GRM3_HUMAN
ID GRM3_HUMAN Reviewed; 879 AA.
AC Q14832; Q2PNZ6; Q75MV4; Q75N17; Q86YG6; Q8TBH9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Metabotropic glutamate receptor 3;
DE Short=mGluR3;
DE Flags: Precursor;
GN Name=GRM3; Synonyms=GPRC1C, MGLUR3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=8840013; DOI=10.1016/0169-328x(96)00037-x;
RA Makoff A., Volpe F., Lelchuk R., Harrington K., Emson P.;
RT "Molecular characterization and localization of human metabotropic
RT glutamate receptor type 3.";
RL Brain Res. Mol. Brain Res. 40:55-63(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
RC TISSUE=Lymphoblast;
RX PubMed=16417579; DOI=10.1111/j.1471-4159.2005.03609.x;
RA Sartorius L.J., Nagappan G., Lipska B.K., Lu B., Sei Y., Ren-Patterson R.,
RA Li Z., Weinberger D.R., Harrison P.J.;
RT "Alternative splicing of human metabotropic glutamate receptor 3.";
RL J. Neurochem. 96:1139-1148(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., 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., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC 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 [5]
RP X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) OF 26-504 OF MUTANT SER-240, AND
RP DISULFIDE BONDS.
RG Structural genomics consortium (SGC);
RT "Crystal structure of metabotropic glutamate receptor 3 precursor in
RT presence of LY341495 antagonist.";
RL Submitted (JUL-2011) to the PDB data bank.
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 inhibits adenylate cyclase activity.
CC {ECO:0000269|PubMed:8840013}.
CC -!- SUBUNIT: Interacts with TAMALIN. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8840013};
CC Multi-pass membrane protein {ECO:0000269|PubMed:8840013}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14832-1; Sequence=Displayed;
CC Name=2; Synonyms=GRM3Delta4;
CC IsoId=Q14832-2; Sequence=VSP_047679, VSP_047680;
CC -!- TISSUE SPECIFICITY: Detected in brain cortex, thalamus, subthalamic
CC nucleus, substantia nigra, hypothalamus, hippocampus, corpus callosum,
CC caudate nucleus and amygdala. {ECO:0000269|PubMed:8840013}.
CC -!- MISCELLANEOUS: [Isoform 2]: Appears to be membrane-associated, despite
CC the absence of the seven-transmembrane domain. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD15616.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=ABC47402.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA54796.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X77748; CAA54796.1; ALT_INIT; mRNA.
DR EMBL; DQ315361; ABC47402.1; ALT_INIT; mRNA.
DR EMBL; AC004829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005009; AAD15616.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC002081; AAC60379.2; -; Genomic_DNA.
DR EMBL; BC022496; AAH22496.2; -; mRNA.
DR EMBL; BC041407; AAH41407.1; -; mRNA.
DR CCDS; CCDS5600.1; -. [Q14832-1]
DR CCDS; CCDS87515.1; -. [Q14832-2]
DR RefSeq; NP_000831.2; NM_000840.2. [Q14832-1]
DR RefSeq; XP_011514390.1; XM_011516088.1.
DR PDB; 3SM9; X-ray; 2.26 A; A=26-504.
DR PDB; 4XAR; X-ray; 2.26 A; A=2-508.
DR PDB; 5CNK; X-ray; 3.15 A; A/B/C=2-507.
DR PDB; 5CNM; X-ray; 2.84 A; A=2-507.
DR PDB; 6B7H; X-ray; 2.82 A; A=2-507.
DR PDB; 7WI6; EM; 3.71 A; A/B=23-879.
DR PDB; 7WI8; EM; 4.17 A; A/B=23-879.
DR PDB; 7WIH; EM; 3.68 A; A/B=23-879.
DR PDBsum; 3SM9; -.
DR PDBsum; 4XAR; -.
DR PDBsum; 5CNK; -.
