PRRT2_MOUSE
ID PRRT2_MOUSE Reviewed; 346 AA.
AC E9PUL5;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Proline-rich transmembrane protein 2;
DE AltName: Full=Dispanin subfamily B member 3;
DE Short=DSPB3;
GN Name=Prrt2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; THR-74; THR-78; SER-98;
RP SER-102; SER-254 AND SER-255, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=22101681; DOI=10.1038/ng.1008;
RA Chen W.J., Lin Y., Xiong Z.Q., Wei W., Ni W., Tan G.H., Guo S.L., He J.,
RA Chen Y.F., Zhang Q.J., Li H.F., Lin Y., Murong S.X., Xu J., Wang N.,
RA Wu Z.Y.;
RT "Exome sequencing identifies truncating mutations in PRRT2 that cause
RT paroxysmal kinesigenic dyskinesia.";
RL Nat. Genet. 43:1252-1255(2011).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=22243967; DOI=10.1016/j.ajhg.2011.12.003;
RA Heron S.E., Grinton B.E., Kivity S., Afawi Z., Zuberi S.M., Hughes J.N.,
RA Pridmore C., Hodgson B.L., Iona X., Sadleir L.G., Pelekanos J.,
RA Herlenius E., Goldberg-Stern H., Bassan H., Haan E., Korczyn A.D.,
RA Gardner A.E., Corbett M.A., Gecz J., Thomas P.Q., Mulley J.C.,
RA Berkovic S.F., Scheffer I.E., Dibbens L.M.;
RT "PRRT2 mutations cause benign familial infantile epilepsy and infantile
RT convulsions with choreoathetosis syndrome.";
RL Am. J. Hum. Genet. 90:152-160(2012).
RN [5]
RP TISSUE SPECIFICITY, AND INTERACTION WITH SNAP25.
RX PubMed=22832103; DOI=10.1016/j.celrep.2011.11.001;
RA Lee H.Y., Huang Y., Bruneau N., Roll P., Roberson E.D., Hermann M.,
RA Quinn E., Maas J., Edwards R., Ashizawa T., Baykan B., Bhatia K.,
RA Bressman S., Bruno M.K., Brunt E.R., Caraballo R., Echenne B., Fejerman N.,
RA Frucht S., Gurnett C.A., Hirsch E., Houlden H., Jankovic J., Lee W.L.,
RA Lynch D.R., Mohammed S., Mueller U., Nespeca M.P., Renner D., Rochette J.,
RA Rudolf G., Saiki S., Soong B.W., Swoboda K.J., Tucker S., Wood N.,
RA Hanna M., Bowcock A.M., Szepetowski P., Fu Y.H., Ptacek L.J.;
RT "Mutations in the gene PRRT2 cause paroxysmal kinesigenic dyskinesia with
RT infantile convulsions.";
RL Cell Rep. 1:2-12(2012).
RN [6]
RP IDENTIFICATION IN AMPAR COMPLEX, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=22632720; DOI=10.1016/j.neuron.2012.03.034;
RA Schwenk J., Harmel N., Brechet A., Zolles G., Berkefeld H., Muller C.S.,
RA Bildl W., Baehrens D., Huber B., Kulik A., Klocker N., Schulte U.,
RA Fakler B.;
RT "High-resolution proteomics unravel architecture and molecular diversity of
RT native AMPA receptor complexes.";
RL Neuron 74:621-633(2012).
RN [7]
RP GENE FAMILY.
RX PubMed=22363774; DOI=10.1371/journal.pone.0031961;
RA Sallman Almen M., Bringeland N., Fredriksson R., Schioth H.B.;
RT "The dispanins: a novel gene family of ancient origin that contains 14
RT human members.";
RL PLoS ONE 7:E31961-E31961(2012).
RN [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-246, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [9]
RP INTERACTION WITH GRIA1, AND TISSUE SPECIFICITY.
RX PubMed=25915028; DOI=10.3390/ijms16059134;
RA Li M., Niu F., Zhu X., Wu X., Shen N., Peng X., Liu Y.;
RT "PRRT2 Mutant Leads to Dysfunction of Glutamate Signaling.";
RL Int. J. Mol. Sci. 16:9134-9151(2015).
