GRM1_MOUSE
ID GRM1_MOUSE Reviewed; 1199 AA.
AC P97772; Q6AXG4; Q9EPV6;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 11-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Metabotropic glutamate receptor 1;
DE Short=mGluR1;
DE Flags: Precursor;
GN Name=Grm1; Synonyms=Gprc1a, Mglur1;
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 [MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=10581402; DOI=10.1016/s0169-328x(99)00239-9;
RA Zhu H., Ryan K., Chen S.;
RT "Cloning of novel splice variants of mouse mGluR1.";
RL Brain Res. Mol. Brain Res. 73:93-103(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 945-1127 (ISOFORM 1).
RC STRAIN=C57BL/6J;
RA Watanabe M.;
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=17296554; DOI=10.1016/j.neuron.2007.01.019;
RA Ihara M., Yamasaki N., Hagiwara A., Tanigaki A., Kitano A., Hikawa R.,
RA Tomimoto H., Noda M., Takanashi M., Mori H., Hattori N., Miyakawa T.,
RA Kinoshita M.;
RT "Sept4, a component of presynaptic scaffold and Lewy bodies, is required
RT for the suppression of alpha-synuclein neurotoxicity.";
RL Neuron 53:519-533(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-853; THR-871; SER-969;
RP SER-1097; SER-1147 AND SER-1154, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [7]
RP FUNCTION, AND MUTAGENESIS OF ILE-536.
RX PubMed=26427409; DOI=10.1007/978-3-319-17121-0_24;
RA Charette J.R., Samuels I.S., Yu M., Stone L., Hicks W., Shi L.Y.,
RA Krebs M.P., Naggert J.K., Nishina P.M., Peachey N.S.;
RT "A Chemical Mutagenesis Screen Identifies Mouse Models with ERG Defects.";
RL Adv. Exp. Med. Biol. 854:177-183(2016).
CC -!- FUNCTION: G-protein coupled receptor for glutamate. Ligand binding
CC causes a conformation change that triggers signaling via guanine
CC nucleotide-binding proteins (G proteins) and modulates the activity of
CC down-stream effectors. Signaling activates a phosphatidylinositol-
CC calcium second messenger system. May participate in the central action
CC of glutamate in the CNS, such as long-term potentiation in the
CC hippocampus and long-term depression in the cerebellum (By.
CC similarity). May function in the light response in the retina
CC (PubMed:26427409). {ECO:0000269|PubMed:26427409}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). The PPXXF motif
CC binds HOMER1, HOMER2 and HOMER3. Interacts with TAMALIN (By
CC similarity). Interacts with RYR1, RYR2, ITPR1, SHANK1 and SHANK3.
CC Interacts with SHIA1 (By similarity). {ECO:0000250|UniProtKB:P23385}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q13255};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q13255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=A;
CC IsoId=P97772-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=P97772-2; Sequence=VSP_007186, VSP_007187;
CC Name=3; Synonyms=E55;
CC IsoId=P97772-3; Sequence=VSP_007184, VSP_007185;
CC -!- TISSUE SPECIFICITY: Expressed in the striatum (at protein level).
CC {ECO:0000269|PubMed:17296554}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC {ECO:0000305}.
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DR EMBL; AF320126; AAG41991.2; -; mRNA.
DR EMBL; BC067057; AAH67057.1; -; mRNA.
DR EMBL; BC079566; AAH79566.1; -; mRNA.
DR EMBL; U89891; AAB48099.1; -; mRNA.
DR CCDS; CCDS23696.1; -. [P97772-1]
DR CCDS; CCDS48499.1; -. [P97772-2]
DR RefSeq; NP_001107805.1; NM_001114333.2. [P97772-2]
DR RefSeq; NP_058672.1; NM_016976.3. [P97772-1]
DR RefSeq; XP_006512612.1; XM_006512549.3. [P97772-1]
DR AlphaFoldDB; P97772; -.
DR SMR; P97772; -.
DR BioGRID; 200073; 11.
DR CORUM; P97772; -.
DR IntAct; P97772; 7.
DR MINT; P97772; -.
DR STRING; 10090.ENSMUSP00000037255; -.
DR BindingDB; P97772; -.
DR ChEMBL; CHEMBL2892; -.
DR GlyGen; P97772; 5 sites.
DR iPTMnet; P97772; -.
DR PhosphoSitePlus; P97772; -.
DR SwissPalm; P97772; -.
DR jPOST; P97772; -.
DR MaxQB; P97772; -.
DR PaxDb; P97772; -.
DR PeptideAtlas; P97772; -.
DR PRIDE; P97772; -.
DR ProteomicsDB; 269836; -. [P97772-1]
DR ProteomicsDB; 269837; -. [P97772-2]
DR ProteomicsDB; 269838; -. [P97772-3]
DR Antibodypedia; 2943; 712 antibodies from 43 providers.
