ID   METH_MOUSE              Reviewed;        1253 AA.
AC   A6H5Y3; Q3UQP2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=Methionine synthase;
DE            Short=MS;
DE            EC=2.1.1.13 {ECO:0000250|UniProtKB:Q9Z2Q4};
DE   AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase;
DE   AltName: Full=Cobalamin-dependent methionine synthase;
DE   AltName: Full=Vitamin-B12 dependent methionine synthase;
GN   Name=Mtr {ECO:0000312|MGI:MGI:894292};
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 [LARGE SCALE MRNA].
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-738.
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Lung, Pancreas, Spleen, and Testis;
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).
CC   -!- FUNCTION: Catalyzes the transfer of a methyl group from
CC       methylcob(III)alamin (MeCbl) to homocysteine, yielding enzyme-bound
CC       cob(I)alamin and methionine in the cytosol. MeCbl is an active form of
CC       cobalamin (vitamin B12) used as a cofactor for methionine biosynthesis.
CC       Cob(I)alamin form is regenerated to MeCbl by a transfer of a methyl
CC       group from 5-methyltetrahydrofolate. The processing of cobalamin in the
CC       cytosol occurs in a multiprotein complex composed of at least MMACHC,
CC       MMADHC, MTRR (methionine synthase reductase) and MTR which may
CC       contribute to shuttle safely and efficiently cobalamin towards MTR in
CC       order to produce methionine. {ECO:0000250|UniProtKB:Q99707}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + L-homocysteine =
CC         (6S)-5,6,7,8-tetrahydrofolate + L-methionine; Xref=Rhea:RHEA:11172,
CC         ChEBI:CHEBI:18608, ChEBI:CHEBI:57453, ChEBI:CHEBI:57844,
CC         ChEBI:CHEBI:58199; EC=2.1.1.13;
CC         Evidence={ECO:0000250|UniProtKB:Q9Z2Q4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11173;
CC         Evidence={ECO:0000250|UniProtKB:Q9Z2Q4};
CC   -!- COFACTOR:
CC       Name=methylcob(III)alamin; Xref=ChEBI:CHEBI:28115;
CC         Evidence={ECO:0000250|UniProtKB:P13009};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P13009};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P13009};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; L-methionine from L-homocysteine (MetH route): step 1/1.
CC       {ECO:0000250|UniProtKB:Q9Z2Q4}.
CC   -!- SUBUNIT: Monomer. Dimer. Forms a multiprotein complex with MMACHC,
CC       MMADHC and MTRR. {ECO:0000250|UniProtKB:Q99707}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99707}.
CC   -!- DOMAIN: Modular enzyme with four functionally distinct domains. The
CC       isolated Hcy-binding domain catalyzes methyl transfer from free
CC       methylcobalamin to homocysteine. The Hcy-binding domain in association
CC       with the pterin-binding domain catalyzes the methylation of
CC       cob(I)alamin by methyltetrahydrofolate and the methylation of
CC       homocysteine. The B12-binding domain binds the cofactor. The AdoMet
CC       activation domain binds S-adenosyl-L-methionine. Under aerobic
CC       conditions cob(I)alamin can be converted to inactive cob(II)alamin.
CC       Reductive methylation by S-adenosyl-L-methionine and flavodoxin
CC       regenerates methylcobalamin (By similarity).
CC       {ECO:0000250|UniProtKB:P13009}.
CC   -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine synthase
CC       family. {ECO:0000305}.
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DR   EMBL; BC145683; AAI45684.1; -; mRNA.
DR   EMBL; BC145685; AAI45686.1; -; mRNA.
DR   EMBL; AK142258; BAE24997.1; -; mRNA.
DR   CCDS; CCDS36591.1; -.
DR   RefSeq; NP_001074597.1; NM_001081128.3.
DR   AlphaFoldDB; A6H5Y3; -.
DR   SMR; A6H5Y3; -.
