METK1_HUMAN
ID METK1_HUMAN Reviewed; 395 AA.
AC Q00266; D3DWD5; Q5QP09;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=S-adenosylmethionine synthase isoform type-1;
DE Short=AdoMet synthase 1;
DE EC=2.5.1.6 {ECO:0000269|PubMed:10677294};
DE AltName: Full=Methionine adenosyltransferase 1;
DE Short=MAT 1;
DE AltName: Full=Methionine adenosyltransferase I/III;
DE Short=MAT-I/III;
GN Name=MAT1A; Synonyms=AMS1, MATA1;
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], AND TISSUE SPECIFICITY.
RX PubMed=8393662; DOI=10.1042/bj2930481;
RA Alvarez L., Corrales F., Mato J.M.;
RT "Characterization of a full-length cDNA encoding human liver S-
RT adenosylmethionine synthetase: tissue-specific gene expression and mRNA
RT levels in hepatopathies.";
RL Biochem. J. 293:481-486(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=1772450;
RA Horikawa S., Tsukada K.;
RT "Molecular cloning and nucleotide sequence of cDNA encoding the human liver
RT S-adenosylmethionine synthetase.";
RL Biochem. Int. 25:81-90(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
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 [6]
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., Buerckstuemmer T.,
RA 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 14-395 IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE, AND SUBUNIT.
RX PubMed=23425511; DOI=10.1042/bj20121580;
RA Shafqat N., Muniz J.R., Pilka E.S., Papagrigoriou E., von Delft F.,
RA Oppermann U., Yue W.W.;
RT "Insight into S-adenosylmethionine biosynthesis from the crystal structures
RT of the human methionine adenosyltransferase catalytic and regulatory
RT subunits.";
RL Biochem. J. 452:27-36(2013).
RN [9]
RP VARIANTS MATD ASP-55; PRO-305; MET-322 AND LEU-357.
RX PubMed=7560086; DOI=10.1172/jci118240;
RA Ubagai T., Lei K.-J., Huang S., Mudd S.H., Levy H.L., Chou J.Y.;
RT "Molecular mechanisms of an inborn error of methionine pathway. Methionine
RT adenosyltransferase deficiency.";
RL J. Clin. Invest. 96:1943-1947(1995).
RN [10]
RP VARIANTS MATD CYS-199; GLN-356 AND SER-378.
RX PubMed=8770875; DOI=10.1172/jci118862;
RA Chamberlin M.E., Ubagai T., Mudd S.H., Wilson W.G., Leonard J.V.,
RA Chou J.Y.;
RT "Demyelination of the brain is associated with methionine
RT adenosyltransferase I/III deficiency.";
RL J. Clin. Invest. 98:1021-1027(1996).
RN [11]
RP VARIANT MATD HIS-264.
RX PubMed=9042912;
RA Chamberlin M.E., Ubagai T., Mudd S.H., Levy H.L., Chou J.Y.;
RT "Dominant inheritance of isolated hypermethioninemia is associated with a
RT mutation in the human methionine adenosyltransferase 1A gene.";
RL Am. J. Hum. Genet. 60:540-546(1997).
RN [12]
RP VARIANTS MATD ASN-38; CYS-264; HIS-264; MET-322; ARG-336 AND ALA-344,
RP CHARACTERIZATION OF VARIANTS MATD ASN-38; CYS-264; HIS-264; MET-322;
RP ARG-336 AND ALA-344, CATALYTIC ACTIVITY, FUNCTION, AND PATHWAY.
RX PubMed=10677294; DOI=10.1086/302752;
RA Chamberlin M.E., Ubagai T., Mudd S.H., Thomas J., Pao V.Y., Nguyen T.K.,
RA Levy H.L., Greene C., Freehauf C., Chou J.Y.;
RT "Methionine adenosyltransferase I/III deficiency: novel mutations and
RT clinical variations.";
RL Am. J. Hum. Genet. 66:347-355(2000).
