ID GRM8_HUMAN Reviewed; 908 AA. AC O00222; A4D0Y3; B0FZ74; B0M0L0; O15493; O95945; O95946; Q3MIV9; AC Q52M02; Q6J165; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 13-FEB-2019, entry version 173. DE RecName: Full=Metabotropic glutamate receptor 8; DE Short=mGluR8; DE Flags: Precursor; GN Name=GRM8; Synonyms=GPRC1H, MGLUR8; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A). RX PubMed=9299241; DOI=10.1006/geno.1997.4842; RA Scherer S.W., Soder S., Duvoisin R.M., Huizenga J.J., Tsui L.-C.; RT "The human metabotropic glutamate receptor 8 (GRM8) gene: a RT disproportionately large gene located at 7q31.3-q32.1."; RL Genomics 44:232-236(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND VARIANT ASN-768. RX PubMed=9473604; DOI=10.1016/S0169-328X(97)00277-5; RA Wu S., Wright R.A., Rockey P.K., Burgett S.G., Arnold J.S., RA Rosteck P.R. Jr., Johnson B.G., Schoepp D.D., Belagaje R.M.; RT "Group III human metabotropic glutamate receptors 4, 7 and 8: RT molecular cloning, functional expression, and comparison of RT pharmacological properties in RGT cells."; RL Brain Res. Mol. Brain Res. 53:88-97(1998). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND C). RC TISSUE=Fetal brain; RX PubMed=10216218; DOI=10.1016/S0169-328X(99)00050-9; RA Malherbe P., Kratzeisen C., Lundstrom K., Richards J.G., Faull R.L.M., RA Mutel V.; RT "Cloning and functional expression of alternative spliced variants of RT the human metabotropic glutamate receptor 8."; RL Brain Res. Mol. Brain Res. 67:201-210(1999). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B). RA Stormann T.M., Simin R.T., Hammerland L.G., Fuller F.H.; RT "Homo sapiens metabotropic glutamate receptor."; RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A). RC TISSUE=Brain; RA Kaighin V.A., Martin A.L., Aronstam R.S.; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-10; THR-265; RP TYR-362; ASP-368 AND PHE-430. RG NIEHS SNPs program; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM A), AND VARIANT RP GLN-343. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., RA Waterston R.H., Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). RC TISSUE=Colon; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). 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 CC activity of down-stream effectors, such as adenylate cyclase. CC Signaling inhibits adenylate cyclase activity. CC {ECO:0000269|PubMed:9473604}. CC -!- SUBUNIT: Interacts with PICK1. