
RL Cell Rep. 23:535-545(2018).
RN [12] {ECO:0007744|PDB:6V4D}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF 39-547, FUNCTION,
RP TRANSPORTER ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF ARG-88 AND
RP ARG-322.
RX PubMed=32439795; DOI=10.1126/science.aba9202;
RA Li F., Eriksen J., Finer-Moore J., Chang R., Nguyen P., Bowen A.,
RA Myasnikov A., Yu Z., Bulkley D., Cheng Y., Edwards R.H., Stroud R.M.;
RT "Ion transport and regulation in a synaptic vesicle glutamate
RT transporter.";
RL Science 368:893-897(2020).
CC -!- FUNCTION: Multifunctional transporter that transports L-glutamate as
CC well as multiple ions such as chloride, proton, potassium, sodium and
CC phosphate (PubMed:18080752, PubMed:11551935, PubMed:11698619,
CC PubMed:11502256, PubMed:29642010, PubMed:17046815, PubMed:32439795,
CC PubMed:27133463, PubMed:25433636). At the synaptic vesicle membrane,
CC mainly functions as a uniporter which transports preferentially L-
CC glutamate but also, phosphate from the cytoplasm into synaptic vesicles
CC at presynaptic nerve terminals of excitatory neural cells
CC (PubMed:18080752, PubMed:11698619, PubMed:11551935, PubMed:11502256,
CC PubMed:29642010, PubMed:17046815, PubMed:32439795, PubMed:27133463).
CC The L-glutamate or phosphate uniporter activity is electrogenic and is
CC driven by the proton electrochemical gradient, mainly by the electrical
CC gradient established by the vacuolar H(+)-ATPase across the synaptic
CC vesicle membrane (PubMed:11551935, PubMed:11698619, PubMed:11502256,
CC PubMed:17046815, PubMed:32439795, PubMed:29642010). In addition,
CC functions as a chloride channel that allows a chloride permeation
CC through the synaptic vesicle membrane therefore affects the proton
CC electrochemical gradient and promotes synaptic vesicles acidification
CC (PubMed:27133463). Moreover, functions as a vesicular K(+)/H(+)
CC antiport allowing to maintain the electrical gradient and to decrease
CC chemical gradient and therefore sustain vesicular L-glutamate uptake
CC (PubMed:25433636). The vesicular H(+)/H(+) antiport activity is
CC electroneutral (PubMed:25433636). At the plasma membrane, following
CC exocytosis, functions as a symporter of Na(+) and phosphate from the
CC extracellular space to the cytoplasm allowing synaptic phosphate
CC homeostasis regulation (PubMed:17046815, PubMed:29642010). The
CC symporter activity is driven by an inside negative membrane potential
CC and is electrogenic (PubMed:29642010, PubMed:17046815). Also involved
CC in the regulation of retinal hyaloid vessel regression during postnatal
CC development (By similarity). May also play a role in the endocrine L-
CC glutamatergic system of other tissues such as pineal gland and pancreas
CC (PubMed:11551935). {ECO:0000250|UniProtKB:Q8BLE7,
CC ECO:0000269|PubMed:11502256, ECO:0000269|PubMed:11551935,
CC ECO:0000269|PubMed:11698619, ECO:0000269|PubMed:17046815,
CC ECO:0000269|PubMed:25433636, ECO:0000269|PubMed:27133463,
CC ECO:0000269|PubMed:29642010, ECO:0000269|PubMed:32439795}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamate(out) = L-glutamate(in); Xref=Rhea:RHEA:66336,
CC ChEBI:CHEBI:29985; Evidence={ECO:0000269|PubMed:11502256,
CC ECO:0000269|PubMed:11551935, ECO:0000269|PubMed:11698619,
CC ECO:0000269|PubMed:17046815, ECO:0000269|PubMed:27133463,
CC ECO:0000269|PubMed:29642010, ECO:0000269|PubMed:32439795,
CC ECO:0000305|PubMed:18080752};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 Na(+)(out) + phosphate(out) = 3 Na(+)(in) + phosphate(in);
CC Xref=Rhea:RHEA:71255, ChEBI:CHEBI:29101, ChEBI:CHEBI:43474;
CC Evidence={ECO:0000269|PubMed:17046815, ECO:0000269|PubMed:29642010};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate(in) = phosphate(out); Xref=Rhea:RHEA:32823,