RN [10]
RP FUNCTION, INTERACTION WITH SNAP25; SYT1 AND SYT2, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=27052163; DOI=10.1016/j.celrep.2016.03.005;
RA Valente P., Castroflorio E., Rossi P., Fadda M., Sterlini B.,
RA Cervigni R.I., Prestigio C., Giovedi S., Onofri F., Mura E.,
RA Guarnieri F.C., Marte A., Orlando M., Zara F., Fassio A., Valtorta F.,
RA Baldelli P., Corradi A., Benfenati F.;
RT "PRRT2 Is a Key Component of the Ca(2+)-Dependent Neurotransmitter Release
RT Machinery.";
RL Cell Rep. 15:117-131(2016).
RN [11]
RP INTERACTION WITH ITSN1, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=26797119; DOI=10.1074/jbc.m115.683888;
RA Rossi P., Sterlini B., Castroflorio E., Marte A., Onofri F., Valtorta F.,
RA Maragliano L., Corradi A., Benfenati F.;
RT "A Novel Topology of Proline-rich Transmembrane Protein 2 (PRRT2): hints
RT for an intracellular function at the synapse.";
RL J. Biol. Chem. 291:6111-6123(2016).
RN [12]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=27172900; DOI=10.18632/oncotarget.9258;
RA Liu Y.T., Nian F.S., Chou W.J., Tai C.Y., Kwan S.Y., Chen C., Kuo P.W.,
RA Lin P.H., Chen C.Y., Huang C.W., Lee Y.C., Soong B.W., Tsai J.W.;
RT "PRRT2 mutations lead to neuronal dysfunction and neurodevelopmental
RT defects.";
RL Oncotarget 7:39184-39196(2016).
RN [13]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=28007585; DOI=10.1016/j.nbd.2016.12.018;
RA Michetti C., Castroflorio E., Marchionni I., Forte N., Sterlini B.,
RA Binda F., Fruscione F., Baldelli P., Valtorta F., Zara F., Corradi A.,
RA Benfenati F.;
RT "The PRRT2 knockout mouse recapitulates the neurological diseases
RT associated with PRRT2 mutations.";
RL Neurobiol. Dis. 99:66-83(2017).
RN [14]
RP FUNCTION, INTERACTION WITH SNAP25 AND STX1A, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=29056747; DOI=10.1038/cr.2017.128;
RA Tan G.H., Liu Y.Y., Wang L., Li K., Zhang Z.Q., Li H.F., Yang Z.F., Li Y.,
RA Li D., Wu M.Y., Yu C.L., Long J.J., Chen R.C., Li L.X., Yin L.P., Liu J.W.,
RA Cheng X.W., Shen Q., Shu Y.S., Sakimura K., Liao L.J., Wu Z.Y., Xiong Z.Q.;
RT "PRRT2 deficiency induces paroxysmal kinesigenic dyskinesia by regulating
RT synaptic transmission in cerebellum.";
RL Cell Res. 28:90-110(2018).
CC -!- FUNCTION: As a component of the outer core of AMPAR complex, may be
CC involved in synaptic transmission in the central nervous system. In
CC hippocampal neurons, in presynaptic terminals, plays an important role
CC in the final steps of neurotransmitter release, possibly by regulating
CC Ca(2+)-sensing (PubMed:27052163). In the cerebellum, may inhibit SNARE
CC complex formation and down-regulate short-term facilitation
CC (PubMed:29056747). {ECO:0000269|PubMed:27052163,
CC ECO:0000269|PubMed:29056747}.
CC -!- SUBUNIT: Component of the outer core of AMPAR complex (PubMed:22632720,
CC PubMed:25915028). AMPAR complex consists of an inner core made of 4
CC pore-forming GluA/GRIA proteins (GRIA1, GRIA2, GRIA3 and GRIA4) and 4
CC major auxiliary subunits arranged in a twofold symmetry. One of the two
CC pairs of distinct binding sites is occupied either by CNIH2, CNIH3 or
CC CACNG2, CACNG3. The other harbors CACNG2, CACNG3, CACNG4, CACNG8 or
CC GSG1L. This inner core of AMPAR complex is complemented by outer core
CC constituents binding directly to the GluA/GRIA proteins at sites
CC distinct from the interaction sites of the inner core constituents.
CC Outer core constituents include at least PRRT1, PRRT2, CKAMP44/SHISA9,
CC FRRS1L and NRN1. The proteins of the inner and outer core serve as a
CC platform for other, more peripherally associated AMPAR constituents.
