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Database: UniProt
Entry: Q99707
LinkDB: Q99707
Original site: Q99707 
ID   METH_HUMAN              Reviewed;        1265 AA.
AC   Q99707; A1L4N8; A9Z1W4; B9EGF7; Q99713; Q99723;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 2.
DT   26-NOV-2014, entry version 153.
DE   RecName: Full=Methionine synthase;
DE            EC=2.1.1.13;
DE   AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase;
DE   AltName: Full=Vitamin-B12 dependent methionine synthase;
DE            Short=MS;
GN   Name=MTR;
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], AND VARIANTS HMAG ILE-881 DEL AND ASP-920.
RC   TISSUE=Fibroblast;
RX   PubMed=8968737; DOI=10.1093/hmg/5.12.1867;
RA   Leclerc D., Campeau E., Goyette P., Adjalla C.E., Christensen B.,
RA   Ross M., Eydoux P., Rosenblatt D.S., Rozen R., Gravel R.A.;
RT   "Human methionine synthase: cDNA cloning and identification of
RT   mutations in patients of the cblG complementation group of
RT   folate/cobalamin disorders.";
RL   Hum. Mol. Genet. 5:1867-1874(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=8968735; DOI=10.1093/hmg/5.12.1851;
RA   Li Y.N., Gulati S., Baker P.J., Brody L.C., Banerjee R., Kruger W.D.;
RT   "Cloning, mapping and RNA analysis of the human methionine synthase
RT   gene.";
RL   Hum. Mol. Genet. 5:1851-1858(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS TYR-255 AND GLY-919.
RC   TISSUE=Fetal liver;
RX   PubMed=9013615; DOI=10.1074/jbc.272.6.3444;
RA   Chen L.H., Liu M.-L., Hwang H.-Y., Chen L.-S., Korenberg J., Shane B.;
RT   "Human methionine synthase. cDNA cloning, gene localization, and
RT   expression.";
RL   J. Biol. Chem. 272:3628-3634(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-919.
RC   TISSUE=Testis;
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).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [8]
RP   VARIANTS HMAG ILE-881 DEL AND LEU-1173, AND VARIANT LYS-61.
RX   PubMed=8968736; DOI=10.1093/hmg/5.12.1859;
RA   Gulati S., Baker P.J., Li Y.N., Fowler B., Kruger W.D., Brody L.C.,
RA   Banerjee R.;
RT   "Defects in human methionine synthase in cblG patients.";
RL   Hum. Mol. Genet. 5:1859-1865(1996).
RN   [9]
RP   ASSOCIATION OF VARIANT GLY-919 WITH SUSCEPTIBILITY TO FS-NTD.
RX   PubMed=12375236; DOI=10.1086/344209;
RA   Doolin M.-T., Barbaux S., McDonnell M., Hoess K., Whitehead A.S.,
RA   Mitchell L.E.;
RT   "Maternal genetic effects, exerted by genes involved in homocysteine
RT   remethylation, influence the risk of spina bifida.";
RL   Am. J. Hum. Genet. 71:1222-1226(2002).
RN   [10]
RP   NO ASSOCIATION OF VARIANT GLY-919 WITH SUSCEPTIBILITY TO FS-NTD.
RX   PubMed=15979034; DOI=10.1016/j.ymgme.2005.02.003;
RA   O'Leary V.B., Mills J.L., Pangilinan F., Kirke P.N., Cox C.,
RA   Conley M., Weiler A., Peng K., Shane B., Scott J.M.,
RA   Parle-McDermott A., Molloy A.M., Brody L.C.;
RT   "Analysis of methionine synthase reductase polymorphisms for neural
RT   tube defects risk association.";
RL   Mol. Genet. Metab. 85:220-227(2005).
CC   -!- FUNCTION: Catalyzes the transfer of a methyl group from methyl-
CC       cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and
CC       methionine. Subsequently, remethylates the cofactor using
CC       methyltetrahydrofolate (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + L-homocysteine =
CC       tetrahydrofolate + L-methionine.
CC   -!- COFACTOR:
CC       Name=methyl(III)cobalamin; Xref=ChEBI:CHEBI:28115;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-methionine from L-homocysteine (MetH route): step
CC       1/1.