CC -!- FUNCTION: Catalyzes the formation of S-adenosylmethionine from
CC methionine and ATP. The reaction comprises two steps that are both
CC catalyzed by the same enzyme: formation of S-adenosylmethionine
CC (AdoMet) and triphosphate, and subsequent hydrolysis of the
CC triphosphate. {ECO:0000269|PubMed:10677294}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-
CC adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6;
CC Evidence={ECO:0000269|PubMed:10677294};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P13444};
CC Note=Binds 2 magnesium ions per subunit. The magnesium ions interact
CC primarily with the substrate. {ECO:0000250|UniProtKB:P13444};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000250|UniProtKB:P13444};
CC Note=Binds 1 potassium ion per subunit. The potassium ion interacts
CC primarily with the substrate. {ECO:0000250|UniProtKB:P13444};
CC -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis;
CC S-adenosyl-L-methionine from L-methionine: step 1/1.
CC {ECO:0000269|PubMed:10677294}.
CC -!- SUBUNIT: Homotetramer (MAT-I); dimer of dimers (PubMed:23425511).
CC Homodimer (MAT-III) (By similarity). {ECO:0000250|UniProtKB:P13444,
CC ECO:0000269|PubMed:23425511}.
CC -!- INTERACTION:
CC Q00266; P05067: APP; NbExp=3; IntAct=EBI-967087, EBI-77613;
CC Q00266; P42858: HTT; NbExp=3; IntAct=EBI-967087, EBI-466029;
CC Q00266; Q00266: MAT1A; NbExp=4; IntAct=EBI-967087, EBI-967087;
CC Q00266; P31153: MAT2A; NbExp=7; IntAct=EBI-967087, EBI-1050743;
CC -!- TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:8393662}.
CC -!- PTM: S-nitrosylation of Cys-120 inactivates the enzyme.
CC {ECO:0000250|UniProtKB:P13444}.
CC -!- PTM: An intrachain disulfide bond can be formed. The protein structure
CC shows that the relevant Cys residues are in a position that would
CC permit formation of a disulfide bond. {ECO:0000250|UniProtKB:P13444}.
CC -!- DISEASE: Methionine adenosyltransferase deficiency (MATD) [MIM:250850]:
CC An inborn error of metabolism resulting in isolated hypermethioninemia.
CC Most patients have no clinical abnormalities, although some neurologic
CC symptoms may be present in rare cases with severe loss of methionine
CC adenosyltransferase activity. {ECO:0000269|PubMed:10677294,
CC ECO:0000269|PubMed:7560086, ECO:0000269|PubMed:8770875,
CC ECO:0000269|PubMed:9042912}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the AdoMet synthase family. {ECO:0000305}.
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DR EMBL; D49357; BAA08355.1; -; mRNA.
DR EMBL; X69078; CAA48822.1; -; mRNA.
DR EMBL; AL359195; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471142; EAW80396.1; -; Genomic_DNA.
DR EMBL; CH471142; EAW80397.1; -; Genomic_DNA.
DR EMBL; BC018359; AAH18359.1; -; mRNA.
DR CCDS; CCDS7365.1; -.
DR PIR; S27363; S27363.
DR RefSeq; NP_000420.1; NM_000429.2.
DR RefSeq; XP_005269899.1; XM_005269842.4.
DR PDB; 2OBV; X-ray; 2.05 A; A=16-395.
DR PDB; 6SW5; X-ray; 2.35 A; A/B/C/D=1-395.
DR PDB; 6SW6; X-ray; 2.85 A; A/B=1-395.
DR PDBsum; 2OBV; -.
DR PDBsum; 6SW5; -.
DR PDBsum; 6SW6; -.
DR AlphaFoldDB; Q00266; -.
DR SMR; Q00266; -.
DR BioGRID; 110313; 20.
DR ComplexPortal; CPX-3168; Methionine adenosyltransferase complex variant 1.
DR ComplexPortal; CPX-3169; Methionine adenosyltransferase complex variant 3.
DR CORUM; Q00266; -.
DR IntAct; Q00266; 5.