DR PDBsum; 5CNM; -.
DR PDBsum; 6B7H; -.
DR PDBsum; 7WI6; -.
DR PDBsum; 7WI8; -.
DR PDBsum; 7WIH; -.
DR AlphaFoldDB; Q14832; -.
DR SMR; Q14832; -.
DR BioGRID; 109170; 8.
DR CORUM; Q14832; -.
DR IntAct; Q14832; 1.
DR STRING; 9606.ENSP00000355316; -.
DR BindingDB; Q14832; -.
DR ChEMBL; CHEMBL2888; -.
DR DrugBank; DB05096; LY2140023.
DR DrugCentral; Q14832; -.
DR GuidetoPHARMACOLOGY; 291; -.
DR GlyGen; Q14832; 4 sites.
DR iPTMnet; Q14832; -.
DR PhosphoSitePlus; Q14832; -.
DR BioMuta; GRM3; -.
DR DMDM; 76803803; -.
DR MassIVE; Q14832; -.
DR PaxDb; Q14832; -.
DR PeptideAtlas; Q14832; -.
DR PRIDE; Q14832; -.
DR ProteomicsDB; 60202; -. [Q14832-1]
DR ProteomicsDB; 61428; -.
DR Antibodypedia; 15243; 392 antibodies from 35 providers.
DR DNASU; 2913; -.
DR Ensembl; ENST00000361669.7; ENSP00000355316.2; ENSG00000198822.11. [Q14832-1]
DR Ensembl; ENST00000439827.1; ENSP00000398767.1; ENSG00000198822.11. [Q14832-2]
DR GeneID; 2913; -.
DR KEGG; hsa:2913; -.
DR MANE-Select; ENST00000361669.7; ENSP00000355316.2; NM_000840.3; NP_000831.2.
DR UCSC; uc003uid.4; human. [Q14832-1]
DR CTD; 2913; -.
DR DisGeNET; 2913; -.
DR GeneCards; GRM3; -.
DR HGNC; HGNC:4595; GRM3.
DR HPA; ENSG00000198822; Tissue enriched (brain).
DR MIM; 601115; gene.
DR neXtProt; NX_Q14832; -.
DR OpenTargets; ENSG00000198822; -.
DR PharmGKB; PA28992; -.
DR VEuPathDB; HostDB:ENSG00000198822; -.
DR eggNOG; KOG1056; Eukaryota.
DR GeneTree; ENSGT01030000234595; -.
DR HOGENOM; CLU_005389_0_0_1; -.
DR InParanoid; Q14832; -.
DR OMA; CIARIFN; -.
DR PhylomeDB; Q14832; -.
DR TreeFam; TF313240; -.
DR PathwayCommons; Q14832; -.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-420499; Class C/3 (Metabotropic glutamate/pheromone receptors).
DR SignaLink; Q14832; -.
DR SIGNOR; Q14832; -.
DR BioGRID-ORCS; 2913; 9 hits in 1069 CRISPR screens.
DR ChiTaRS; GRM3; human.
DR GeneWiki; Metabotropic_glutamate_receptor_3; -.
DR GenomeRNAi; 2913; -.
DR Pharos; Q14832; Tchem.
DR PRO; PR:Q14832; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q14832; protein.
DR Bgee; ENSG00000198822; Expressed in endothelial cell and 101 other tissues.
DR ExpressionAtlas; Q14832; baseline and differential.
DR Genevisible; Q14832; HS.
DR GO; GO:0097449; C:astrocyte projection; ISS:ARUK-UCL.
DR GO; GO:0030424; C:axon; ISS:ARUK-UCL.
DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0001640; F:adenylate cyclase inhibiting G protein-coupled glutamate receptor activity; IBA:GO_Central.
DR GO; GO:0005246; F:calcium channel regulator activity; IEA:Ensembl.
DR GO; GO:0004930; F:G protein-coupled receptor activity; TAS:UniProtKB.
