M2GD_HUMAN
ID M2GD_HUMAN Reviewed; 866 AA.
AC Q9UI17; B2RBN0; B4E1J9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Dimethylglycine dehydrogenase, mitochondrial;
DE EC=1.5.8.4 {ECO:0000269|PubMed:27486859};
DE AltName: Full=ME2GLYDH;
DE Flags: Precursor;
GN Name=DMGDH;
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), AND VARIANT PRO-279.
RX PubMed=10767172; DOI=10.1006/mgme.2000.2980;
RA Binzak B.A., Vockley J.G., Jenkins R.B., Vockley J.;
RT "Structure and analysis of the human dimethylglycine dehydrogenase gene.";
RL Mol. Genet. Metab. 69:181-187(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLY-530 AND PRO-646, AND
RP VARIANT DMGDHD ARG-109.
RX PubMed=11231903; DOI=10.1086/319520;
RA Binzak B.A., Wevers R.A., Moolenaar S.H., Lee Y.-M., Hwu W.-L.,
RA Poggi-Bach J., Engelke U.F.H., Hoard H.M., Vockley J.G., Vockley J.;
RT "Cloning of dimethylglycine dehydrogenase and a new human inborn error of
RT metabolism, dimethylglycine dehydrogenase deficiency.";
RL Am. J. Hum. Genet. 68:839-847(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP PRO-279.
RC TISSUE=Synovial cell, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
RP DISEASE.
RX PubMed=10102904;
RA Moolenaar S.H., Poggi-Bach J., Engelke U.F.H., Corstiaensen J.M.B.,
RA Heerschap A., de Jong J.G.N., Binzak B.A., Vockley J., Wevers R.A.;
RT "Defect in dimethylglycine dehydrogenase, a new inborn error of metabolism:
RT NMR spectroscopy study.";
RL Clin. Chem. 45:459-464(1999).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.09 ANGSTROMS) OF 29-866 IN COMPLEX WITH FAD,
RP CHARACTERIZATION OF VARIANT DMGDHD ARG-109, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME KINETICS.
RX PubMed=27486859; DOI=10.1111/febs.13828;
RA Augustin P., Hromic A., Pavkov-Keller T., Gruber K., Macheroux P.;
RT "Structure and biochemical properties of recombinant human dimethylglycine
RT dehydrogenase and comparison to the disease-related H109R variant.";
RL FEBS J. 283:3587-3603(2016).
RN [7]
RP VARIANT [LARGE SCALE ANALYSIS] PRO-646, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: Catalyzes the demethylation of N,N-dimethylglycine to
CC sarcosine. Also has activity with sarcosine in vitro.
CC {ECO:0000269|PubMed:27486859}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + H(+) + N,N-
CC dimethylglycine + oxidized [electron-transfer flavoprotein] = (6R)-
CC 5,10-methylenetetrahydrofolyl-(gamma-L-Glu)(n) + reduced [electron-
CC transfer flavoprotein] + sarcosine; Xref=Rhea:RHEA:52856, Rhea:RHEA-
CC COMP:10685, Rhea:RHEA-COMP:10686, Rhea:RHEA-COMP:13257, Rhea:RHEA-
CC COMP:14738, ChEBI:CHEBI:15378, ChEBI:CHEBI:57433, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58251, ChEBI:CHEBI:58307, ChEBI:CHEBI:136572,
CC ChEBI:CHEBI:141005; EC=1.5.8.4;
CC Evidence={ECO:0000269|PubMed:27486859};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:27486859};
CC Note=Binds 1 FAD covalently per monomer. {ECO:0000269|PubMed:27486859};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.4 mM for N,N-dimethylglycine {ECO:0000269|PubMed:27486859};
CC Vmax=22.1 umol/min/mg enzyme;
CC Note=kcat is 213 min(-1) for N,N-dimethylglycine.
CC {ECO:0000269|PubMed:27486859};
CC -!- PATHWAY: Amine and polyamine degradation; betaine degradation;
CC sarcosine from betaine: step 2/2.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UI17-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UI17-2; Sequence=VSP_056959, VSP_056960, VSP_056961,
CC VSP_056962;
CC -!- DISEASE: DMGDH deficiency (DMGDHD) [MIM:605850]: Disorder characterized
CC by fish odor, muscle fatigue with increased serum creatine kinase.
CC Biochemically it is characterized by an increase of N,N-dimethylglycine
CC (DMG) in serum and urine. {ECO:0000269|PubMed:11231903,
CC ECO:0000269|PubMed:27486859}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000305}.