DR STRING; 9606.ENSP00000361287; -.
DR DrugBank; DB03191; 3-Oxiran-2ylalanine.
DR DrugBank; DB00118; Ademetionine.
DR DrugBank; DB03611; L-2-amino-4-methoxy-cis-but-3-enoic acid.
DR DrugBank; DB00134; Methionine.
DR iPTMnet; Q00266; -.
DR PhosphoSitePlus; Q00266; -.
DR BioMuta; MAT1A; -.
DR DMDM; 417297; -.
DR EPD; Q00266; -.
DR jPOST; Q00266; -.
DR MassIVE; Q00266; -.
DR MaxQB; Q00266; -.
DR PaxDb; Q00266; -.
DR PeptideAtlas; Q00266; -.
DR PRIDE; Q00266; -.
DR ProteomicsDB; 57842; -.
DR Antibodypedia; 29977; 259 antibodies from 33 providers.
DR DNASU; 4143; -.
DR Ensembl; ENST00000372213.8; ENSP00000361287.3; ENSG00000151224.13.
DR GeneID; 4143; -.
DR KEGG; hsa:4143; -.
DR MANE-Select; ENST00000372213.8; ENSP00000361287.3; NM_000429.3; NP_000420.1.
DR UCSC; uc001kbw.4; human.
DR CTD; 4143; -.
DR DisGeNET; 4143; -.
DR GeneCards; MAT1A; -.
DR HGNC; HGNC:6903; MAT1A.
DR HPA; ENSG00000151224; Tissue enriched (liver).
DR MalaCards; MAT1A; -.
DR MIM; 250850; phenotype.
DR MIM; 610550; gene.
DR neXtProt; NX_Q00266; -.
DR OpenTargets; ENSG00000151224; -.
DR Orphanet; 168598; Brain demyelination due to methionine adenosyltransferase deficiency.
DR PharmGKB; PA30646; -.
DR VEuPathDB; HostDB:ENSG00000151224; -.
DR eggNOG; KOG1506; Eukaryota.
DR GeneTree; ENSGT00950000183185; -.
DR HOGENOM; CLU_041802_0_1_1; -.
DR InParanoid; Q00266; -.
DR OMA; INPTGRY; -.
DR OrthoDB; 685006at2759; -.
DR PhylomeDB; Q00266; -.
DR TreeFam; TF300511; -.
DR BioCyc; MetaCyc:HS07715-MON; -.
DR BRENDA; 2.5.1.6; 2681.
DR PathwayCommons; Q00266; -.
DR Reactome; R-HSA-156581; Methylation.
DR Reactome; R-HSA-1614635; Sulfur amino acid metabolism.
DR Reactome; R-HSA-2408508; Metabolism of ingested SeMet, Sec, MeSec into H2Se.
DR Reactome; R-HSA-5579024; Defective MAT1A causes MATD.
DR SignaLink; Q00266; -.
DR UniPathway; UPA00315; UER00080.
DR BioGRID-ORCS; 4143; 12 hits in 1071 CRISPR screens.
DR ChiTaRS; MAT1A; human.
DR EvolutionaryTrace; Q00266; -.
DR GenomeRNAi; 4143; -.
DR Pharos; Q00266; Tbio.
DR PRO; PR:Q00266; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q00266; protein.
DR Bgee; ENSG00000151224; Expressed in right lobe of liver and 119 other tissues.
DR ExpressionAtlas; Q00266; baseline and differential.
DR Genevisible; Q00266; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0048269; C:methionine adenosyltransferase complex; IPI:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004478; F:methionine adenosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0009087; P:methionine catabolic process; IMP:UniProtKB.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IDA:ComplexPortal.
DR HAMAP; MF_00086; S_AdoMet_synth1; 1.
DR InterPro; IPR022631; ADOMET_SYNTHASE_CS.
DR InterPro; IPR022630; S-AdoMet_synt_C.
DR InterPro; IPR022629; S-AdoMet_synt_central.
DR InterPro; IPR022628; S-AdoMet_synt_N.