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=A; Synonyms=mGluR8a; CC IsoId=O00222-1; Sequence=Displayed; CC Name=B; Synonyms=mGluR8b; CC IsoId=O00222-2; Sequence=VSP_002032; CC Name=C; Synonyms=mGluR8c; CC IsoId=O00222-3; Sequence=VSP_002033, VSP_002034; CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/grm8/"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; U95025; AAB72040.1; -; mRNA. DR EMBL; U92459; AAB51764.1; -; mRNA. DR EMBL; AJ236921; CAB36968.1; -; mRNA. DR EMBL; AJ236922; CAB36969.1; -; mRNA. DR EMBL; AY608335; AAT37959.1; -; mRNA. DR EMBL; EU432125; ABY87924.1; -; mRNA. DR EMBL; EU368948; ABY59657.1; -; Genomic_DNA. DR EMBL; CH236947; EAL24322.1; -; Genomic_DNA. DR EMBL; BC093725; AAH93725.1; -; mRNA. DR EMBL; BC101675; AAI01676.1; -; mRNA. DR CCDS; CCDS47696.1; -. [O00222-2] DR CCDS; CCDS5794.1; -. [O00222-1] DR RefSeq; NP_000836.2; NM_000845.2. [O00222-1] DR RefSeq; NP_001120795.1; NM_001127323.1. [O00222-2] DR RefSeq; XP_006716001.1; XM_006715938.3. [O00222-1] DR RefSeq; XP_011514393.1; XM_011516091.1. [O00222-1] DR RefSeq; XP_011514394.1; XM_011516092.2. [O00222-2] DR RefSeq; XP_016867563.1; XM_017012074.1. [O00222-1] DR UniGene; Hs.449625; -. DR PDB; 6BSZ; X-ray; 2.65 A; A/B=37-514. DR PDB; 6BT5; X-ray; 2.92 A; A/B=37-514. DR PDB; 6E5V; X-ray; 2.95 A; A/B=2-508. DR PDBsum; 6BSZ; -. DR PDBsum; 6BT5; -. DR PDBsum; 6E5V; -. DR ProteinModelPortal; O00222; -. DR SMR; O00222; -. DR CORUM; O00222; -. DR IntAct; O00222; 1. DR STRING; 9606.ENSP00000344173; -. DR BindingDB; O00222; -. DR ChEMBL; CHEMBL3228; -. DR DrugBank; DB00142; L-Glutamic Acid. DR GuidetoPHARMACOLOGY; 296; -. DR iPTMnet; O00222; -. DR PhosphoSitePlus; O00222; -. DR BioMuta; GRM8; -. DR PaxDb; O00222; -. DR PeptideAtlas; O00222; -. DR PRIDE; O00222; -. DR ProteomicsDB; 47792; -. DR ProteomicsDB; 47793; -. [O00222-2] DR ProteomicsDB; 47794; -. [O00222-3] DR Ensembl; ENST00000339582; ENSP00000344173; ENSG00000179603. [O00222-1] DR Ensembl; ENST00000341617; ENSP00000345747; ENSG00000179603. [O00222-3] DR Ensembl; ENST00000358373; ENSP00000351142; ENSG00000179603. [O00222-2] DR Ensembl; ENST00000472701; ENSP00000419832; ENSG00000179603. [O00222-2] DR GeneID; 2918; -. DR KEGG; hsa:2918; -. DR UCSC; uc003vlr.3; human. [O00222-1] DR CTD; 2918; -. DR DisGeNET; 2918; -. DR EuPathDB; HostDB:ENSG00000179603.17; -. DR GeneCards; GRM8; -. DR H-InvDB; HIX0025292; -. DR HGNC; HGNC:4600; GRM8. DR HPA; HPA051481; -. DR MIM; 601116; gene. DR neXtProt; NX_O00222; -. DR OpenTargets; ENSG00000179603; -. DR PharmGKB; PA28997; -. DR eggNOG; KOG1056; Eukaryota. DR eggNOG; ENOG410XR6W; LUCA. DR GeneTree; ENSGT00940000153879; -. DR HOVERGEN; HBG107965; -. DR InParanoid; O00222; -. DR KO; K04608; -. DR OMA; TYVHAIA; -. DR OrthoDB; 483746at2759; -. DR PhylomeDB; O00222; -. DR TreeFam; TF313240; -. DR Reactome; R-HSA-418594; G alpha (i) signalling events. DR Reactome; R-HSA-420499; Class C/3 (Metabotropic glutamate/pheromone receptors). DR ChiTaRS; GRM8; human. DR GeneWiki; Metabotropic_glutamate_receptor_8; -. DR GenomeRNAi; 2918; -. DR PRO; PR:O00222; -. DR Proteomes; UP000005640; Chromosome 7. DR Bgee; ENSG00000179603; Expressed in 138 organ(s), highest expression level in anterior cingulate cortex. DR ExpressionAtlas; O00222; baseline and differential. DR Genevisible; O00222; HS. