ID 3MG_HUMAN Reviewed; 298 AA. AC P29372; G5E9E2; Q13770; Q15275; Q15961; Q5J9I4; Q96BZ6; Q96S33; Q9NNX5; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 3. DT 02-SEP-2026, entry version 243. DE RecName: Full=DNA-3-methyladenine glycosylase; DE EC=3.2.2.21; DE AltName: Full=3-alkyladenine DNA glycosylase; DE AltName: Full=3-methyladenine DNA glycosidase; DE AltName: Full=ADPG; DE AltName: Full=N-methylpurine-DNA glycosylase; DE Flags: Precursor; GN Name=MPG; Synonyms=AAG, ANPG, MID1; 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). RC TISSUE=Liver; RX PubMed=1924375; DOI=10.1073/pnas.88.20.9127; RA Samson L., Derfler B., Boosalis M., Call K.; RT "Cloning and characterization of a 3-methyladenine DNA glycosylase cDNA RT from human cells whose gene maps to chromosome 16."; RL Proc. Natl. Acad. Sci. U.S.A. 88:9127-9131(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=8475094; DOI=10.1073/pnas.90.8.3437; RA Vickers M.A., Vyas P., Harris P.C., Simmons D.L., Higgs D.R.; RT "Structure of the human 3-methyladenine DNA glycosylase gene and RT localization close to the 16p telomere."; RL Proc. Natl. Acad. Sci. U.S.A. 90:3437-3441(1993). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RA Kim J.W.; RT "Identification of a human cell proliferation gene 11."; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-22; HIS-71; VAL-258 AND RP SER-298. RG NIEHS SNPs program; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11157797; DOI=10.1093/hmg/10.4.339; RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., RA Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.; RT "Sequence, structure and pathology of the fully annotated terminal 2 Mb of RT the short arm of human chromosome 16."; RL Hum. Mol. Genet. 10:339-352(2001). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [7] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Pancreas; 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 [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 28-298 (ISOFORMS 1/2). RX PubMed=1874728; DOI=10.1016/s0021-9258(18)98467-x; RA Chakravarti D., Ibeanu G.C., Tano K., Mitra S.; RT "Cloning and expression in Escherichia coli of a human cDNA encoding the RT DNA repair protein N-methylpurine-DNA glycosylase."; RL J. Biol. Chem. 266:15710-15715(1991). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 69-298 (ISOFORMS 1/2). RX PubMed=1645538; DOI=10.1016/0006-291x(91)90408-y; RA O'Connor T.R., Laval J.; RT "Human cDNA expressing a functional DNA glycosylase excising 3- RT methyladenine and 7-methylguanine."; RL Biochem. Biophys. Res. Commun. 176:1170-1177(1991). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 230-298 (ISOFORMS 1/2). RX PubMed=8318735; DOI=10.1007/bf00357090; RA Kielman M.F., Smits R., Devi T.S., Fodde R., Bernini L.F.; RT "Homology of a 130-kb region enclosing the alpha-globin gene cluster, the RT alpha-locus controlling region, and two non-globin genes in human and RT mouse."; RL Mamm. Genome 4:314-323(1993). RN [12] RP INTERACTION WITH MBD1. RX PubMed=14555760; DOI=10.1073/pnas.2131819100; RA Watanabe S., Ichimura T., Fujita N., Tsuruzoe S., Ohki I., Shirakawa M., RA Kawasuji M., Nakao M.; RT "Methylated DNA-binding domain 1 and methylpurine-DNA glycosylase link RT transcriptional repression and DNA repair in chromatin."; RL Proc. Natl. Acad. Sci. U.S.A. 100:12859-12864(2003). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [14] 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 [15] RP SUBCELLULAR LOCATION, INTERACTION WITH SSBP1, AND ACTIVITY REGULATION. RX PubMed=23290262; DOI=10.1016/j.dnarep.2012.11.009; RA van Loon B., Samson L.D.; RT "Alkyladenine DNA glycosylase (AAG) localizes to mitochondria and interacts RT with mitochondrial single-stranded binding protein (mtSSB)."; RL DNA Repair 12:177-187(2013). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 80-199. RX PubMed=9790531; DOI=10.1016/s0092-8674(00)81755-9; RA Lau A.Y., Scharer O.D., Samson L., Verdine G.L., Ellenberger T.; RT "Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA: RT mechanisms for nucleotide flipping and base excision."; RL Cell 95:249-258(1998). CC -!- FUNCTION: Hydrolysis of the deoxyribose N-glycosidic bond to excise 3- CC methyladenine, and 7-methylguanine from the damaged DNA polymer formed CC by alkylation lesions. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3- CC methylguanine, 7-methylguanine and 7-methyladenine.; EC=3.2.2.21; CC -!- ACTIVITY REGULATION: Binding to SSBP1 in mitochondria inhibits CC glycosylase activity in the context of a single-stranded DNA (ssDNA), CC but not a double-stranded DNA (dsDNA) substrates. CC {ECO:0000269|PubMed:23290262}. CC -!- SUBUNIT: Binds MBD1. Binds SSBP1. CC -!- INTERACTION: CC P29372; Q9BPX1: HSD17B14; NbExp=4; IntAct=EBI-1043398, EBI-742664; CC P29372; P04156: PRNP; NbExp=4; IntAct=EBI-1043398, EBI-977302; CC P29372-4; Q9BPX1: HSD17B14; NbExp=3; IntAct=EBI-10695618, EBI-742664; CC P29372-4; P40692: MLH1; NbExp=3; IntAct=EBI-10695618, EBI-744248; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23290262}. CC Mitochondrion matrix, mitochondrion nucleoid CC {ECO:0000269|PubMed:23290262}. Nucleus {ECO:0000269|PubMed:23290262}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Comment=Experimental confirmation may be lacking for some isoforms.; CC Name=1; CC IsoId=P29372-1; Sequence=Displayed; CC Name=2; CC IsoId=P29372-2; Sequence=VSP_003249, VSP_035485; CC Name=3; CC IsoId=P29372-4; Sequence=VSP_003249; CC Name=4; CC IsoId=P29372-5; Sequence=VSP_046678; CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. {ECO:0000305}. 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; M74905; AAA58627.1; -; mRNA. DR EMBL; L10752; AAF77073.1; -; mRNA. DR EMBL; AY258284; AAP82229.1; -; mRNA. DR EMBL; AY305873; AAQ95215.1; -; mRNA. DR EMBL; AF499437; AAM14628.1; -; Genomic_DNA. DR EMBL; AE006462; AAK61213.1; -; Genomic_DNA. DR EMBL; Z69720; CAA93540.1; -; Genomic_DNA. DR EMBL; Z69720; CAI95610.1; -; Genomic_DNA. DR EMBL; CH471112; EAW85871.1; -; Genomic_DNA. DR EMBL; BC014991; AAH14991.1; -; mRNA. DR EMBL; S51033; AAB19537.1; -; mRNA. DR EMBL; X56528; CAA39875.1; -; mRNA. DR EMBL; M71215; AAA58369.1; -; mRNA. DR EMBL; M99626; AAB46421.1; -; mRNA. DR CCDS; CCDS32345.1; -. [P29372-4] DR CCDS; CCDS32346.1; -. [P29372-1] DR CCDS; CCDS42087.1; -. [P29372-5] DR PIR; A40798; A40798. DR PIR; A41230; A41230. DR PIR; A47471; A47471. DR PIR; JN0062; JN0062. DR RefSeq; NP_001015052.1; NM_001015052.3. [P29372-4] DR RefSeq; NP_001015054.1; NM_001015054.3. [P29372-5] DR RefSeq; NP_002425.2; NM_002434.4. [P29372-1] DR PDB; 1BNK; X-ray; 2.70 A; A=80-295. DR PDB; 1EWN; X-ray; 2.10 A; A=80-298. DR PDB; 1F4R; X-ray; 2.40 A; A=80-298. DR PDB; 1F6O; X-ray; 2.40 A; A=80-298. DR PDB; 3QI5; X-ray; 2.20 A; A/B=84-298. DR PDB; 3UBY; X-ray; 2.00 A; A/B=84-298. DR PDB; 7XFH; EM; 2.90 A; K=1-298. DR PDB; 7XFJ; EM; 3.00 A; K=1-298. DR PDB; 7XFM; EM; 3.10 A; K=1-298. DR AlphaFoldDB; P29372; -. DR EMDB; EMD-33172; -. DR EMDB; EMD-33174; -. DR EMDB; EMD-33176; -. DR SMR; P29372; -. DR BioGRID; 110490; 116. DR FunCoup; P29372; 704. DR IntAct; P29372; 33. DR MINT; P29372; -. DR NDEx; IQUERY-CP-MPG; 4 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000219431; -. DR BindingDB; P29372; -. DR ChEMBL; CHEMBL3396943; -. DR DrugBank; DB00515; Cisplatin. DR