GNMT_RAT
ID GNMT_RAT Reviewed; 293 AA.
AC P13255;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Glycine N-methyltransferase;
DE EC=2.1.1.20 {ECO:0000269|PubMed:12859184, ECO:0000269|PubMed:3838667};
DE AltName: Full=Folate-binding protein {ECO:0000303|PubMed:6587377};
GN Name=Gnmt; Synonyms=Fbp-cII {ECO:0000303|PubMed:6587377};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 2-7, CLEAVAGE
RP OF INITIATOR METHIONINE, AND ACETYLATION AT VAL-2.
RC STRAIN=Sprague-Dawley;
RX PubMed=2822402; DOI=10.1111/j.1432-1033.1987.tb13398.x;
RA Ogawa H., Konishi K., Takata Y., Nakashima H., Fujioka M.;
RT "Rat glycine methyltransferase. Complete amino acid sequence deduced from a
RT cDNA clone and characterization of the genomic DNA.";
RL Eur. J. Biochem. 168:141-151(1987).
RN [2]
RP SUBCELLULAR LOCATION, AND FOLATE BINDING.
RX PubMed=6587377; DOI=10.1073/pnas.81.12.3631;
RA Cook R.J., Wagner C.;
RT "Glycine N-methyltransferase is a folate binding protein of rat liver
RT cytosol.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:3631-3634(1984).
RN [3]
RP CATALYTIC ACTIVITY, FUNCTION, ACTIVITY REGULATION, AND FOLATE BINDING.
RX PubMed=3838667; DOI=10.1016/s0006-291x(85)80006-1;
RA Wagner C., Briggs W.T., Cook R.J.;
RT "Inhibition of glycine N-methyltransferase activity by folate derivatives:
RT implications for regulation of methyl group metabolism.";
RL Biochem. Biophys. Res. Commun. 127:746-752(1985).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 2-293 IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE.
RC TISSUE=Liver;
RX PubMed=8810903; DOI=10.1021/bi961068n;
RA Fu Z., Hu Y., Konishi K., Takata Y., Ogawa H., Gomi T., Fujioka M.,
RA Takusagawa F.;
RT "Crystal structure of glycine N-methyltransferase from rat liver.";
RL Biochemistry 35:11985-11993(1996).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=9655336; DOI=10.1002/pro.5560070608;
RA Pattanayek R., Newcomer M.E., Wagner C.;
RT "Crystal structure of apo-glycine N-methyltransferase (GNMT).";
RL Protein Sci. 7:1326-1331(1998).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=10756111; DOI=10.1006/jmbi.2000.3637;
RA Huang Y., Komoto J., Konishi K., Takata Y., Ogawa H., Gomi T., Fujioka M.,
RA Takusagawa F.;
RT "Mechanisms for auto-inhibition and forced product release in glycine N-
RT methyltransferase: crystal structures of wild-type, mutant R175K and S-
RT adenosylhomocysteine-bound R175K enzymes.";
RL J. Mol. Biol. 298:149-162(2000).
RN [7] {ECO:0007744|PDB:1NBH, ECO:0007744|PDB:1NBI}
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-292 IN COMPLEXES WITH
RP S-ADENOSYL-L-METHIONINE AND ACETATE, MUTAGENESIS OF TYR-34; ARG-176 AND
RP TYR-221, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12859184; DOI=10.1021/bi034245a;
RA Takata Y., Huang Y., Komoto J., Yamada T., Konishi K., Ogawa H., Gomi T.,
RA Fujioka M., Takusagawa F.;
RT "Catalytic mechanism of glycine N-methyltransferase.";
RL Biochemistry 42:8394-8402(2003).
RN [8] {ECO:0007744|PDB:2IDJ, ECO:0007744|PDB:2IDK}
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 2-292 IN COMPLEX WITH
RP 5-METHYLTETRAHYDROFOLATE, AND ACTIVITY REGULATION.
RX PubMed=17158459; DOI=10.1074/jbc.m610384200;
RA Luka Z., Pakhomova S., Loukachevitch L.V., Egli M., Newcomer M.E.,
RA Wagner C.;
RT "5-methyltetrahydrofolate is bound in intersubunit areas of rat liver
RT folate-binding protein glycine N-methyltransferase.";
RL J. Biol. Chem. 282:4069-4075(2007).
RN [9] {ECO:0007744|PDB:3THR, ECO:0007744|PDB:3THS}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-293 IN COMPLEXES WITH
RP 5-METHYLTETRAHYDROFOLATE PENTAGLUTAMATE AND 5-METHYLTETRAHYDROFOLATE
RP MONOGLUTAMATE, AND SUBUNIT.