DR GO; GO:0008066; F:glutamate receptor activity; TAS:UniProtKB.
DR GO; GO:0001641; F:group II metabotropic glutamate receptor activity; IBA:GO_Central.
DR GO; GO:0097110; F:scaffold protein binding; ISS:ARUK-UCL.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; TAS:ProtInc.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IBA:GO_Central.
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; IPR001234; GPCR_3_mGluR3.
DR InterPro; IPR000162; GPCR_3_mtglu_rcpt.
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; PR01053; MTABOTROPC3R.
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; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..879
FT /note="Metabotropic glutamate receptor 3"
FT /id="PRO_0000012927"
FT TOPO_DOM 23..576
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 577..599
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 600..613
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 614..634
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 635..645
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 646..664
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 665..688
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 689..709
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 710..734
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 735..756
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 757..769
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 770..792
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 793..802
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 803..828
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 829..879
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 151
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 172..174
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 389
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 57..99
FT /evidence="ECO:0000269|Ref.5"
FT DISULFID 240..527
FT /evidence="ECO:0000250"
FT DISULFID 361..373
FT /evidence="ECO:0000269|Ref.5"
FT DISULFID 412..419
FT /evidence="ECO:0000269|Ref.5"
FT DISULFID 509..528
FT /evidence="ECO:0000250"
FT DISULFID 513..531
FT /evidence="ECO:0000250"
FT DISULFID 534..546
FT /evidence="ECO:0000250"
FT DISULFID 549..562
FT /evidence="ECO:0000250"
FT VAR_SEQ 442..537
FT /note="APFNPNKDADSIVKFDTFGDGMGRYNVFNFQNVGGKYSYLKVGHWAETLSLD
FT VNSIHWSRNSVPTSQCSDPCAPNEMKNMQPGDVCCWICIPCEPY -> GADDNHVHLCQ
FT PEWLCGLGLFVCTQGSHHPVSTPEECCHTQTAPQQVQCQWNWDHILSVLCKHVCANGVQ
FT WAGSPRLHHLISVIVNCSSVLVFLDC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16417579"
FT /id="VSP_047679"
FT VAR_SEQ 538..879
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16417579"
FT /id="VSP_047680"
FT VARIANT 475
FT /note="G -> D (in dbSNP:rs17161026)"
FT /id="VAR_049274"
FT CONFLICT 96
FT /note="L -> F (in Ref. 4; AAH41407)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="P -> T (in Ref. 4; AAH22496)"
FT /evidence="ECO:0000305"
FT CONFLICT 512
FT /note="P -> A (in Ref. 4; AAH22496)"
FT /evidence="ECO:0000305"
FT CONFLICT 856
FT /note="S -> Y (in Ref. 4; AAH22496)"
FT /evidence="ECO:0000305"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:3SM9"
FT STRAND 38..45