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0042734; C:presynaptic membrane; IBA:GO_Central. DR GO; GO:0004930; F:G protein-coupled receptor activity; IMP:UniProtKB. DR GO; GO:0008066; F:glutamate receptor activity; IMP:UniProtKB. DR GO; GO:0007196; P:adenylate cyclase-inhibiting G protein-coupled glutamate receptor signaling pathway; IMP:UniProtKB. DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; IBA:GO_Central. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:Reactome. DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IBA:GO_Central. DR GO; GO:0007601; P:visual perception; TAS:ProtInc. 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; IPR000162; GPCR_3_mtglu_rcpt. DR InterPro; IPR000144; GPCR_3_mtglu_rcpt_8. DR InterPro; IPR028082; Peripla_BP_I. DR Pfam; PF00003; 7tm_3; 1. DR Pfam; PF01094; ANF_receptor; 1. DR Pfam; PF07562; NCD3G; 1. DR PRINTS; PR00248; GPCRMGR. DR PRINTS; PR01058; MTABOTROPC8R. DR PRINTS; PR00593; MTABOTROPICR. 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 3D-structure; Alternative splicing; Cell membrane; Complete proteome; KW Disulfide bond; G-protein coupled receptor; Glycoprotein; KW Isopeptide bond; Membrane; Polymorphism; Receptor; Reference proteome; KW Sensory transduction; Signal; Transducer; Transmembrane; KW Transmembrane helix; Ubl conjugation. FT SIGNAL 1 33 {ECO:0000255}. FT CHAIN 34 908 Metabotropic glutamate receptor 8. FT /FTId=PRO_0000012941. FT TOPO_DOM 34 583 Extracellular. {ECO:0000255}. FT TRANSMEM 584 608 Helical; Name=1. {ECO:0000255}. FT TOPO_DOM 609 620 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 621 641 Helical; Name=2. {ECO:0000255}. FT TOPO_DOM 642 647 Extracellular. {ECO:0000255}. FT TRANSMEM 648 668 Helical; Name=3. {ECO:0000255}. FT TOPO_DOM 669 695 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 696 716 Helical; Name=4. {ECO:0000255}. FT TOPO_DOM 717 746 Extracellular. {ECO:0000255}. FT TRANSMEM 747 768 Helical; Name=5. {ECO:0000255}. FT TOPO_DOM 769 781 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 782 803 Helical; Name=6. {ECO:0000255}. FT TOPO_DOM 804 818 Extracellular. {ECO:0000255}. FT TRANSMEM 819 843 Helical; Name=7. {ECO:0000255}. FT TOPO_DOM 844 908 Cytoplasmic. {ECO:0000255}. FT REGION 177 179 Glutamate binding. {ECO:0000250}. FT BINDING 156 156 Glutamate. {ECO:0000250}. FT BINDING 227 227 Glutamate. {ECO:0000250}. FT BINDING 309 309 