DR   BioGRID; 231991; 5.
DR   IntAct; A6H5Y3; 1.
DR   MINT; A6H5Y3; -.
DR   STRING; 10090.ENSMUSP00000097442; -.
DR   ChEMBL; CHEMBL3188; -.
DR   iPTMnet; A6H5Y3; -.
DR   PhosphoSitePlus; A6H5Y3; -.
DR   SwissPalm; A6H5Y3; -.
DR   EPD; A6H5Y3; -.
DR   MaxQB; A6H5Y3; -.
DR   PaxDb; 10090-ENSMUSP00000097442; -.
DR   PeptideAtlas; A6H5Y3; -.
DR   ProteomicsDB; 252541; -.
DR   Pumba; A6H5Y3; -.
DR   Antibodypedia; 20817; 175 antibodies from 30 providers.
DR   Ensembl; ENSMUST00000099856.6; ENSMUSP00000097442.5; ENSMUSG00000021311.10.
DR   GeneID; 238505; -.
DR   KEGG; mmu:238505; -.
DR   UCSC; uc007plh.2; mouse.
DR   AGR; MGI:894292; -.
DR   CTD; 4548; -.
DR   MGI; MGI:894292; Mtr.
DR   VEuPathDB; HostDB:ENSMUSG00000021311; -.
DR   eggNOG; KOG1579; Eukaryota.
DR   GeneTree; ENSGT00420000029824; -.
DR   HOGENOM; CLU_004914_2_0_1; -.
DR   InParanoid; A6H5Y3; -.
DR   OMA; ADCIAMS; -.
DR   OrthoDB; 66796at2759; -.
DR   PhylomeDB; A6H5Y3; -.
DR   TreeFam; TF312829; -.
DR   Reactome; R-MMU-156581; Methylation.
DR   Reactome; R-MMU-1614635; Sulfur amino acid metabolism.
DR   Reactome; R-MMU-9013407; RHOH GTPase cycle.
DR   Reactome; R-MMU-9759218; Cobalamin (Cbl) metabolism.
DR   UniPathway; UPA00051; UER00081.
DR   BioGRID-ORCS; 238505; 18 hits in 79 CRISPR screens.
DR   ChiTaRS; Mtr; mouse.
DR   PRO; PR:A6H5Y3; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; A6H5Y3; Protein.
DR   Bgee; ENSMUSG00000021311; Expressed in myocardium of ventricle and 227 other cell types or tissues.
DR   ExpressionAtlas; A6H5Y3; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0016597; F:amino acid binding; ISO:MGI.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005542; F:folic acid binding; ISO:MGI.
DR   GO; GO:0008705; F:methionine synthase activity; IMP:MGI.
DR   GO; GO:0008168; F:methyltransferase activity; ISO:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0031103; P:axon regeneration; ISO:MGI.
DR   GO; GO:0071732; P:cellular response to nitric oxide; ISO:MGI.
DR   GO; GO:0009235; P:cobalamin metabolic process; IMP:MGI.
DR   GO; GO:0050667; P:homocysteine metabolic process; ISO:MGI.
DR   GO; GO:0009086; P:methionine biosynthetic process; IMP:MGI.
DR   GO; GO:0006555; P:methionine metabolic process; ISO:MGI.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0048678; P:response to axon injury; ISO:MGI.
DR   GO; GO:0046653; P:tetrahydrofolate metabolic process; ISO:MGI.
DR   CDD; cd02069; methionine_synthase_B12_BD; 1.
DR   CDD; cd00740; MeTr; 1.
DR   Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR   Gene3D; 1.10.288.10; Cobalamin-dependent Methionine Synthase, domain 2; 1.
DR   Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 1.
DR   Gene3D; 3.20.20.330; Homocysteine-binding-like domain; 1.
DR   Gene3D; 1.10.1240.10; Methionine synthase domain; 1.