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DR EMBL; AF111858; AAF21941.1; -; mRNA.
DR EMBL; AK303873; BAG64811.1; -; mRNA.
DR EMBL; AK314736; BAG37277.1; -; mRNA.
DR EMBL; AC008502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC016559; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC020937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS4044.1; -. [Q9UI17-1]
DR RefSeq; NP_037523.2; NM_013391.3. [Q9UI17-1]
DR PDB; 5L46; X-ray; 3.09 A; A/B=29-866.
DR PDBsum; 5L46; -.
DR AlphaFoldDB; Q9UI17; -.
DR SMR; Q9UI17; -.
DR BioGRID; 118994; 11.
DR IntAct; Q9UI17; 3.
DR MINT; Q9UI17; -.
DR STRING; 9606.ENSP00000255189; -.
DR CarbonylDB; Q9UI17; -.
DR iPTMnet; Q9UI17; -.
DR PhosphoSitePlus; Q9UI17; -.
DR BioMuta; DMGDH; -.
DR DMDM; 296434575; -.
DR MassIVE; Q9UI17; -.
DR PaxDb; Q9UI17; -.
DR PeptideAtlas; Q9UI17; -.
DR PRIDE; Q9UI17; -.
DR ProteomicsDB; 5764; -.
DR ProteomicsDB; 84455; -. [Q9UI17-1]
DR Antibodypedia; 48453; 194 antibodies from 26 providers.
DR DNASU; 29958; -.
DR Ensembl; ENST00000255189.8; ENSP00000255189.3; ENSG00000132837.15. [Q9UI17-1]
DR GeneID; 29958; -.
DR KEGG; hsa:29958; -.
DR MANE-Select; ENST00000255189.8; ENSP00000255189.3; NM_013391.3; NP_037523.2.
DR UCSC; uc003kfs.5; human. [Q9UI17-1]
DR CTD; 29958; -.
DR DisGeNET; 29958; -.
DR GeneCards; DMGDH; -.
DR HGNC; HGNC:24475; DMGDH.
DR HPA; ENSG00000132837; Group enriched (kidney, liver).
DR MalaCards; DMGDH; -.
DR MIM; 605849; gene.
DR MIM; 605850; phenotype.
DR neXtProt; NX_Q9UI17; -.
DR OpenTargets; ENSG00000132837; -.
DR Orphanet; 243343; Dimethylglycine dehydrogenase deficiency.
DR PharmGKB; PA134947212; -.
DR VEuPathDB; HostDB:ENSG00000132837; -.
DR eggNOG; KOG2844; Eukaryota.
DR GeneTree; ENSGT00940000158176; -.
DR HOGENOM; CLU_007884_11_1_1; -.
DR InParanoid; Q9UI17; -.
DR OMA; PAIPVEH; -.
DR PhylomeDB; Q9UI17; -.
DR TreeFam; TF314735; -.
DR BioCyc; MetaCyc:HS05695-MON; -.
DR BRENDA; 1.5.8.4; 2681.
DR PathwayCommons; Q9UI17; -.
DR Reactome; R-HSA-6798163; Choline catabolism.
DR SignaLink; Q9UI17; -.
DR UniPathway; UPA00291; UER00433.
DR BioGRID-ORCS; 29958; 7 hits in 1072 CRISPR screens.
DR ChiTaRS; DMGDH; human.
DR GenomeRNAi; 29958; -.
DR Pharos; Q9UI17; Tbio.
DR PRO; PR:Q9UI17; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9UI17; protein.
DR Bgee; ENSG00000132837; Expressed in kidney epithelium and 122 other tissues.
DR ExpressionAtlas; Q9UI17; baseline and differential.
DR Genevisible; Q9UI17; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0047865; F:dimethylglycine dehydrogenase activity; IMP:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; NAS:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006579; P:amino-acid betaine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0042426; P:choline catabolic process; IMP:UniProtKB.
DR GO; GO:0019695; P:choline metabolic process; NAS:UniProtKB.
DR Gene3D; 3.30.1360.120; -; 1.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR032503; FAO_M.
DR InterPro; IPR013977; GCV_T_C.
DR InterPro; IPR006222; GCV_T_N.
DR InterPro; IPR029043; GcvT/YgfZ_C.
DR InterPro; IPR027266; TrmE/GcvT_dom1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16350; FAO_M; 1.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 1.