CC   -!- INTERACTION:
CC       Q9Y4U1:MMACHC; NbExp=3; IntAct=EBI-1045782, EBI-9775184;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed at the highest
CC       levels in pancreas, heart, brain, skeletal muscle and placenta.
CC       Expressed at lower levels in lung, liver and kidney.
CC   -!- DOMAIN: Modular enzyme with four functionally distinct domains.
CC       The isolated Hcy-binding domain catalyzes methyl transfer from
CC       free methylcobalamin to homocysteine. The Hcy-binding domain in
CC       association with the pterin-binding domain catalyzes the
CC       methylation of cob(I)alamin by methyltetrahydrofolate and the
CC       methylation of homocysteine. The B12-binding domain binds the
CC       cofactor. The AdoMet activation domain binds S-adenosyl-L-
CC       methionine. Under aerobic conditions cob(I)alamin can be converted
CC       to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L-
CC       methionine and flavodoxin regenerates methylcobalamin (By
CC       similarity). {ECO:0000250}.
CC   -!- DISEASE: Homocystinuria-megaloblastic anemia, cblG complementation
CC       type (HMAG) [MIM:250940]: An autosomal recessive inborn error of
CC       metabolism resulting from defects in the cobalamin-dependent
CC       pathway that converts homocysteine to methionine. It causes
CC       delayed psychomotor development, megaloblastic anemia,
CC       homocystinuria, and hypomethioninemia.
CC       {ECO:0000269|PubMed:8968736, ECO:0000269|PubMed:8968737}. Note=The
CC       disease is caused by mutations affecting the gene represented in
CC       this entry.
CC   -!- DISEASE: Folate-sensitive neural tube defects (FS-NTD)
CC       [MIM:601634]: The most common NTDs are open spina bifida
CC       (myelomeningocele) and anencephaly. {ECO:0000269|PubMed:12375236}.
CC       Note=Disease susceptibility is associated with variations
CC       affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: L-homocysteine is bound via the zinc atom.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine
CC       synthase family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 AdoMet activation domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00346}.
CC   -!- SIMILARITY: Contains 1 B12-binding domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00666}.
CC   -!- SIMILARITY: Contains 1 B12-binding N-terminal domain.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00333}.
CC   -!- SIMILARITY: Contains 1 pterin-binding domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00334}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=5-methyltetrahydrofolate-
CC       homocysteine methyltransferase entry;
CC       URL="http://en.wikipedia.org/wiki/5-Methyltetrahydrofolate-homocysteine_methyltransferase";
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DR   EMBL; U71285; AAC51188.1; -; mRNA.
DR   EMBL; U75743; AAB58906.1; -; mRNA.
DR   EMBL; U73338; AAB39704.1; -; mRNA.
DR   EMBL; AL359185; CAH73198.1; -; Genomic_DNA.
DR   EMBL; AL359259; CAH73198.1; JOINED; Genomic_DNA.
DR   EMBL; AL359259; CAH70983.1; -; Genomic_DNA.
DR   EMBL; AL359185; CAH70983.1; JOINED; Genomic_DNA.
DR   EMBL; CH471098; EAW70066.1; -; Genomic_DNA.
DR   EMBL; BC130616; AAI30617.1; -; mRNA.
DR   EMBL; BC136440; AAI36441.1; -; mRNA.
DR   CCDS; CCDS1614.1; -.
DR   RefSeq; NP_000245.2; NM_000254.2.
DR   RefSeq; NP_001278869.1; NM_001291940.1.
DR   UniGene; Hs.498187; -.
DR   PDB; 2O2K; X-ray; 1.60 A; A/B=925-1265.
DR   PDB; 4CCZ; X-ray; 2.70 A; A=16-657.
DR   PDBsum; 2O2K; -.
DR   PDBsum; 4CCZ; -.
DR   ProteinModelPortal; Q99707; -.
DR   SMR; Q99707; 17-651, 665-920, 926-1264.
DR   BioGrid; 110642; 17.
DR   IntAct; Q99707; 3.
DR   STRING; 9606.ENSP00000355536; -.
DR   BindingDB; Q99707; -.