CC Alone or in combination, these auxiliary subunits control the gating
CC and pharmacology of the AMPAR complex and profoundly impact their
CC biogenesis and protein processing (PubMed:22632720). Interacts with
CC intersectin 1/ITSN1 (PubMed:26797119). Interacts with SNARE complex
CC components, including SNAP25, STX1A, SYT1 and SYT2; this interaction
CC may inhibit SNARE complex formation (PubMed:22832103, PubMed:27052163,
CC PubMed:29056747). {ECO:0000269|PubMed:22632720,
CC ECO:0000269|PubMed:22832103, ECO:0000269|PubMed:25915028,
CC ECO:0000269|PubMed:26797119, ECO:0000269|PubMed:27052163,
CC ECO:0000269|PubMed:29056747}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26797119,
CC ECO:0000269|PubMed:27172900}; Single-pass membrane protein
CC {ECO:0000305|PubMed:26797119}. Presynaptic cell membrane
CC {ECO:0000269|PubMed:27052163, ECO:0000269|PubMed:29056747}; Single-pass
CC membrane protein {ECO:0000305|PubMed:26797119}. Synapse
CC {ECO:0000269|PubMed:27052163, ECO:0000269|PubMed:29056747,
CC ECO:0000305|PubMed:22632720}. Cell projection, axon
CC {ECO:0000269|PubMed:29056747}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle membrane {ECO:0000250|UniProtKB:D3ZFB6}. Postsynaptic
CC density membrane {ECO:0000250|UniProtKB:D3ZFB6}. Cell projection,
CC dendritic spine {ECO:0000250|UniProtKB:D3ZFB6}.
CC -!- TISSUE SPECIFICITY: Neuron-specific expression throughout the brain,
CC with the highest levels in the cerebellum, basal ganglia, hippocampus,
CC substantia nigra, and neocortex (at protein level) (PubMed:22101681,
CC PubMed:22243967, PubMed:22832103, PubMed:22632720, PubMed:25915028,
CC PubMed:27052163, PubMed:27172900, PubMed:28007585, PubMed:29056747).
CC Highly expressed also in spinal cord (at protein level)
CC (PubMed:22101681, PubMed:22832103). Detected at very low levels in the
CC heart, lung, kidney and skin (PubMed:22101681).
CC {ECO:0000269|PubMed:22101681, ECO:0000269|PubMed:22243967,
CC ECO:0000269|PubMed:22632720, ECO:0000269|PubMed:22832103,
CC ECO:0000269|PubMed:25915028, ECO:0000269|PubMed:27052163,
CC ECO:0000269|PubMed:27172900, ECO:0000269|PubMed:28007585,
CC ECO:0000269|PubMed:29056747}.
CC -!- DEVELOPMENTAL STAGE: At the mRNA level, expressed at low levels in the
CC developing brain before 16 dpc. Expression markedly increases during
CC early postnatal stages with a peak at P14. At this stage, expressed
CC throughout the brain, with high levels in the cerebral cortex (cortical
CC layers), hippocampus and cerebellum (granule cells and Purkinje cell
CC layers). Progressively declines to relatively low levels in adulthood.
CC At the protein level, first detected at very low levels at 17.5 dpc.
CC Expression increases at early postnatal stages in the cerebral cortex,
CC hippocampus and cerebellum. Expression increases to reach a plateau
CC around P14, a period of intense synapse formation and rearrangement,
CC and starts to slightly decrease around P90 (at protein level)
CC (PubMed:27052163, PubMed:29056747). {ECO:0000269|PubMed:22101681,
CC ECO:0000269|PubMed:27052163, ECO:0000269|PubMed:29056747}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice are normal at birth, but display
CC paroxysmal movements at the onset of locomotion that persist in the
CC adulthood. Adult animals present abnormal motor behaviors characterized
CC by wild running and jumping in response to audiogenic stimuli that are
CC ineffective in wild-type mice and an increased sensitivity to the
CC convulsive effects of pentylentetrazol. Although the overall brain
CC structure is not affected by the knockout, the thickness of the
CC neocortex in young adult is significantly reduced in medial and caudal
CC regions compared to their wild-type littermates. No significant
CC differences are observed in the thickness of the CA1, CA3 and DG
CC regions of the hippocampus, as well as for the molecular and granule
CC layers of the cerebellum (PubMed:28007585). Mice with a conditional
CC knockout in the central nervous system develop normally, but showed
CC poor performance in motor coordination functions (PubMed:29056747).