DR   Gene3D; 3.10.196.10; Vitamin B12-dependent methionine synthase, activation domain; 1.
DR   InterPro; IPR003759; Cbl-bd_cap.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR036724; Cobalamin-bd_sf.
DR   InterPro; IPR011005; Dihydropteroate_synth-like_sf.
DR   InterPro; IPR003726; HCY_dom.
DR   InterPro; IPR036589; HCY_dom_sf.
DR   InterPro; IPR033706; Met_synthase_B12-bd.
DR   InterPro; IPR011822; MetH.
DR   InterPro; IPR036594; Meth_synthase_dom.
DR   InterPro; IPR000489; Pterin-binding_dom.
DR   InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom.
DR   InterPro; IPR037010; VitB12-dep_Met_synth_activ_sf.
DR   NCBIfam; TIGR02082; metH; 1.
DR   PANTHER; PTHR45833; METHIONINE SYNTHASE; 1.
DR   PANTHER; PTHR45833:SF1; METHIONINE SYNTHASE; 1.
DR   Pfam; PF02310; B12-binding; 1.
DR   Pfam; PF02607; B12-binding_2; 1.
DR   Pfam; PF02965; Met_synt_B12; 1.
DR   Pfam; PF00809; Pterin_bind; 1.
DR   Pfam; PF02574; S-methyl_trans; 1.
DR   PIRSF; PIRSF000381; MetH; 1.
DR   SMART; SM01018; B12-binding_2; 1.
DR   SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR   SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1.
DR   SUPFAM; SSF82282; Homocysteine S-methyltransferase; 1.
DR   SUPFAM; SSF56507; Methionine synthase activation domain-like; 1.
DR   SUPFAM; SSF47644; Methionine synthase domain; 1.
DR   PROSITE; PS50974; ADOMET_ACTIVATION; 1.
DR   PROSITE; PS51332; B12_BINDING; 1.
DR   PROSITE; PS51337; B12_BINDING_NTER; 1.
DR   PROSITE; PS50970; HCY; 1.
DR   PROSITE; PS50972; PTERIN_BINDING; 1.
DR   Genevisible; A6H5Y3; MM.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Cobalamin; Cobalt; Cytoplasm; Metal-binding;
KW   Methionine biosynthesis; Methyltransferase; Phosphoprotein;
KW   Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase; Zinc.
FT   CHAIN           1..1253
FT                   /note="Methionine synthase"
FT                   /id="PRO_0000312901"
FT   DOMAIN          6..326
FT                   /note="Hcy-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT   DOMAIN          359..620
FT                   /note="Pterin-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00334"
FT   DOMAIN          650..747
FT                   /note="B12-binding N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00667"
FT   DOMAIN          760..895
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00666"
FT   DOMAIN          911..1253
FT                   /note="AdoMet activation"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00346"
FT   BINDING         248
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT   BINDING         311
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT   BINDING         312
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT   BINDING         370..372
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000250|UniProtKB:Q99707"
FT   BINDING         437
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000250|UniProtKB:Q99707"
FT   BINDING         458
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000250|UniProtKB:Q99707"
FT   BINDING         525
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000250|UniProtKB:Q99707"
FT   BINDING         567
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000250|UniProtKB:Q99707"
FT   BINDING         573
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000250|UniProtKB:Q99707"