DR   ChEMBL; CHEMBL2150844; -.
DR   DrugBank; DB00115; Cyanocobalamin.
DR   DrugBank; DB00200; Hydroxocobalamin.
DR   DrugBank; DB00134; L-Methionine.
DR   DrugBank; DB00116; Tetrahydrofolic acid.
DR   PhosphoSite; Q99707; -.
DR   DMDM; 2842762; -.
DR   MaxQB; Q99707; -.
DR   PaxDb; Q99707; -.
DR   PRIDE; Q99707; -.
DR   Ensembl; ENST00000366577; ENSP00000355536; ENSG00000116984.
DR   GeneID; 4548; -.
DR   KEGG; hsa:4548; -.
DR   UCSC; uc001hyi.4; human.
DR   CTD; 4548; -.
DR   GeneCards; GC01P236958; -.
DR   GeneReviews; MTR; -.
DR   HGNC; HGNC:7468; MTR.
DR   HPA; HPA044474; -.
DR   MIM; 156570; gene.
DR   MIM; 250940; phenotype.
DR   MIM; 601634; phenotype.
DR   MIM; 603174; phenotype.
DR   neXtProt; NX_Q99707; -.
DR   Orphanet; 2170; Methylcobalamin deficiency type cblG.
DR   PharmGKB; PA31272; -.
DR   eggNOG; COG1410; -.
DR   GeneTree; ENSGT00420000029824; -.
DR   HOGENOM; HOG000251409; -.
DR   HOVERGEN; HBG006347; -.
DR   InParanoid; Q99707; -.
DR   KO; K00548; -.
DR   OMA; KAQPMVT; -.
DR   OrthoDB; EOG7TF786; -.
DR   PhylomeDB; Q99707; -.
DR   TreeFam; TF312829; -.
DR   BioCyc; MetaCyc:HS04076-MONOMER; -.
DR   Reactome; REACT_115639; Sulfur amino acid metabolism.
DR   Reactome; REACT_163862; Cobalamin (Cbl, vitamin B12) transport and metabolism.
DR   Reactome; REACT_169149; Defective MTR causes methylmalonic aciduria and homocystinuria type cblG.
DR   Reactome; REACT_169439; Defective MTRR causes methylmalonic aciduria and homocystinuria type cblE.
DR   Reactome; REACT_6946; Methylation.
DR   UniPathway; UPA00051; UER00081.
DR   ChiTaRS; MTR; human.
DR   EvolutionaryTrace; Q99707; -.
DR   GeneWiki; Methionine_synthase; -.
DR   GenomeRNAi; 4548; -.
DR   NextBio; 17533; -.
DR   PRO; PR:Q99707; -.
DR   Bgee; Q99707; -.
DR   CleanEx; HS_MTR; -.
DR   ExpressionAtlas; Q99707; baseline and differential.
DR   Genevestigator; Q99707; -.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
DR   GO; GO:0009235; P:cobalamin metabolic process; TAS:Reactome.
DR   GO; GO:0032259; P:methylation; TAS:Reactome.
DR   GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR   GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro.
DR   GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR   GO; GO:0000096; P:sulfur amino acid metabolic process; TAS:Reactome.
DR   GO; GO:0006766; P:vitamin metabolic process; TAS:Reactome.
DR   GO; GO:0006767; P:water-soluble vitamin metabolic process; TAS:Reactome.
DR   GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
DR   Gene3D; 1.10.1240.10; -; 1.
DR   Gene3D; 3.10.196.10; -; 1.
DR   Gene3D; 3.20.20.20; -; 1.
DR   Gene3D; 3.20.20.330; -; 1.
DR   Gene3D; 3.40.50.280; -; 1.
DR   InterPro; IPR003759; Cbl-bd_cap.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR011005; Dihydropteroate_synth-like.
DR   InterPro; IPR011822; MetH.
DR   InterPro; IPR000489; Pterin-binding.
DR   InterPro; IPR003726; S_MeTrfase.
DR   InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom.
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; SSF47644; SSF47644; 1.
DR   SUPFAM; SSF51717; SSF51717; 1.
DR   SUPFAM; SSF52242; SSF52242; 1.