DR InterPro; IPR002133; S-AdoMet_synthetase.
DR InterPro; IPR022636; S-AdoMet_synthetase_sfam.
DR PANTHER; PTHR11964; PTHR11964; 1.
DR Pfam; PF02773; S-AdoMet_synt_C; 1.
DR Pfam; PF02772; S-AdoMet_synt_M; 1.
DR Pfam; PF00438; S-AdoMet_synt_N; 1.
DR PIRSF; PIRSF000497; MAT; 1.
DR SUPFAM; SSF55973; SSF55973; 3.
DR TIGRFAMs; TIGR01034; metK; 1.
DR PROSITE; PS00376; ADOMET_SYNTHASE_1; 1.
DR PROSITE; PS00377; ADOMET_SYNTHASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Disease variant; Disulfide bond; Magnesium;
KW Metal-binding; Nucleotide-binding; One-carbon metabolism; Potassium;
KW Reference proteome; S-nitrosylation; Transferase.
FT CHAIN 1..395
FT /note="S-adenosylmethionine synthase isoform type-1"
FT /id="PRO_0000174432"
FT REGION 113..125
FT /note="Flexible loop"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 23
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P13444"
FT BINDING 29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000305|PubMed:23425511,
FT ECO:0007744|PDB:2OBV"
FT BINDING 57
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 70
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 113
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 179..181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000305|PubMed:23425511,
FT ECO:0007744|PDB:2OBV"
FT BINDING 247..250
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000305|PubMed:23425511,
FT ECO:0007744|PDB:2OBV"
FT BINDING 258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000305|PubMed:23425511,
FT ECO:0007744|PDB:2OBV"
FT BINDING 258
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 264..265
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 285
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 289
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P13444"
FT BINDING 289
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT MOD_RES 120
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P13444"
FT DISULFID 34..60
FT /evidence="ECO:0000250|UniProtKB:P13444"
FT VARIANT 38
FT /note="S -> N (in MATD; abolishes enzyme activity)"
FT /evidence="ECO:0000269|PubMed:10677294"
FT /id="VAR_031242"
FT VARIANT 55
FT /note="A -> D (in MATD; dbSNP:rs118204002)"
FT /evidence="ECO:0000269|PubMed:7560086"
FT /id="VAR_006935"
FT VARIANT 119
FT /note="Q -> H (in dbSNP:rs1143693)"
FT /id="VAR_028944"
FT VARIANT 199
FT /note="R -> C (in MATD; retains 11% of wild-type activity;
FT dbSNP:rs773267230)"
FT /evidence="ECO:0000269|PubMed:8770875"
FT /id="VAR_006936"
FT VARIANT 264
FT /note="R -> C (in MATD; has virtually no enzymatic
FT activity; dbSNP:rs118204005)"
FT /evidence="ECO:0000269|PubMed:10677294"
FT /id="VAR_031243"
FT VARIANT 264
FT /note="R -> H (in MATD; dominant mutation;
FT dbSNP:rs72558181)"
FT /evidence="ECO:0000269|PubMed:10677294,
FT ECO:0000269|PubMed:9042912"
FT /id="VAR_006937"
FT VARIANT 305
FT /note="L -> P (in MATD; dbSNP:rs118204004)"
FT /evidence="ECO:0000269|PubMed:7560086"
FT /id="VAR_006938"
FT VARIANT 322
FT /note="I -> M (in MATD; diminishes but do not completely
FT abolishes enzyme activity; 46% of the level of the wild-
FT type enzyme; dbSNP:rs118204001)"
FT /evidence="ECO:0000269|PubMed:10677294,
FT ECO:0000269|PubMed:7560086"
FT /id="VAR_006939"
FT VARIANT 336