DR DNASU; 14816; -.
DR Ensembl; ENSMUST00000044306; ENSMUSP00000037255; ENSMUSG00000019828. [P97772-1]
DR Ensembl; ENSMUST00000105560; ENSMUSP00000101189; ENSMUSG00000019828. [P97772-2]
DR Ensembl; ENSMUST00000105561; ENSMUSP00000101190; ENSMUSG00000019828. [P97772-2]
DR GeneID; 14816; -.
DR KEGG; mmu:14816; -.
DR UCSC; uc007ejh.2; mouse. [P97772-2]
DR UCSC; uc007eji.2; mouse. [P97772-1]
DR CTD; 2911; -.
DR MGI; MGI:1351338; Grm1.
DR VEuPathDB; HostDB:ENSMUSG00000019828; -.
DR eggNOG; KOG1056; Eukaryota.
DR GeneTree; ENSGT01030000234595; -.
DR HOGENOM; CLU_005389_0_1_1; -.
DR InParanoid; P97772; -.
DR OMA; CWYAPVA; -.
DR PhylomeDB; P97772; -.
DR TreeFam; TF313240; -.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-420499; Class C/3 (Metabotropic glutamate/pheromone receptors).
DR Reactome; R-MMU-6794361; Neurexins and neuroligins.
DR BioGRID-ORCS; 14816; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Grm1; mouse.
DR PRO; PR:P97772; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P97772; protein.
DR Bgee; ENSMUSG00000019828; Expressed in medial dorsal nucleus of thalamus and 82 other tissues.
DR Genevisible; P97772; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0038037; C:G protein-coupled receptor dimeric complex; ISO:MGI.
DR GO; GO:0038038; C:G protein-coupled receptor homodimeric complex; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; ISO:MGI.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:BHF-UCL.
DR GO; GO:0043025; C:neuronal cell body; TAS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0098839; C:postsynaptic density membrane; ISO:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; TAS:UniProtKB.
DR GO; GO:0042734; C:presynaptic membrane; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0001640; F:adenylate cyclase inhibiting G protein-coupled glutamate receptor activity; IBA:GO_Central.
DR GO; GO:0098872; F:G protein-coupled neurotransmitter receptor activity involved in regulation of postsynaptic cytosolic calcium ion concentration; IDA:SynGO.
DR GO; GO:0099530; F:G protein-coupled receptor activity involved in regulation of postsynaptic membrane potential; ISO:MGI.
DR GO; GO:0008066; F:glutamate receptor activity; ISS:UniProtKB.
DR GO; GO:0099583; F:neurotransmitter receptor activity involved in regulation of postsynaptic cytosolic calcium ion concentration; IMP:SynGO.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:MGI.
DR GO; GO:0001639; F:PLC activating G protein-coupled glutamate receptor activity; TAS:MGI.
DR GO; GO:0019722; P:calcium-mediated signaling; ISO:MGI.
DR GO; GO:0071257; P:cellular response to electrical stimulus; IMP:MGI.
DR GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0098712; P:L-glutamate import across plasma membrane; IDA:MGI.
DR GO; GO:0007626; P:locomotory behavior; IMP:UniProtKB.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; ISS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:UniProtKB.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IDA:UniProtKB.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; ISO:MGI.
DR GO; GO:0019233; P:sensory perception of pain; IMP:UniProtKB.
DR Gene3D; 2.10.50.30; -; 1.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR000337; GPCR_3.
DR InterPro; IPR011500; GPCR_3_9-Cys_dom.
DR InterPro; IPR038550; GPCR_3_9-Cys_sf.
DR InterPro; IPR017978; GPCR_3_C.
DR InterPro; IPR017979; GPCR_3_CS.
DR InterPro; IPR001256; GPCR_3_mGluR1.
DR InterPro; IPR000162; GPCR_3_mtglu_rcpt.
DR InterPro; IPR019588; Metabotropic_Glu_rcpt_Homer-bd.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF00003; 7tm_3; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF10606; GluR_Homer-bdg; 1.
DR Pfam; PF07562; NCD3G; 1.
DR PRINTS; PR00248; GPCRMGR.
DR PRINTS; PR01051; MTABOTROPC1R.
DR PRINTS; PR00593; MTABOTROPICR.
DR SMART; SM01229; GluR_Homer-bdg; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
DR PROSITE; PS00979; G_PROTEIN_RECEP_F3_1; 1.
DR PROSITE; PS00980; G_PROTEIN_RECEP_F3_2; 1.
DR PROSITE; PS00981; G_PROTEIN_RECEP_F3_3; 1.