RX PubMed=22037183; DOI=10.1016/j.bbapap.2011.10.008;
RA Luka Z., Pakhomova S., Loukachevitch L.V., Newcomer M.E., Wagner C.;
RT "Differences in folate-protein interactions result in differing inhibition
RT of native rat liver and recombinant glycine N-methyltransferase by 5-
RT methyltetrahydrofolate.";
RL Biochim. Biophys. Acta 1824:286-291(2012).
CC -!- FUNCTION: Catalyzes the methylation of glycine by using S-
CC adenosylmethionine (AdoMet) to form N-methylglycine (sarcosine) with
CC the concomitant production of S-adenosylhomocysteine (AdoHcy), a
CC reaction regulated by the binding of 5-methyltetrahydrofolate. Possible
CC crucial role in the regulation of tissue concentration of AdoMet and of
CC metabolism of methionine. {ECO:0000250|UniProtKB:Q14749}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-
CC homocysteine + sarcosine; Xref=Rhea:RHEA:19937, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57433, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789; EC=2.1.1.20;
CC Evidence={ECO:0000269|PubMed:12859184, ECO:0000269|PubMed:3838667};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19938;
CC Evidence={ECO:0000305|PubMed:12859184};
CC -!- ACTIVITY REGULATION: Inhibited by 5-methyltetrahydrofolate
CC monoglutamate and by 5-methyltetrahydrofolate pentaglutamate,
CC inhibition is much more effective by the pentaglutamate form than by
CC the monoglutamate form (PubMed:3838667). Two molecules of 5-
CC methyltetrahydrofolate are bound per tetramer. The binding sites are
CC localized between subunits. Inhibitor binding may preclude movements of
CC the polypeptide chain that are necessary for enzyme activity.
CC {ECO:0000269|PubMed:17158459, ECO:0000269|PubMed:22037183,
CC ECO:0000269|PubMed:3838667}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=36 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:12859184};
CC KM=0.43 uM for glycine {ECO:0000269|PubMed:12859184};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17158459,
CC ECO:0000269|PubMed:22037183}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:6587377}.
CC -!- TISSUE SPECIFICITY: Abundant in liver.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Glycine N-methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00932}.
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; X06150; CAA29508.1; -; mRNA.
DR EMBL; X07833; CAA30686.1; -; Genomic_DNA.
DR PIR; S00112; S00112.
DR RefSeq; NP_058780.1; NM_017084.1.
DR PDB; 1BHJ; X-ray; 2.50 A; A/B=2-293.
DR PDB; 1D2C; X-ray; 2.50 A; A/B=2-293.
DR PDB; 1D2G; X-ray; 2.50 A; A/B=2-293.
DR PDB; 1D2H; X-ray; 3.00 A; A/B/C/D=2-293.
DR PDB; 1KIA; X-ray; 2.80 A; A/B/C/D=2-293.
DR PDB; 1NBH; X-ray; 2.80 A; A/B/C/D=2-293.
DR PDB; 1NBI; X-ray; 3.00 A; A/B/C/D=2-293.
DR PDB; 1XVA; X-ray; 2.20 A; A/B=2-293.
DR PDB; 2IDJ; X-ray; 2.35 A; A/B/C/D=2-293.
DR PDB; 2IDK; X-ray; 2.55 A; A/B/C/D=2-293.
DR PDB; 3THR; X-ray; 2.00 A; A/B/C/D=2-293.
DR PDB; 3THS; X-ray; 2.50 A; A/B/C/D=2-293.
DR PDBsum; 1BHJ; -.
DR PDBsum; 1D2C; -.
DR PDBsum; 1D2G; -.
DR PDBsum; 1D2H; -.
DR PDBsum; 1KIA; -.
DR PDBsum; 1NBH; -.
DR PDBsum; 1NBI; -.
DR PDBsum; 1XVA; -.
DR PDBsum; 2IDJ; -.
DR PDBsum; 2IDK; -.
DR PDBsum; 3THR; -.
DR PDBsum; 3THS; -.
DR AlphaFoldDB; P13255; -.
DR SMR; P13255; -.
DR STRING; 10116.ENSRNOP00000022307; -.
DR iPTMnet; P13255; -.
DR PhosphoSitePlus; P13255; -.
DR PaxDb; P13255; -.
DR PRIDE; P13255; -.
DR Ensembl; ENSRNOT00000022307; ENSRNOP00000022307; ENSRNOG00000016349.
DR GeneID; 25134; -.