FT /note="G -> R (in MATD; retains significant enzymatic
FT activity; 23% of the level of the wild-type enzyme;
FT dbSNP:rs118204006)"
FT /evidence="ECO:0000269|PubMed:10677294"
FT /id="VAR_031244"
FT VARIANT 344
FT /note="E -> A (in MATD; diminishes but do not completely
FT abolishes enzyme activity; 12% of the level of the wild-
FT type enzyme)"
FT /evidence="ECO:0000269|PubMed:10677294"
FT /id="VAR_031245"
FT VARIANT 356
FT /note="R -> Q (in MATD; dbSNP:rs138742870)"
FT /evidence="ECO:0000269|PubMed:8770875"
FT /id="VAR_006940"
FT VARIANT 357
FT /note="P -> L (in MATD; dbSNP:rs118204003)"
FT /evidence="ECO:0000269|PubMed:7560086"
FT /id="VAR_006941"
FT VARIANT 378
FT /note="G -> S (in MATD; dbSNP:rs1170028069)"
FT /evidence="ECO:0000269|PubMed:8770875"
FT /id="VAR_006942"
FT CONFLICT 272..273
FT /note="GG -> AA (in Ref. 2; BAA08355)"
FT /evidence="ECO:0000305"
FT STRAND 18..25
FT /evidence="ECO:0007829|PDB:2OBV"
FT HELIX 30..48
FT /evidence="ECO:0007829|PDB:2OBV"
FT STRAND 53..61
FT /evidence="ECO:0007829|PDB:2OBV"
FT STRAND 64..72
FT /evidence="ECO:0007829|PDB:2OBV"
FT HELIX 79..90
FT /evidence="ECO:0007829|PDB:2OBV"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:2OBV"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:2OBV"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:2OBV"
FT HELIX 115..121
FT /evidence="ECO:0007829|PDB:2OBV"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:2OBV"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:2OBV"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:2OBV"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:2OBV"
FT HELIX 152..170
FT /evidence="ECO:0007829|PDB:2OBV"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:2OBV"
FT STRAND 176..191
FT /evidence="ECO:0007829|PDB:2OBV"
FT STRAND 194..209
FT /evidence="ECO:0007829|PDB:2OBV"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:2OBV"
FT HELIX 215..224
FT /evidence="ECO:0007829|PDB:2OBV"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:2OBV"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:2OBV"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:2OBV"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:2OBV"
FT TURN 266..273
FT /evidence="ECO:0007829|PDB:2OBV"
FT HELIX 290..307
FT /evidence="ECO:0007829|PDB:2OBV"
FT STRAND 312..320
FT /evidence="ECO:0007829|PDB:2OBV"
FT STRAND 328..333
FT /evidence="ECO:0007829|PDB:2OBV"
FT HELIX 342..352
FT /evidence="ECO:0007829|PDB:2OBV"
FT HELIX 357..363
FT /evidence="ECO:0007829|PDB:2OBV"
FT TURN 364..367
FT /evidence="ECO:0007829|PDB:2OBV"
FT HELIX 371..374
FT /evidence="ECO:0007829|PDB:2OBV"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:2OBV"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:2OBV"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:2OBV"
SQ SEQUENCE 395 AA; 43648 MW; B3462A5670A5B0D4 CRC64;
MNGPVDGLCD HSLSEGVFMF TSESVGEGHP DKICDQISDA VLDAHLKQDP NAKVACETVC
KTGMVLLCGE ITSMAMVDYQ RVVRDTIKHI GYDDSAKGFD FKTCNVLVAL EQQSPDIAQC
VHLDRNEEDV GAGDQGLMFG YATDETEECM PLTIILAHKL NARMADLRRS GLLPWLRPDS
KTQVTVQYMQ DNGAVIPVRI HTIVISVQHN EDITLEEMRR ALKEQVIRAV VPAKYLDEDT
VYHLQPSGRF VIGGPQGDAG VTGRKIIVDT YGGWGAHGGG AFSGKDYTKV DRSAAYAARW
VAKSLVKAGL CRRVLVQVSY AIGVAEPLSI SIFTYGTSQK TERELLDVVH KNFDLRPGVI
VRDLDLKKPI YQKTACYGHF GRSEFPWEVP RKLVF