Glutamate. {ECO:0000250}. FT BINDING 401 401 Glutamate. {ECO:0000250}. FT CARBOHYD 95 95 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 298 298 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 452 452 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 480 480 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 565 565 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 64 106 {ECO:0000250}. FT DISULFID 246 534 {ECO:0000250}. FT DISULFID 369 384 {ECO:0000250}. FT DISULFID 424 431 {ECO:0000250}. FT DISULFID 516 535 {ECO:0000250}. FT DISULFID 520 538 {ECO:0000250}. FT DISULFID 541 553 {ECO:0000250}. FT DISULFID 556 569 {ECO:0000250}. FT CROSSLNK 882 882 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO1). FT {ECO:0000250|UniProtKB:P47743}. FT VAR_SEQ 454 501 SAGTPVTFNENGDAPGRYDIFQYQITNKSTEYKVIGHWTNQ FT LHLKVED -> CRRGIQMSLPWPTLFTPSFSSSWAVLALLS FT LLMKTEMLLDVMISSSIK (in isoform C). FT {ECO:0000303|PubMed:10216218}. FT /FTId=VSP_002033. FT VAR_SEQ 502 908 Missing (in isoform C). FT {ECO:0000303|PubMed:10216218}. FT /FTId=VSP_002034. FT VAR_SEQ 893 908 TSSTKTTYISYSNHSI -> SKSSVEFPMVKSGSTS (in FT isoform B). {ECO:0000303|PubMed:10216218, FT ECO:0000303|Ref.4}. FT /FTId=VSP_002032. FT VARIANT 10 10 S -> C (in dbSNP:rs769194). FT {ECO:0000269|Ref.6}. FT /FTId=VAR_014446. FT VARIANT 21 21 F -> C (in dbSNP:rs769202). FT /FTId=VAR_014447. FT VARIANT 265 265 I -> T (in dbSNP:rs17150343). FT {ECO:0000269|Ref.6}. FT /FTId=VAR_049278. FT VARIANT 343 343 R -> Q (in dbSNP:rs13309334). FT {ECO:0000269|PubMed:12853948}. FT /FTId=VAR_054752. FT VARIANT 362 362 F -> Y (in dbSNP:rs78124913). FT {ECO:0000269|Ref.6}. FT /FTId=VAR_054477. FT VARIANT 368 368 G -> D (in dbSNP:rs78947184). FT {ECO:0000269|Ref.6}. FT /FTId=VAR_054478. FT VARIANT 392 392 R -> Q (in dbSNP:rs2234947). FT /FTId=VAR_014448. FT VARIANT 430 430 L -> F (in dbSNP:rs75863532). FT {ECO:0000269|Ref.6}. FT /FTId=VAR_054479. FT VARIANT 548 548 V -> G (in dbSNP:rs2234948). FT /FTId=VAR_014449. FT VARIANT 768 768 I -> N (in dbSNP:rs1051433). FT {ECO:0000269|PubMed:9473604}. FT /FTId=VAR_054753. FT VARIANT 902 902 S -> I (in dbSNP:rs10225567). FT /FTId=VAR_054754. FT CONFLICT 194 194 R -> A (in Ref. 1; AAB72040). FT {ECO:0000305}. FT CONFLICT 460 460 T -> I (in Ref. 1; AAB72040). FT {ECO:0000305}. FT CONFLICT 591 591 A -> V (in Ref. 5; ABY87924). FT {ECO:0000305}. FT CONFLICT 642 642 A -> G (in Ref. 1; AAB72040). FT {ECO:0000305}. FT CONFLICT 904 904 S -> T (in Ref. 1; AAB72040). FT {ECO:0000305}. FT STRAND 39 42 {ECO:0000244|PDB:6BSZ}. FT STRAND 45 52 {ECO:0000244|PDB:6BSZ}. FT STRAND 55 57 {ECO:0000244|PDB:6BSZ}. FT STRAND 63 67 {ECO:0000244|PDB:6BSZ}. FT TURN 69 72 {ECO:0000244|PDB:6BSZ}. FT HELIX 73 88 {ECO:0000244|PDB:6BSZ}. FT TURN 92 95 {ECO:0000244|PDB:6BSZ}. FT STRAND 98 104 {ECO:0000244|PDB:6BSZ}. FT HELIX 109 116 {ECO:0000244|PDB:6BSZ}. FT HELIX 117 119 {ECO:0000244|PDB:6BSZ}. FT STRAND 147 151 {ECO:0000244|PDB:6BSZ}. FT HELIX 156 166 {ECO:0000244|PDB:6BSZ}. FT TURN 167 170 {ECO:0000244|PDB:6BSZ}. FT STRAND 173 177 {ECO:0000244|PDB:6BSZ}. FT HELIX 181 184 {ECO:0000244|PDB:6BSZ}. FT TURN 186 188 {ECO:0000244|PDB:6BSZ}. FT STRAND 192 196 {ECO:0000244|PDB:6BSZ}. FT HELIX 199 213 {ECO:0000244|PDB:6BSZ}. FT STRAND 217 225 {ECO:0000244|PDB:6BSZ}. FT HELIX 226 241 {ECO:0000244|PDB:6BSZ}. FT STRAND 242 244 {ECO:0000244|PDB:6BSZ}. FT STRAND 246 253 {ECO:0000244|PDB:6BSZ}. FT HELIX 261 269 {ECO:0000244|PDB:6BSZ}. FT STRAND 277 281 {ECO:0000244|PDB:6BSZ}. FT HELIX 284 296 {ECO:0000244|PDB:6BSZ}. FT TURN 300 302 {ECO:0000244|PDB:6BSZ}. FT STRAND 304 307 {ECO:0000244|PDB:6BSZ}. FT TURN 309 313 {ECO:0000244|PDB:6BSZ}. FT TURN 316 320 {ECO:0000244|PDB:6BSZ}. FT TURN 322 327 {ECO:0000244|PDB:6BSZ}. FT STRAND 329 334 {ECO:0000244|PDB:6BSZ}. FT HELIX 339 346 {ECO:0000244|PDB:6BSZ}. FT TURN 350 352 {ECO:0000244|PDB:6BSZ}. FT HELIX 359 367 {ECO:0000244|PDB:6BSZ}. FT TURN 390 392 {ECO:0000244|PDB:6BSZ}. FT HELIX 402 423 {ECO:0000244|PDB:6BSZ}. FT STRAND 424 426 {ECO:0000244|PDB:6BSZ}. FT HELIX 432 434 {ECO:0000244|PDB:6BSZ}. FT HELIX 439 448 {ECO:0000244|PDB:6BSZ}. FT STRAND 450 452 {ECO:0000244|PDB:6BT5}. FT TURN 454 456 {ECO:0000244|PDB:6E5V}. FT STRAND 458 460 {ECO:0000244|PDB:6BT5}. FT STRAND 463 465 {ECO:0000244|PDB:6BT5}. FT STRAND 470 478 {ECO:0000244|PDB:6BSZ}. FT STRAND 483 497 {ECO:0000244|PDB:6BSZ}. FT HELIX 499 501 {ECO:0000244|PDB:6BSZ}. SQ SEQUENCE 908 AA; 101741 MW; 95C2D5883DAF6FDE CRC64; MVCEGKRSAS CPCFFLLTAK FYWILTMMQR THSQEYAHSI RVDGDIILGG LFPVHAKGER GVPCGELKKE KGIHRLEAML YAIDQINKDP DLLSNITLGV RILDTCSRDT YALEQSLTFV QALIEKDASD VKCANGDPPI FTKPDKISGV IGAAASSVSI MVANILRLFK IPQISYASTA PELSDNTRYD FFSRVVPPDS YQAQAMVDIV TALGWNYVST LASEGNYGES GVEAFTQISR EIGGVCIAQS QKIPREPRPG EFEKIIKRLL ETPNARAVIM FANEDDIRRI LEAAKKLNQS GHFLWIGSDS WGSKIAPVYQ QEEIAEGAVT ILPKRASIDG FDRYFRSRTL ANNRRNVWFA EFWEENFGCK LGSHGKRNSH IKKCTGLERI ARDSSYEQEG KVQFVIDAVY SMAYALHNMH KDLCPGYIGL CPRMSTIDGK ELLGYIRAVN FNGSAGTPVT FNENGDAPGR YDIFQYQITN KSTEYKVIGH WTNQLHLKVE DMQWAHREHT HPASVCSLPC KPGERKKTVK GVPCCWHCER CEGYNYQVDE LSCELCPLDQ RPNMNRTGCQ LIPIIKLEWH SPWAVVPVFV AILGIIATTF VIVTFVRYND TPIVRASGRE LSYVLLTGIF LCYSITFLMI AAPDTIICSF RRVFLGLGMC FSYAALLTKT NRIHRIFEQG KKSVTAPKFI SPASQLVITF SLISVQLLGV FVWFVVDPPH IIIDYGEQRT LDPEKARGVL KCDISDLSLI CSLGYSILLM VTCTVYAIKT RGVPETFNEA KPIGFTMYTT CIIWLAFIPI FFGTAQSAEK MYIQTTTLTV SMSLSASVSL GMLYMPKVYI IIFHPEQNVQ KRKRSFKAVV TAATMQSKLI QKGNDRPNGE VKSELCESLE TNTSSTKTTY ISYSNHSI //