FT   BINDING         579
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000250|UniProtKB:Q99707"
FT   BINDING         697
FT                   /ligand="methylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:28115"
FT                   /evidence="ECO:0000250|UniProtKB:P13009"
FT   BINDING         770..774
FT                   /ligand="methylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:28115"
FT                   /evidence="ECO:0000250|UniProtKB:P13009"
FT   BINDING         773
FT                   /ligand="methylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:28115"
FT                   /ligand_part="Co"
FT                   /ligand_part_id="ChEBI:CHEBI:27638"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P13009"
FT   BINDING         818
FT                   /ligand="methylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:28115"
FT                   /evidence="ECO:0000250|UniProtKB:P13009"
FT   BINDING         822
FT                   /ligand="methylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:28115"
FT                   /evidence="ECO:0000250|UniProtKB:P13009"
FT   BINDING         874
FT                   /ligand="methylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:28115"
FT                   /evidence="ECO:0000250|UniProtKB:P13009"
FT   BINDING         962
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P13009"
FT   BINDING         1160
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P13009"
FT   BINDING         1215..1216
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P13009"
FT   MOD_RES         1252
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z2Q4"
FT   CONFLICT        343
FT                   /note="M -> L (in Ref. 2; BAE24997)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1253 AA;  139069 MW;  5507CAD9F9522537 CRC64;
     MKKTLQDEIE AILRKRIMVL DGGMGTMIQR YKLSEEHFQG QEFKDHSRPL KGNNDILSIT
     QPDIIYQIHK EYLLAGADII ETNTFSSTSI AQADYGLEHL AYRMNKCSAD VARKAAEEIT
     LQTGVKRFVA GALGPTNKTL SVSPSVERPD YRNITFDELV DAYQEQAKGL LDGRVDILLI
     ETIFDTANAK AALFAIQNLF EENYAPPRPI FISGTIVDKS GRTLSGQTGE AFVTSVSHSD
     PLCIGLNCSL GAAEMRPFIE TIGKCTTAYV LCYPNAGLPN TFGDYDETPS TMATHLKDFA
     VDGLVNIVGG CCGSTPDHIR EIAEAVKKCK PRVPPASVFE GHMLLSGLEP FRIGPYTNFV
     NIGERCNVAG SRKFAKLIMA GNYEEALSIA KAQVEMGAQV LDINMDDGML DGPSAMTRFC
     NSIASEPDIA KVPLCIDSSN FAVIEAGLKC CQGKCIVNSI SLKEGEGDFL EKARKIKKFG
     AAVVVMAFDE EGQATETDVK VNVCTRAYHL LVDKVGFNPN DIIFDPNILT IGTGMEEHNL
     YAINFIHATR VIKETLPGVR ISGGLSNLSF SFRGMEAIRE AMHGVFLYHA IKFGMDMGIV
     NAGNLPVYDA IHKDLLQLCE DLIWNKDSEA TEKLLRYAQT HGTGGKKVIQ TDEWRNGSIE
     ERLEYALVKG IEKHIVEDTE EARLNGEKYP RPLNIIEGPL MNGMKVVGDL FGAGKMFLPQ
     VIKSARVMKK AVGHLIPFME KEREEARLIN GSVEEEDPYQ GTIVLATVKG DVHDIGKNIV
     GVVLACNNFR VIDLGVMTPC DKILQAALDH KADIIGLSGL ITPSLDEMIF VAKEMERLAI
     KIPLLIGGAT TSRTHTAVKI APRYSAPVIH VLDASKSVVV CSQLLDENLR DDYFEEILEE
     YEDIRQDHYE SLKERKYVPL SQARKHGFHI DWLSEPHPVK PTFIGTQVFE DYNLQKLVDY
     IDWKPFFDVW QLRGKYPNRG FPKIFNDKAV GEEARKVYND AQNMLNILIS QKKLQARGVV
     GFWPAQSVQD DIHLYAEGVV PQAAEPIATF YGLRQQAEKD SSSTDPYHCL SDFIAPLHSG
     VCDYLGLFAV ACFGVEELSK TYEDDGDDYS SIMVKALGDR LAEAFAEELH ERVRRELWAY
     SRSEQLGVPD LRRLRYEGIR PAPGYPSQPD HTEKLTMWRL ASIEQATGIR LTESLAMAPA
     SAVSGLYFSN VKAKYFAVGK ISKDQTEDYA LRKNMPVAEV EKWLGPILGY DTD
//