CC ChEBI:CHEBI:43474; Evidence={ECO:0000269|PubMed:29642010};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + K(+)(in) = H(+)(in) + K(+)(out);
CC Xref=Rhea:RHEA:29467, ChEBI:CHEBI:15378, ChEBI:CHEBI:29103;
CC Evidence={ECO:0000269|PubMed:25433636};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823,
CC ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:27133463};
CC -!- ACTIVITY REGULATION: Chloride channel activity is allosterically
CC activated by lumenal H(+) and Cl(-) leading to synaptic vesicles
CC acidification (PubMed:27133463). The L-glutamate transport activity is
CC allosterically activated by lumenal H(+) and Cl(-) (PubMed:27133463,
CC PubMed:32439795). The allosteric requirement for H(+) efficiently
CC prevents non-vesicular efflux across the plasma membrane
CC (PubMed:27133463). The L-glutamate uniporter activity exhibits a
CC biphasic dependence on chloride concentration (PubMed:11502256,
CC PubMed:17046815). {ECO:0000269|PubMed:11502256,
CC ECO:0000269|PubMed:17046815, ECO:0000269|PubMed:27133463,
CC ECO:0000269|PubMed:32439795}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.9 mM for L-glutamate {ECO:0000269|PubMed:11698619};
CC KM=4.7 mM for L-glutamate {ECO:0000269|PubMed:11502256};
CC KM=4.8 mM for L-glutamate {ECO:0000269|PubMed:17046815};
CC KM=10.1 mM for phosphate (when a Na(+) gradient is imposed in
CC proteoliposomes) {ECO:0000269|PubMed:17046815};
CC Vmax=470 pmol/min/mg enzyme toward L-glutamate
CC {ECO:0000269|PubMed:11698619};
CC Vmax=120 nmol/min/mg enzyme toward L-glutamate
CC {ECO:0000269|PubMed:17046815};
CC Vmax=127 nmol/min/mg enzyme toward phosphate (when a Na(+) gradient
CC is imposed in proteoliposomes) {ECO:0000269|PubMed:17046815};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000269|PubMed:11502256,
CC ECO:0000269|PubMed:11551935, ECO:0000269|PubMed:11698619,
CC ECO:0000269|PubMed:11698620}; Multi-pass membrane protein
CC {ECO:0000255}. Synapse, synaptosome {ECO:0000269|PubMed:11502256,
CC ECO:0000269|PubMed:11698619}. Cell membrane
CC {ECO:0000269|PubMed:18080752}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level). Expressed in
CC brainstem, deep nuclei, septal nuclei, nuclei of the diagonal band,
CC frontal cortex, hypothalamus, midbrain, parietal cortex and temporal
CC cortex. Also expressed in pineal gland and islets of Langerhans.
CC {ECO:0000269|PubMed:11502256, ECO:0000269|PubMed:11551935,
CC ECO:0000269|PubMed:11698619, ECO:0000269|PubMed:11698620}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sodium/anion
CC cotransporter family. VGLUT subfamily. {ECO:0000305}.
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DR EMBL; AF271235; AAF76223.1; -; mRNA.
DR RefSeq; NP_445879.1; NM_053427.1.
DR PDB; 6V4D; EM; 3.80 A; A=39-547.
DR PDBsum; 6V4D; -.
DR AlphaFoldDB; Q9JI12; -.
DR SMR; Q9JI12; -.
DR BioGRID; 249986; 2.
DR IntAct; Q9JI12; 1.
DR MINT; Q9JI12; -.
DR STRING; 10116.ENSRNOP00000022383; -.
DR TCDB; 2.A.1.14.16; the major facilitator superfamily (mfs).
DR GlyGen; Q9JI12; 3 sites.
DR PhosphoSitePlus; Q9JI12; -.
DR PaxDb; Q9JI12; -.
DR PRIDE; Q9JI12; -.
DR ABCD; Q9JI12; 1 sequenced antibody.
DR GeneID; 84487; -.
DR KEGG; rno:84487; -.
DR UCSC; RGD:620531; rat.
DR CTD; 57084; -.
DR RGD; 620531; Slc17a6.
DR eggNOG; KOG2532; Eukaryota.
DR InParanoid; Q9JI12; -.
DR PhylomeDB; Q9JI12; -.
DR Reactome; R-RNO-428643; Organic anion transporters.
DR PRO; PR:Q9JI12; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005769; C:early endosome; IDA:RGD.
DR GO; GO:0060076; C:excitatory synapse; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:1990030; C:pericellular basket; IDA:RGD.