DR SUPFAM; SSF101790; SSF101790; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Disease variant; FAD;
KW Flavoprotein; Mitochondrion; Oxidoreductase; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..50
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 51..866
FT /note="Dimethylglycine dehydrogenase, mitochondrial"
FT /id="PRO_0000010767"
FT REGION 20..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 59..60
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:27486859,
FT ECO:0007744|PDB:5L46"
FT BINDING 80..81
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:27486859,
FT ECO:0007744|PDB:5L46"
FT BINDING 87..95
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:27486859,
FT ECO:0007744|PDB:5L46"
FT BINDING 219
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:27486859,
FT ECO:0007744|PDB:5L46"
FT BINDING 251
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q63342"
FT BINDING 397..402
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:27486859,
FT ECO:0007744|PDB:5L46"
FT BINDING 580..582
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000250|UniProtKB:Q63342"
FT BINDING 676
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000250|UniProtKB:Q63342"
FT BINDING 683..685
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000250|UniProtKB:Q63342"
FT BINDING 744
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000250|UniProtKB:Q63342"
FT MOD_RES 91
FT /note="Tele-8alpha-FAD histidine"
FT /evidence="ECO:0000269|PubMed:27486859,
FT ECO:0007744|PDB:5L46"
FT MOD_RES 114
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBT9"
FT MOD_RES 148
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DBT9"
FT MOD_RES 148
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DBT9"
FT MOD_RES 168
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBT9"
FT MOD_RES 223
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBT9"
FT MOD_RES 317
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBT9"
FT MOD_RES 319
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBT9"
FT MOD_RES 335
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBT9"
FT MOD_RES 360
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBT9"
FT MOD_RES 434
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DBT9"
FT MOD_RES 434
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DBT9"
FT MOD_RES 523
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DBT9"
FT MOD_RES 523
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DBT9"
FT MOD_RES 655
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DBT9"
FT MOD_RES 655
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DBT9"
FT MOD_RES 764
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBT9"
FT MOD_RES 795
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBT9"
FT VAR_SEQ 1..18
FT /note="MLRPGAQLLRGLLLRSCP -> MWSCWRNQSSRLDLPGTQ (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056959"
FT VAR_SEQ 19..398
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056960"
FT VAR_SEQ 751..774
FT /note="PADFIGKQALKQIKAKGLKRRLVC -> DQNSCFAHFKEENGWVSRWAIRPY
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056961"
FT VAR_SEQ 775..866
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056962"
FT VARIANT 109
FT /note="H -> R (in DMGDHD; shows 10 fold lower catalytic
FT efficiency due to lower cofactor saturation and reduced
FT thermal stability; dbSNP:rs121908331)"
FT /evidence="ECO:0000269|PubMed:11231903,
FT ECO:0000269|PubMed:27486859"
FT /id="VAR_011505"
FT VARIANT 279
FT /note="S -> P (in dbSNP:rs532964)"
FT /evidence="ECO:0000269|PubMed:10767172,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_014950"
FT VARIANT 530
FT /note="A -> G (in dbSNP:rs1805073)"
FT /evidence="ECO:0000269|PubMed:11231903"
FT /id="VAR_014951"
FT VARIANT 646
FT /note="S -> P (in dbSNP:rs1805074)"
FT /evidence="ECO:0000269|PubMed:11231903,
FT ECO:0007744|PubMed:24275569"
FT /id="VAR_014952"
FT CONFLICT 381
FT /note="M -> I (in Ref. 3; BAG37277)"
FT /evidence="ECO:0000305"
FT CONFLICT 627
FT /note="L -> F (in Ref. 3; BAG37277)"
FT /evidence="ECO:0000305"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:5L46"
FT HELIX 59..70
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:5L46"
FT TURN 84..88
FT /evidence="ECO:0007829|PDB:5L46"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:5L46"
FT HELIX 105..123
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:5L46"
FT HELIX 141..154
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:5L46"
FT HELIX 166..170