DR KEGG; rno:25134; -.
DR UCSC; RGD:2719; rat.
DR CTD; 27232; -.
DR RGD; 2719; Gnmt.
DR eggNOG; ENOG502QRN6; Eukaryota.
DR GeneTree; ENSGT00390000006845; -.
DR HOGENOM; CLU_069129_0_0_1; -.
DR InParanoid; P13255; -.
DR OMA; YALKSRW; -.
DR OrthoDB; 1049906at2759; -.
DR PhylomeDB; P13255; -.
DR TreeFam; TF324814; -.
DR BRENDA; 2.1.1.20; 5301.
DR Reactome; R-RNO-389661; Glyoxylate metabolism and glycine degradation.
DR SABIO-RK; P13255; -.
DR EvolutionaryTrace; P13255; -.
DR PRO; PR:P13255; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000016349; Expressed in liver and 8 other tissues.
DR Genevisible; P13255; RN.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0034708; C:methyltransferase complex; IMP:CAFA.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005542; F:folic acid binding; IDA:UniProtKB.
DR GO; GO:0016594; F:glycine binding; IDA:UniProtKB.
DR GO; GO:0017174; F:glycine N-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:CAFA.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IMP:CAFA.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:RGD.
DR GO; GO:0098603; F:selenol Se-methyltransferase activity; TAS:Reactome.
DR GO; GO:0046655; P:folic acid metabolic process; TAS:RGD.
DR GO; GO:0006544; P:glycine metabolic process; IMP:CAFA.
DR GO; GO:0005977; P:glycogen metabolic process; ISO:RGD.
DR GO; GO:0006555; P:methionine metabolic process; ISO:RGD.
DR GO; GO:0032259; P:methylation; IMP:CAFA.
DR GO; GO:0006730; P:one-carbon metabolic process; ISO:RGD.
DR GO; GO:0051289; P:protein homotetramerization; IPI:UniProtKB.
DR GO; GO:0006111; P:regulation of gluconeogenesis; ISO:RGD.
DR GO; GO:0046498; P:S-adenosylhomocysteine metabolic process; IDA:RGD.
DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; IDA:UniProtKB.
DR GO; GO:1901052; P:sarcosine metabolic process; IMP:RGD.
DR DisProt; DP00031; -.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR014369; Gly/Sar_N_MeTrfase.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR16458; PTHR16458; 1.
DR Pfam; PF13649; Methyltransf_25; 1.
DR PIRSF; PIRSF000385; Gly_N-mtase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51600; SAM_GNMT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Folate-binding; Methyltransferase; Phosphoprotein; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2822402"
FT CHAIN 2..293
FT /note="Glycine N-methyltransferase"
FT /id="PRO_0000087528"
FT BINDING 4
FT /ligand="(6S)-5-methyl-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:18608"
FT /ligand_label="1"
FT /ligand_note="ligand shared between tetrameric partners"
FT /evidence="ECO:0000269|PubMed:22037183,
FT ECO:0000312|PDB:3THR, ECO:0000312|PDB:3THS"
FT BINDING 6
FT /ligand="(6S)-5-methyl-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:18608"
FT /ligand_label="1"
FT /ligand_note="ligand shared between tetrameric partners"
FT /evidence="ECO:0000269|PubMed:17158459,
FT ECO:0000312|PDB:2IDK"
FT BINDING 6
FT /ligand="(6S)-5-methyl-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:18608"
FT /ligand_label="2"
FT /ligand_note="ligand shared between tetrameric partners"
FT /evidence="ECO:0000269|PubMed:22037183,
FT ECO:0000312|PDB:3THS"
FT BINDING 22
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12859184,
FT ECO:0007744|PDB:1NBH"
FT BINDING 31
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12859184,
FT ECO:0007744|PDB:1NBH, ECO:0007744|PDB:1NBI"
FT BINDING 34
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:8810903,
FT ECO:0007744|PDB:1XVA"
FT BINDING 41
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12859184,
FT ECO:0007744|PDB:1NBH, ECO:0007744|PDB:1NBI"
FT BINDING 65
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12859184,
FT ECO:0000269|PubMed:8810903, ECO:0000312|PDB:1XVA,
FT ECO:0007744|PDB:1NBH, ECO:0007744|PDB:1NBI"
FT BINDING 86..88
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12859184,
FT ECO:0007744|PDB:1NBH, ECO:0007744|PDB:1NBI"
FT BINDING 117..118
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12859184,
FT ECO:0007744|PDB:1NBH, ECO:0007744|PDB:1NBI"
FT BINDING 137..140