DR PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1199
FT /note="Metabotropic glutamate receptor 1"
FT /id="PRO_0000012923"
FT TOPO_DOM 21..592
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 593..615
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 616..629
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 630..650
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 651..658
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 659..680
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 681..703
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 704..727
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 728..750
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 751..772
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 773..785
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 786..807
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 808..815
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 816..840
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 841..1199
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 882..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 959..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1055..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1117..1177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..973
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1033
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1082
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1157..1177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 74
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 186..188
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 409
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT MOD_RES 853
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 871
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 894
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23385"
FT MOD_RES 969
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1097
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1151
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P23385"
FT MOD_RES 1154
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 747
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 67..109
FT /evidence="ECO:0000250"
FT DISULFID 140
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 289..291
FT /evidence="ECO:0000250"
FT DISULFID 378..394
FT /evidence="ECO:0000250"
FT DISULFID 432..439
FT /evidence="ECO:0000250"
FT DISULFID 657..746
FT /evidence="ECO:0000250"
FT VAR_SEQ 317..321
FT /note="SDGWA -> RDSRN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10581402"
FT /id="VSP_007184"
FT VAR_SEQ 322..1199
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10581402"
FT /id="VSP_007185"
FT VAR_SEQ 887..906
FT /note="NSNGKSVSWSEPGGRQAPKG -> KKRQPEFSPSSQCPSAHVQL (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:10581402,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007186"
FT VAR_SEQ 907..1199
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10581402,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007187"
FT MUTAGEN 536
FT /note="I->K: Normal response to light but reduced retinal
FT electrical activity in response to light in dark adapted
FT retinas. Gross morphology is normal."
FT /evidence="ECO:0000269|PubMed:26427409"
SQ SEQUENCE 1199 AA; 133212 MW; FE5370AF160CC16E CRC64;
MVRLLLIFFP MIFLEMSILP RMPDRKVLLA GASSQRSVAR MDGDVIIGAL FSVHHQPPAE
KVPERKCGEI REQYGIQRVE AMFHTLDKIN ADPVLLPNIT LGSEIRDSCW HSSVALEQSI
EFIRDSLISI RDEKDGLNRC LPDGQTLPPG RTKKPIAGVI GPGSSSVAIQ VQNLLQLFDI
PQIAYSATSI DLSDKTLYKY FLRVVPSDTL QARAMLDIVK RYNWTYVSAV HTEGNYGESG
MDAFKELAAQ EGLCIAHSDK IYSNAGEKSF DRLLRKLRER LPKARVVVCF CEGMTVRGLL
SAMRRLGVVG EFSLIGSDGW ADRDEVIEGY EVEANGGITI KLQSPEVRSF DDYFLKLRLD
TNTRNPWFPE FWQHRFQCRL PGHLLENPNF KKVCTGNESL EENYVQDSKM GFVINAIYAM
AHGLQNMHHA LCPGYVGLCD AMKPIDGRKL LDFLIKSSFV GVSGEEVWFD EKGDAPGRYD
IMNLQYTEAN RYDYVHVGTW HEGVLNIDDY KIQMNKSGMV RSVCSEPCLK GQIKVIRKGE
VSCCWICTAC KENEFVQDEF TCRACDLGWW PNAELTGCEP ITIRYLEWSD IESIIAIAFS
CLGILVTLFV TLIFVLYRDT PVVKSSSREL CYIILAGIFL GYVCPFTLIA KPTTTSCYLQ
RLLVGLSSAM CYSALVTKTN RIARILAGSK KKICTRKPRF MSAWAQVIIA SILISVQLTL
VVTLIIMEPP MPILSYPSIK EVYLICNTSN LGVVAPVGYN GLLIMSCTYY AFKTRNVPAN
FNEAKYIAFT MYTTCIIWLA FVPIYFGSNY KIITTCFAVS LSVTVALGCM FTPKMYIIIA
KPERNVRSAF TTSDVVRMHV GDGKLPCRSN TFLNIFRRKK PGAGNANSNG KSVSWSEPGG
RQAPKGQHVW QRLSVHVKTN ETACNQTAVI KPLTKSYQGS GKSLTFSDAS TKTLYNVEEE
DNTPSTHFSP PSSPSMVVHR RGPPVATTPP LPPHLSAEET PLFLADSVIP KGLPPPLPQQ
QQQPPPQPPP QQPKSLMDQL QGVVTNFGSG IPDFHAVLAG PGTPGNGLRS LYPPPPPPQH
LQMLPLQLST FREEPISPPG EDDDDDSSER FKLLQEFVYE REGNTEEDDL EEEEDLPAAS
KLTPEDSPAL TPPSPFRDSV ASGSSVPSSP VSESVLCTPP NVTYASVILR DYKQSSSTL