DR   SUPFAM; SSF56507; SSF56507; 1.
DR   SUPFAM; SSF82282; SSF82282; 1.
DR   TIGRFAMs; TIGR02082; metH; 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.
PE   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; Cobalamin; Cobalt;
KW   Complete proteome; Cytoplasm; Disease mutation; Metal-binding;
KW   Methionine biosynthesis; Methyltransferase; Polymorphism;
KW   Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase;
KW   Zinc.
FT   CHAIN         1   1265       Methionine synthase.
FT                                /FTId=PRO_0000204530.
FT   DOMAIN       19    338       Hcy-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00333}.
FT   DOMAIN      371    632       Pterin-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00334}.
FT   DOMAIN      662    759       B12-binding N-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00666}.
FT   DOMAIN      772    907       B12-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00666}.
FT   DOMAIN      923   1265       AdoMet activation. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00346}.
FT   REGION      860    861       Cobalamin-binding. {ECO:0000250}.
FT   REGION     1227   1228       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   METAL       260    260       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00333}.
FT   METAL       323    323       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00333}.
FT   METAL       324    324       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00333}.
FT   METAL       785    785       Cobalt (cobalamin axial ligand).
FT                                {ECO:0000250}.
FT   BINDING     830    830       Cobalamin. {ECO:0000250}.
FT   BINDING     974    974       S-adenosyl-L-methionine. {ECO:0000250}.
FT   BINDING    1172   1172       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000250}.
FT   BINDING    1176   1176       Cobalamin; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   VARIANT      52     52       R -> Q (in dbSNP:rs12749581).
FT                                /FTId=VAR_050033.
FT   VARIANT      61     61       R -> K. {ECO:0000269|PubMed:8968736}.
FT                                /FTId=VAR_004326.
FT   VARIANT     255    255       C -> Y. {ECO:0000269|PubMed:9013615}.
FT                                /FTId=VAR_004327.
FT   VARIANT     314    314       D -> N (in dbSNP:rs2229274).
FT                                /FTId=VAR_061338.
FT   VARIANT     881    881       Missing (in HMAG).
FT                                {ECO:0000269|PubMed:8968736,
FT                                ECO:0000269|PubMed:8968737}.
FT                                /FTId=VAR_004328.
FT   VARIANT     919    919       D -> G (may be associated with
FT                                susceptibility to FS-NTD;
FT                                dbSNP:rs1805087).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:9013615}.
FT                                /FTId=VAR_004329.
FT   VARIANT     920    920       H -> D (in HMAG; dbSNP:rs28933097).
FT                                {ECO:0000269|PubMed:8968737}.
FT                                /FTId=VAR_004330.
FT   VARIANT    1173   1173       P -> L (in HMAG).
FT                                {ECO:0000269|PubMed:8968736}.
FT                                /FTId=VAR_004331.
FT   HELIX        18     28       {ECO:0000244|PDB:4CCZ}.
FT   HELIX        37     44       {ECO:0000244|PDB:4CCZ}.
FT   HELIX        49     51       {ECO:0000244|PDB:4CCZ}.
FT   HELIX        67     69       {ECO:0000244|PDB:4CCZ}.
FT   HELIX        70     73       {ECO:0000244|PDB:4CCZ}.
FT   HELIX        75     87       {ECO:0000244|PDB:4CCZ}.
FT   STRAND       92     94       {ECO:0000244|PDB:4CCZ}.
FT   HELIX       102    105       {ECO:0000244|PDB:4CCZ}.
FT   HELIX       106    108       {ECO:0000244|PDB:4CCZ}.
FT   HELIX       111    113       {ECO:0000244|PDB:4CCZ}.
FT   HELIX       114    136       {ECO:0000244|PDB:4CCZ}.
FT   STRAND      141    146       {ECO:0000244|PDB:4CCZ}.
FT   STRAND      153    155       {ECO:0000244|PDB:4CCZ}.
FT   STRAND      159    161       {ECO:0000244|PDB:4CCZ}.
FT   HELIX       169    185       {ECO:0000244|PDB:4CCZ}.
FT   STRAND      189    198       {ECO:0000244|PDB:4CCZ}.