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12859184,
FT ECO:0000269|PubMed:8810903, ECO:0007744|PDB:1NBI,
FT ECO:0007744|PDB:1XVA"
FT BINDING 176
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:8810903,
FT ECO:0007744|PDB:1XVA"
FT BINDING 215
FT /ligand="(6S)-5-methyl-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:18608"
FT /ligand_label="2"
FT /ligand_note="ligand shared between tetrameric partners"
FT /evidence="ECO:0000269|PubMed:22037183,
FT ECO:0000312|PDB:3THR, ECO:0000312|PDB:3THS"
FT BINDING 221
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:8810903,
FT ECO:0007744|PDB:1XVA"
FT BINDING 240
FT /ligand="(6S)-5-methyl-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:18608"
FT /ligand_label="1"
FT /ligand_note="ligand shared between tetrameric partners"
FT /evidence="ECO:0000269|PubMed:22037183,
FT ECO:0000312|PDB:3THR, ECO:0000312|PDB:3THS"
FT BINDING 240
FT /ligand="(6S)-5-methyl-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:18608"
FT /ligand_label="2"
FT /ligand_note="ligand shared between tetrameric partners"
FT /evidence="ECO:0000269|PubMed:22037183,
FT ECO:0000312|PDB:3THR, ECO:0000312|PDB:3THS"
FT MOD_RES 2
FT /note="N-acetylvaline"
FT /evidence="ECO:0000269|PubMed:2822402"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXF8"
FT MOD_RES 34
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXF8"
FT MOD_RES 46
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXF8"
FT MOD_RES 191
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXF8"
FT MOD_RES 196
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXF8"
FT MOD_RES 201
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXF8"
FT MUTAGEN 34
FT /note="Y->F: Reduces affinity for glycine."
FT /evidence="ECO:0000269|PubMed:12859184"
FT MUTAGEN 176
FT /note="R->K: Strongly reduced affinity for glycine."
FT /evidence="ECO:0000269|PubMed:12859184"
FT MUTAGEN 221
FT /note="Y->F: Reduces affinity for glycine."
FT /evidence="ECO:0000269|PubMed:12859184"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:3THR"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:1NBH"
FT TURN 21..24
FT /evidence="ECO:0007829|PDB:3THR"
FT HELIX 26..35
FT /evidence="ECO:0007829|PDB:3THR"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:2IDJ"
FT HELIX 43..55
FT /evidence="ECO:0007829|PDB:3THR"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:3THR"
FT HELIX 70..77
FT /evidence="ECO:0007829|PDB:3THR"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:3THR"
FT HELIX 89..101
FT /evidence="ECO:0007829|PDB:3THR"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:3THR"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:3THR"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:3THR"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:3THR"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:3THR"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:3THR"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:1NBH"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:3THR"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:3THR"
FT HELIX 152..163
FT /evidence="ECO:0007829|PDB:3THR"
FT STRAND 165..176
FT /evidence="ECO:0007829|PDB:3THR"
FT HELIX 178..184
FT /evidence="ECO:0007829|PDB:3THR"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:3THR"
FT STRAND 202..210
FT /evidence="ECO:0007829|PDB:3THR"
FT STRAND 213..225
FT /evidence="ECO:0007829|PDB:3THR"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:1XVA"
FT STRAND 235..243
FT /evidence="ECO:0007829|PDB:3THR"
FT HELIX 248..257
FT /evidence="ECO:0007829|PDB:3THR"
FT TURN 258..261
FT /evidence="ECO:0007829|PDB:3THR"
FT STRAND 263..269
FT /evidence="ECO:0007829|PDB:3THR"
FT STRAND 283..291
FT /evidence="ECO:0007829|PDB:3THR"
SQ SEQUENCE 293 AA; 32549 MW; 4E98C7512F0228A5 CRC64;
MVDSVYRTRS LGVAAEGIPD QYADGEAARV WQLYIGDTRS RTAEYKAWLL GLLRQHGCHR
VLDVACGTGV DSIMLVEEGF SVTSVDASDK MLKYALKERW NRRKEPAFDK WVIEEANWLT
LDKDVPAGDG FDAVICLGNS FAHLPDSKGD QSEHRLALKN IASMVRPGGL LVIDHRNYDY
ILSTGCAPPG KNIYYKSDLT KDITTSVLTV NNKAHMVTLD YTVQVPGAGR DGAPGFSKFR
LSYYPHCLAS FTELVQEAFG GRCQHSVLGD FKPYRPGQAY VPCYFIHVLK KTG