CC {ECO:0000269|PubMed:28007585, ECO:0000269|PubMed:29056747}.
CC -!- SIMILARITY: Belongs to the CD225/Dispanin family. {ECO:0000305}.
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DR EMBL; AC122863; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS52405.1; -.
DR RefSeq; NP_001096033.1; NM_001102563.1.
DR AlphaFoldDB; E9PUL5; -.
DR BioGRID; 213173; 2.
DR IntAct; E9PUL5; 1.
DR MINT; E9PUL5; -.
DR STRING; 10090.ENSMUSP00000124520; -.
DR iPTMnet; E9PUL5; -.
DR PhosphoSitePlus; E9PUL5; -.
DR SwissPalm; E9PUL5; -.
DR MaxQB; E9PUL5; -.
DR PaxDb; E9PUL5; -.
DR PeptideAtlas; E9PUL5; -.
DR PRIDE; E9PUL5; -.
DR ProteomicsDB; 291802; -.
DR Ensembl; ENSMUST00000159916; ENSMUSP00000124520; ENSMUSG00000045114.
DR GeneID; 69017; -.
DR KEGG; mmu:69017; -.
DR UCSC; uc009jty.1; mouse.
DR CTD; 112476; -.
DR MGI; MGI:1916267; Prrt2.
DR VEuPathDB; HostDB:ENSMUSG00000045114; -.
DR eggNOG; ENOG502S2U1; Eukaryota.
DR GeneTree; ENSGT00940000161103; -.
DR HOGENOM; CLU_070349_0_0_1; -.
DR InParanoid; E9PUL5; -.
DR OMA; DPQPDCQ; -.
DR OrthoDB; 1101977at2759; -.
DR PhylomeDB; E9PUL5; -.
DR TreeFam; TF331357; -.
DR BioGRID-ORCS; 69017; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Prrt2; mouse.
DR PRO; PR:E9PUL5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; E9PUL5; protein.
DR Bgee; ENSMUSG00000045114; Expressed in cerebellar cortex and 56 other tissues.
DR ExpressionAtlas; E9PUL5; baseline and differential.
DR Genevisible; E9PUL5; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0043679; C:axon terminus; IDA:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0098839; C:postsynaptic density membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; IDA:UniProtKB.
DR GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; IDA:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0017075; F:syntaxin-1 binding; IDA:UniProtKB.
DR GO; GO:0099502; P:calcium-dependent activation of synaptic vesicle fusion; IDA:SynGO.
DR GO; GO:1905513; P:negative regulation of short-term synaptic potentiation; IMP:UniProtKB.
DR GO; GO:0035544; P:negative regulation of SNARE complex assembly; IMP:UniProtKB.
DR GO; GO:0050884; P:neuromuscular process controlling posture; ISO:MGI.
DR GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IMP:UniProtKB.
DR InterPro; IPR007593; CD225/Dispanin_fam.
DR Pfam; PF04505; CD225; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Cytoplasmic vesicle; Membrane; Methylation;
KW Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Synapse;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..346
FT /note="Proline-rich transmembrane protein 2"
FT /id="PRO_0000415735"
FT TOPO_DOM 1..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26797119"
FT INTRAMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26797119"
FT TOPO_DOM 296..323
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26797119"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26797119"
FT TOPO_DOM 345..346
FT /note="Extracellular"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26797119"
FT REGION 1..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..167
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..217
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 74
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 78
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZFB6"
FT MOD_RES 246
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 346 AA; 35924 MW; E7C3AF4159F4995F CRC64;
MAASSSQVSE MKGVEDSSKT QTEGPRHSEE GLGPVQVVAE IPDQPEALQP GPGITAAPVD
SGPKAELAPE TTETPVETPE TVQATDLSLN PEEGSKASPS PSPSEARQEP ASKPDVNRET
AAEEGSEPQS TAPPEPTSEP AFQINTQSDP QPTSQPPPKP PLQAEPPTQE DPTTEVLTES
TGEKQENGAV VPLQAGDGEE GPAPQPHSPP STKTPPANGA PPRVLQKLVE EDRIGRAHGG
HPGSPRGSLS RHPSSQLAGP GVEGGEGTQK PRDYIILAIL SCFCPMWPVN IVAFAYAVMS
RNSLQQGDVD GAQRLGRVAK LLSIVALVGG VLIIIASCVI NLGVYK
