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   27-MAR-2024, entry version 204.
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   GlyCosmos; P97772; 5 sites, No reported glycans.
DR   GlyGen; P97772; 6 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; P97772; -.
DR   PhosphoSitePlus; P97772; -.
DR   SwissPalm; P97772; -.
DR   jPOST; P97772; -.
DR   MaxQB; P97772; -.
DR   PaxDb; 10090-ENSMUSP00000037255; -.
DR   PeptideAtlas; P97772; -.
DR   ProteomicsDB; 269836; -. [P97772-1]
DR   ProteomicsDB; 269837; -. [P97772-2]
DR   ProteomicsDB; 269838; -. [P97772-3]
DR   Pumba; P97772; -.
DR   Antibodypedia; 2943; 814 antibodies from 43 providers.
DR   DNASU; 14816; -.
DR   Ensembl; ENSMUST00000044306.13; ENSMUSP00000037255.7; ENSMUSG00000019828.14. [P97772-1]
DR   Ensembl; ENSMUST00000105560.2; ENSMUSP00000101189.2; ENSMUSG00000019828.14. [P97772-2]
DR   Ensembl; ENSMUST00000105561.9; ENSMUSP00000101190.3; ENSMUSG00000019828.14. [P97772-2]
DR   GeneID; 14816; -.
DR   KEGG; mmu:14816; -.
DR   UCSC; uc007ejh.2; mouse. [P97772-2]
DR   UCSC; uc007eji.2; mouse. [P97772-1]
DR   AGR; MGI:1351338; -.
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; NEMACNQ; -.
DR   OrthoDB; 5388627at2759; -.
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; 3 hits in 76 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 cell types or tissues.
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: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:0005886; C:plasma membrane; ISS:UniProtKB.
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; ISO:MGI.
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; ISO:MGI.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
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:0007206; P:phospholipase C-activating G protein-coupled glutamate receptor 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   CDD; cd15449; 7tmC_mGluR1; 1.
DR   CDD; cd06374; PBP1_mGluR_groupI; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 2.10.50.30; GPCR, family 3, nine cysteines domain; 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   PANTHER; PTHR24060; METABOTROPIC GLUTAMATE RECEPTOR; 1.
DR   PANTHER; PTHR24060:SF29; METABOTROPIC GLUTAMATE RECEPTOR 1; 1.
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; Periplasmic binding protein-like I; 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.
DR   Genevisible; P97772; MM.
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
//