FT /evidence="ECO:0007829|PDB:3SM9"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:3SM9"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:3SM9"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:3SM9"
FT HELIX 66..81
FT /evidence="ECO:0007829|PDB:3SM9"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:3SM9"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:3SM9"
FT HELIX 102..114
FT /evidence="ECO:0007829|PDB:3SM9"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:3SM9"
FT HELIX 151..161
FT /evidence="ECO:0007829|PDB:3SM9"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:3SM9"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:3SM9"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:3SM9"
FT TURN 181..186
FT /evidence="ECO:0007829|PDB:3SM9"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:3SM9"
FT HELIX 195..207
FT /evidence="ECO:0007829|PDB:3SM9"
FT STRAND 212..220
FT /evidence="ECO:0007829|PDB:3SM9"
FT HELIX 221..235
FT /evidence="ECO:0007829|PDB:3SM9"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:3SM9"
FT STRAND 240..247
FT /evidence="ECO:0007829|PDB:3SM9"
FT HELIX 253..264
FT /evidence="ECO:0007829|PDB:3SM9"
FT STRAND 271..275
FT /evidence="ECO:0007829|PDB:3SM9"
FT HELIX 278..290
FT /evidence="ECO:0007829|PDB:3SM9"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:3SM9"
FT TURN 301..305
FT /evidence="ECO:0007829|PDB:3SM9"
FT HELIX 307..310
FT /evidence="ECO:0007829|PDB:3SM9"
FT TURN 314..319
FT /evidence="ECO:0007829|PDB:3SM9"
FT STRAND 321..325
FT /evidence="ECO:0007829|PDB:3SM9"
FT HELIX 331..338
FT /evidence="ECO:0007829|PDB:3SM9"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:3SM9"
FT HELIX 351..359
FT /evidence="ECO:0007829|PDB:3SM9"
FT TURN 381..383
FT /evidence="ECO:0007829|PDB:3SM9"
FT HELIX 390..411
FT /evidence="ECO:0007829|PDB:3SM9"
FT HELIX 420..423
FT /evidence="ECO:0007829|PDB:3SM9"
FT HELIX 427..433
FT /evidence="ECO:0007829|PDB:3SM9"
FT HELIX 435..437
FT /evidence="ECO:0007829|PDB:3SM9"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:4XAR"
FT HELIX 450..452
FT /evidence="ECO:0007829|PDB:5CNM"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:4XAR"
FT STRAND 466..476
FT /evidence="ECO:0007829|PDB:3SM9"
FT STRAND 478..492
FT /evidence="ECO:0007829|PDB:3SM9"
FT HELIX 494..496
FT /evidence="ECO:0007829|PDB:3SM9"
SQ SEQUENCE 879 AA; 98879 MW; 7EB84521676E8304 CRC64;
MKMLTRLQVL TLALFSKGFL LSLGDHNFLR REIKIEGDLV LGGLFPINEK GTGTEECGRI
NEDRGIQRLE AMLFAIDEIN KDDYLLPGVK LGVHILDTCS RDTYALEQSL EFVRASLTKV
DEAEYMCPDG SYAIQENIPL LIAGVIGGSY SSVSIQVANL LRLFQIPQIS YASTSAKLSD
KSRYDYFART VPPDFYQAKA MAEILRFFNW TYVSTVASEG DYGETGIEAF EQEARLRNIC
IATAEKVGRS NIRKSYDSVI RELLQKPNAR VVVLFMRSDD SRELIAAASR ANASFTWVAS
DGWGAQESII KGSEHVAYGA ITLELASQPV RQFDRYFQSL NPYNNHRNPW FRDFWEQKFQ
CSLQNKRNHR RVCDKHLAID SSNYEQESKI MFVVNAVYAM AHALHKMQRT LCPNTTKLCD
AMKILDGKKL YKDYLLKINF TAPFNPNKDA DSIVKFDTFG DGMGRYNVFN FQNVGGKYSY
LKVGHWAETL SLDVNSIHWS RNSVPTSQCS DPCAPNEMKN MQPGDVCCWI CIPCEPYEYL
ADEFTCMDCG SGQWPTADLT GCYDLPEDYI RWEDAWAIGP VTIACLGFMC TCMVVTVFIK
HNNTPLVKAS GRELCYILLF GVGLSYCMTF FFIAKPSPVI CALRRLGLGS SFAICYSALL
TKTNCIARIF DGVKNGAQRP KFISPSSQVF ICLGLILVQI VMVSVWLILE APGTRRYTLA
EKRETVILKC NVKDSSMLIS LTYDVILVIL CTVYAFKTRK CPENFNEAKF IGFTMYTTCI
IWLAFLPIFY VTSSDYRVQT TTMCISVSLS GFVVLGCLFA PKVHIILFQP QKNVVTHRLH
LNRFSVSGTG TTYSQSSAST YVPTVCNGRE VLDSTTSSL