FT   HELIX       199    213       {ECO:0000244|PDB:4CCZ}.
FT   TURN        214    216       {ECO:0000244|PDB:4CCZ}.
FT   STRAND      222    226       {ECO:0000244|PDB:4CCZ}.
FT   HELIX       241    248       {ECO:0000244|PDB:4CCZ}.
FT   HELIX       249    251       {ECO:0000244|PDB:4CCZ}.
FT   STRAND      254    263       {ECO:0000244|PDB:4CCZ}.
FT   TURN        264    267       {ECO:0000244|PDB:4CCZ}.
FT   HELIX       268    275       {ECO:0000244|PDB:4CCZ}.
FT   STRAND      279    287       {ECO:0000244|PDB:4CCZ}.
FT   STRAND      318    320       {ECO:0000244|PDB:4CCZ}.
FT   HELIX       328    338       {ECO:0000244|PDB:4CCZ}.
FT   TURN        348    353       {ECO:0000244|PDB:4CCZ}.
FT   STRAND      355    365       {ECO:0000244|PDB:4CCZ}.
FT   STRAND      372    375       {ECO:0000244|PDB:4CCZ}.
FT   TURN        380    382       {ECO:0000244|PDB:4CCZ}.
FT   HELIX       384    391       {ECO:0000244|PDB:4CCZ}.
FT   HELIX       395    407       {ECO:0000244|PDB:4CCZ}.
FT   STRAND      411    416       {ECO:0000244|PDB:4CCZ}.
FT   HELIX       424    437       {ECO:0000244|PDB:4CCZ}.
FT   HELIX       439    442       {ECO:0000244|PDB:4CCZ}.
FT   STRAND      446    449       {ECO:0000244|PDB:4CCZ}.
FT   HELIX       453    462       {ECO:0000244|PDB:4CCZ}.
FT   STRAND      468    472       {ECO:0000244|PDB:4CCZ}.
FT   HELIX       478    491       {ECO:0000244|PDB:4CCZ}.
FT   STRAND      494    501       {ECO:0000244|PDB:4CCZ}.
FT   HELIX       509    527       {ECO:0000244|PDB:4CCZ}.
FT   HELIX       531    533       {ECO:0000244|PDB:4CCZ}.
FT   STRAND      534    537       {ECO:0000244|PDB:4CCZ}.
FT   HELIX       548    552       {ECO:0000244|PDB:4CCZ}.
FT   HELIX       553    567       {ECO:0000244|PDB:4CCZ}.
FT   HELIX       577    584       {ECO:0000244|PDB:4CCZ}.
FT   HELIX       588    605       {ECO:0000244|PDB:4CCZ}.
FT   STRAND      609    612       {ECO:0000244|PDB:4CCZ}.
FT   HELIX       620    622       {ECO:0000244|PDB:4CCZ}.
FT   HELIX       625    635       {ECO:0000244|PDB:4CCZ}.
FT   HELIX       642    648       {ECO:0000244|PDB:4CCZ}.
FT   HELIX       932    937       {ECO:0000244|PDB:2O2K}.
FT   HELIX       944    946       {ECO:0000244|PDB:2O2K}.
FT   STRAND      956    962       {ECO:0000244|PDB:2O2K}.
FT   HELIX       966    970       {ECO:0000244|PDB:2O2K}.
FT   HELIX       976    987       {ECO:0000244|PDB:2O2K}.
FT   HELIX       995    998       {ECO:0000244|PDB:2O2K}.
FT   HELIX      1005   1022       {ECO:0000244|PDB:2O2K}.
FT   STRAND     1026   1040       {ECO:0000244|PDB:2O2K}.
FT   STRAND     1043   1046       {ECO:0000244|PDB:2O2K}.
FT   HELIX      1053   1055       {ECO:0000244|PDB:2O2K}.
FT   STRAND     1059   1063       {ECO:0000244|PDB:2O2K}.
FT   HELIX      1082   1085       {ECO:0000244|PDB:2O2K}.
FT   HELIX      1089   1091       {ECO:0000244|PDB:2O2K}.
FT   STRAND     1095   1106       {ECO:0000244|PDB:2O2K}.
FT   HELIX      1107   1116       {ECO:0000244|PDB:2O2K}.