DR GO; GO:0098793; C:presynapse; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:UniProtKB.
DR GO; GO:0005254; F:chloride channel activity; IDA:UniProtKB.
DR GO; GO:0005313; F:L-glutamate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0022810; F:membrane potential driven uniporter activity; IDA:UniProtKB.
DR GO; GO:0005326; F:neurotransmitter transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015386; F:potassium:proton antiporter activity; IDA:UniProtKB.
DR GO; GO:0005436; F:sodium:phosphate symporter activity; IDA:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006820; P:anion transport; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0021766; P:hippocampus development; IEP:RGD.
DR GO; GO:1990384; P:hyaloid vascular plexus regression; ISS:UniProtKB.
DR GO; GO:0051938; P:L-glutamate import; ISS:UniProtKB.
DR GO; GO:0015813; P:L-glutamate transmembrane transport; IDA:UniProtKB.
DR GO; GO:0003407; P:neural retina development; IEP:RGD.
DR GO; GO:0098700; P:neurotransmitter loading into synaptic vesicle; IDA:SynGO.
DR GO; GO:0001504; P:neurotransmitter uptake; ISO:RGD.
DR GO; GO:0055062; P:phosphate ion homeostasis; ISS:UniProtKB.
DR GO; GO:0050803; P:regulation of synapse structure or activity; IBA:GO_Central.
DR GO; GO:0044341; P:sodium-dependent phosphate transport; IDA:UniProtKB.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiport; Cell membrane; Chloride; Chloride channel;
KW Cytoplasmic vesicle; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Neurotransmitter transport; Phosphate transport; Reference proteome;
KW Sodium; Sodium transport; Symport; Synapse; Synaptosome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..582
FT /note="Vesicular glutamate transporter 2"
FT /id="PRO_0000318171"
FT TOPO_DOM 1..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..125
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..177
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..244
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..310
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..349
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..386
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 408..409
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..443
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..464
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 465..477
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 478..498
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 499..582
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 88
FT /note="R->A: Impairs synaptic transmission. Abolishes the
FT chloride ion conductance."
FT /evidence="ECO:0000269|PubMed:32439795"
FT MUTAGEN 128
FT /note="H->A: Greatly lowers L-glutamate transport."
FT /evidence="ECO:0000269|PubMed:17046815"
FT MUTAGEN 184
FT /note="R->A,E,K: Greatly lowers L-glutamate transport."
FT /evidence="ECO:0000269|PubMed:17046815"
FT MUTAGEN 191
FT /note="E->A: Greatly lowers L-glutamate transport."
FT /evidence="ECO:0000269|PubMed:17046815"
FT MUTAGEN 191
FT /note="E->D,Q: Lowers L-glutamate transport."
FT /evidence="ECO:0000269|PubMed:17046815"
FT MUTAGEN 322
FT /note="R->A: Loss of L-glutamate release. Abolishes the
FT chloride ion conductance."
FT /evidence="ECO:0000269|PubMed:32439795"
SQ SEQUENCE 582 AA; 64576 MW; 99A14F62E685B9E9 CRC64;
MESVKQRILA PGKEGIKNFA GKSLGQIYRV LEKKQDNRET IELTEDGKPL EVPEKKAPLC
DCTCFGLPRR YIIAIMSGLG FCISFGIRCN LGVAIVDMVN NSTIHRGGKV IKEKAKFNWD
PETVGMIHGS FFWGYIITQI PGGYIASRLA ANRVFGAAIL LTSTLNMLIP SAARVHYGCV
IFVRILQGLV EGVTYPACHG IWSKWAPPLE RSRLATTSFC GSYAGAVIAM PLAGILVQYT
GWSSVFYVYG SFGMVWYMFW LLVSYESPAK HPTITDEERR YIEESIGESA NLLGAMEKFK
TPWRKFFTSM PVYAIIVANF CRSWTFYLLL ISQPAYFEEV FGFEISKVGM LSAVPHLVMT
IIVPIGGQIA DFLRSKQILS TTTVRKIMNC GGFGMEATLL LVVGYSHTRG VAISFLVLAV
GFSGFAISGF NVNHLDIAPR YASILMGISN GVGTLSGMVC PIIVGAMTKN KSREEWQYVF
LIAALVHYGG VIFYALFASG EKQPWADPEE TSEEKCGFIH EDELDEETGD ITQNYINYGT
TKSYGATSQE NGGWPNGWEK KEEFVQESAQ DAYSYKDRDD YS