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:5L46"
FT HELIX 195..208
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 238..246
FT /evidence="ECO:0007829|PDB:5L46"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:5L46"
FT HELIX 252..256
FT /evidence="ECO:0007829|PDB:5L46"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 266..275
FT /evidence="ECO:0007829|PDB:5L46"
FT HELIX 279..283
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:5L46"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 298..303
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 306..311
FT /evidence="ECO:0007829|PDB:5L46"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:5L46"
FT HELIX 323..326
FT /evidence="ECO:0007829|PDB:5L46"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:5L46"
FT HELIX 346..355
FT /evidence="ECO:0007829|PDB:5L46"
FT HELIX 357..360
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 364..374
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 381..384
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 391..395
FT /evidence="ECO:0007829|PDB:5L46"
FT HELIX 400..415
FT /evidence="ECO:0007829|PDB:5L46"
FT TURN 425..427
FT /evidence="ECO:0007829|PDB:5L46"
FT HELIX 438..450
FT /evidence="ECO:0007829|PDB:5L46"
FT HELIX 451..453
FT /evidence="ECO:0007829|PDB:5L46"
FT HELIX 474..478
FT /evidence="ECO:0007829|PDB:5L46"
FT HELIX 479..481
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 482..487
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 490..496
FT /evidence="ECO:0007829|PDB:5L46"
FT HELIX 515..527
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 530..533
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 537..544
FT /evidence="ECO:0007829|PDB:5L46"
FT HELIX 547..554
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 564..571
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 577..585
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 591..595
FT /evidence="ECO:0007829|PDB:5L46"
FT HELIX 597..599
FT /evidence="ECO:0007829|PDB:5L46"
FT HELIX 600..613
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 619..622
FT /evidence="ECO:0007829|PDB:5L46"
FT TURN 624..626
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 630..634
FT /evidence="ECO:0007829|PDB:5L46"
FT HELIX 637..642
FT /evidence="ECO:0007829|PDB:5L46"
FT TURN 651..653
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 658..664
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 667..673
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 678..687
FT /evidence="ECO:0007829|PDB:5L46"
FT HELIX 690..702
FT /evidence="ECO:0007829|PDB:5L46"
FT TURN 703..706
FT /evidence="ECO:0007829|PDB:5L46"
FT HELIX 712..722
FT /evidence="ECO:0007829|PDB:5L46"
FT TURN 727..729
FT /evidence="ECO:0007829|PDB:5L46"
FT TURN 737..741
FT /evidence="ECO:0007829|PDB:5L46"
FT HELIX 743..745
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 750..752
FT /evidence="ECO:0007829|PDB:5L46"
FT HELIX 757..766
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 769..777
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 789..792
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 795..806
FT /evidence="ECO:0007829|PDB:5L46"
FT TURN 807..810
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 811..819
FT /evidence="ECO:0007829|PDB:5L46"
FT HELIX 820..822
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 828..833
FT /evidence="ECO:0007829|PDB:5L46"
FT STRAND 836..842
FT /evidence="ECO:0007829|PDB:5L46"
FT TURN 851..853
FT /evidence="ECO:0007829|PDB:5L46"
SQ SEQUENCE 866 AA; 96811 MW; 2EC1FA7DCB6C1F8C CRC64;
MLRPGAQLLR GLLLRSCPLQ GSPGRPRSVC GREGEEKPPL SAETQWKDRA ETVIIGGGCV
GVSLAYHLAK AGMKDVVLLE KSELTAGSTW HAAGLTTYFH PGINLKKIHY DSIKLYEKLE
EETGQVVGFH QPGSIRLATT PVRVDEFKYQ MTRTGWHATE QYLIEPEKIQ EMFPLLNMNK
VLAGLYNPGD GHIDPYSLTM ALAAGARKCG ALLKYPAPVT SLKARSDGTW DVETPQGSMR
ANRIVNAAGF WAREVGKMIG LEHPLIPVQH QYVVTSTISE VKALKRELPV LRDLEGSYYL
RQERDGLLFG PYESQEKMKV QDSWVTNGVP PGFGKELFES DLDRIMEHIK AAMEMVPVLK
KADIINVVNG PITYSPDILP MVGPHQGVRN YWVAIGFGYG IIHAGGVGKY LSDWILHGEP
PFDLIELDPN RYGKWTTTQY TEAKARESYG FNNIVGYPKE ERFAGRPTQR VSGLYQRLES
KCSMGFHAGW EQPHWFYKPG QDTQYRPSFR RTNWFEPVGS EYKQVMQRVA VTDLSPFGKF
NIKGQDSIRL LDHLFANVIP KVGFTNISHM LTPKGRVYAE LTVSHQSPGE FLLITGSGSE
LHDLRWIEEE AVKGGYDVEI KNITDELGVL GVAGPQARKV LQKLTSEDLS DDVFKFLQTK
SLKVSNIPVT AIRISYTGEL GWELYHRRED SVALYDAIMN AGQEEGIDNF GTYAMNALRL
EKAFRAWGLE MNCDTNPLEA GLEYFVKLNK PADFIGKQAL KQIKAKGLKR RLVCLTLATD
DVDPEGNESI WYNGKVVGNT TSGSYSYSIQ KSLAFAYVPV QLSEVGQQVE VELLGKNYPA
VIIQEPLVLT EPTRNRLQKK GGKDKT