FT   HELIX      1120   1147       {ECO:0000244|PDB:2O2K}.
FT   TURN       1152   1155       {ECO:0000244|PDB:2O2K}.
FT   HELIX      1160   1164       {ECO:0000244|PDB:2O2K}.
FT   STRAND     1168   1171       {ECO:0000244|PDB:2O2K}.
FT   HELIX      1185   1192       {ECO:0000244|PDB:2O2K}.
FT   HELIX      1195   1199       {ECO:0000244|PDB:2O2K}.
FT   STRAND     1209   1220       {ECO:0000244|PDB:2O2K}.
FT   HELIX      1235   1245       {ECO:0000244|PDB:2O2K}.
FT   HELIX      1249   1255       {ECO:0000244|PDB:2O2K}.
FT   HELIX      1257   1259       {ECO:0000244|PDB:2O2K}.
SQ   SEQUENCE   1265 AA;  140527 MW;  B04C26BCBE9A57C2 CRC64;
     MSPALQDLSQ PEGLKKTLRD EINAILQKRI MVLDGGMGTM IQREKLNEEH FRGQEFKDHA
     RPLKGNNDIL SITQPDVIYQ IHKEYLLAGA DIIETNTFSS TSIAQADYGL EHLAYRMNMC
     SAGVARKAAE EVTLQTGIKR FVAGALGPTN KTLSVSPSVE RPDYRNITFD ELVEAYQEQA
     KGLLDGGVDI LLIETIFDTA NAKAALFALQ NLFEEKYAPR PIFISGTIVD KSGRTLSGQT
     GEGFVISVSH GEPLCIGLNC ALGAAEMRPF IEIIGKCTTA YVLCYPNAGL PNTFGDYDET
     PSMMAKHLKD FAMDGLVNIV GGCCGSTPDH IREIAEAVKN CKPRVPPATA FEGHMLLSGL
     EPFRIGPYTN FVNIGERCNV AGSRKFAKLI MAGNYEEALC VAKVQVEMGA QVLDVNMDDG
     MLDGPSAMTR FCNLIASEPD IAKVPLCIDS SNFAVIEAGL KCCQGKCIVN SISLKEGEDD
     FLEKARKIKK YGAAMVVMAF DEEGQATETD TKIRVCTRAY HLLVKKLGFN PNDIIFDPNI
     LTIGTGMEEH NLYAINFIHA TKVIKETLPG ARISGGLSNL SFSFRGMEAI REAMHGVFLY
     HAIKSGMDMG IVNAGNLPVY DDIHKELLQL CEDLIWNKDP EATEKLLRYA QTQGTGGKKV
     IQTDEWRNGP VEERLEYALV KGIEKHIIED TEEARLNQKK YPRPLNIIEG PLMNGMKIVG
     DLFGAGKMFL PQVIKSARVM KKAVGHLIPF MEKEREETRV LNGTVEEEDP YQGTIVLATV
     KGDVHDIGKN IVGVVLGCNN FRVIDLGVMT PCDKILKAAL DHKADIIGLS GLITPSLDEM
     IFVAKEMERL AIRIPLLIGG ATTSKTHTAV KIAPRYSAPV IHVLDASKSV VVCSQLLDEN
     LKDEYFEEIM EEYEDIRQDH YESLKERRYL PLSQARKSGF QMDWLSEPHP VKPTFIGTQV
     FEDYDLQKLV DYIDWKPFFD VWQLRGKYPN RGFPKIFNDK TVGGEARKVY DDAHNMLNTL
     ISQKKLRARG VVGFWPAQSI QDDIHLYAEA AVPQAAEPIA TFYGLRQQAE KDSASTEPYY
     CLSDFIAPLH SGIRDYLGLF AVACFGVEEL SKAYEDDGDD YSSIMVKALG DRLAEAFAEE
     LHERVRRELW AYCGSEQLDV ADLRRLRYKG IRPAPGYPSQ PDHTEKLTMW RLADIEQSTG
     IRLTESLAMA PASAVSGLYF SNLKSKYFAV GKISKDQVED YALRKNISVA EVEKWLGPIL
     GYDTD
//
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