DrugBank; DB01593; Zinc. DR DrugBank; DB14487; Zinc acetate. DR DrugBank; DB14533; Zinc chloride. DR DrugBank; DB14548; Zinc sulfate, unspecified form. DR DrugCentral; P29372; -. DR GlyGen; P29372; 10 sites, 2 N-linked glycans (2 sites), 1 O-linked glycan (5 sites). DR iPTMnet; P29372; -. DR PhosphoSitePlus; P29372; -. DR SwissPalm; P29372; -. DR BioMuta; MPG; -. DR jPOST; P29372; -. DR MassIVE; P29372; -. DR PaxDb; 9606-ENSP00000219431; -. DR PeptideAtlas; P29372; -. DR ProteomicsDB; 33913; -. DR ProteomicsDB; 54553; -. [P29372-1] DR ProteomicsDB; 54554; -. [P29372-2] DR ProteomicsDB; 62987; -. DR Pumba; P29372; -. DR TopDownProteomics; P29372-1; -. [P29372-1] DR Antibodypedia; 1865; 421 antibodies from 36 providers. DR DNASU; 4350; -. DR Ensembl; ENST00000219431.4; ENSP00000219431.4; ENSG00000103152.12. [P29372-1] DR Ensembl; ENST00000356432.8; ENSP00000348809.4; ENSG00000103152.12. [P29372-4] DR Ensembl; ENST00000397817.5; ENSP00000380918.1; ENSG00000103152.12. [P29372-5] DR GeneID; 4350; -. DR KEGG; hsa:4350; -. DR MANE-Select; ENST00000356432.8; ENSP00000348809.4; NM_001015052.3; NP_001015052.1. [P29372-4] DR UCSC; uc002cfm.4; human. [P29372-1] DR AGR; HGNC:7211; -. DR ClinPGx; PA30917; -. DR CTD; 4350; -. DR DisGeNET; 4350; -. DR GeneCards; MPG; -. DR HGNC; HGNC:7211; MPG. DR HPA; ENSG00000103152; Low tissue specificity. DR MIM; 156565; gene. DR OpenTargets; ENSG00000103152; -. DR VEuPathDB; HostDB:ENSG00000103152; -. DR eggNOG; KOG4486; Eukaryota. DR GeneTree; ENSGT00390000009825; -. DR HOGENOM; CLU_060471_0_0_1; -. DR InParanoid; P29372; -. DR OMA; VEAYHHT; -. DR OrthoDB; 6353017at2759; -. DR PAN-GO; P29372; 2 GO annotations based on evolutionary models. DR PhylomeDB; P29372; -. DR BRENDA; 3.2.2.21; 2681. DR PathwayCommons; P29372; -. DR Reactome; R-HSA-110330; Recognition and association of DNA glycosylase with site containing an affected purine. DR Reactome; R-HSA-110331; Cleavage of the damaged purine. DR Reactome; R-HSA-110357; Displacement of DNA glycosylase by APEX1. DR SABIO-RK; P29372; -. DR SignaLink; P29372; -. DR SIGNOR; P29372; -. DR Agora; ENSG00000103152; -. DR BioGRID-ORCS; 4350; 9 hits in 1158 CRISPR screens. DR ChiTaRS; MPG; human. DR EvolutionaryTrace; P29372; -. DR GeneWiki; MPG_(gene); -. DR GenomeRNAi; 4350; -. DR Pharos; P29372; Tchem. DR PRO; PR:P29372; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; P29372; protein. DR Bgee; ENSG00000103152; Expressed in ascending aorta and 194 other cell types or tissues. DR ExpressionAtlas; P29372; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; HTP:FlyBase. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0003905; F:alkylbase DNA N-glycosylase activity; IBA:GO_Central. DR GO; GO:0003684; F:damaged DNA binding; TAS:ProtInc. DR GO; GO:0003677; F:DNA binding; EXP:DisProt. DR GO; GO:0019104; F:DNA N-glycosylase activity; TAS:Reactome. DR GO; GO:0006284; P:base-excision repair; IBA:GO_Central. DR GO; GO:0045007; P:depurination; TAS:Reactome. DR GO; GO:0006307; P:DNA alkylation repair; TAS:ProtInc. DR CDD; cd00540; AAG; 1. DR DisProt; DP04189; -. DR FunFam; 3.10.300.10:FF:000001; Putative 3-methyladenine DNA glycosylase; 1. DR Gene3D; 3.10.300.10; Methylpurine-DNA glycosylase (MPG); 1. DR HAMAP; MF_00527; 3MGH; 1. DR InterPro; IPR011034; Formyl_transferase-like_C_sf. DR InterPro; IPR003180; MPG. DR InterPro; IPR036995; MPG_sf. DR NCBIfam; TIGR00567; 3mg; 1. DR PANTHER; PTHR10429; DNA-3-METHYLADENINE GLYCOSYLASE; 1. DR PANTHER; PTHR10429:SF0; DNA-3-METHYLADENINE GLYCOSYLASE; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR SUPFAM; SSF50486; FMT C-terminal domain-like; 1. DR PDBsum; 1BNK; -. DR PDBsum; 1EWN; -. DR PDBsum; 1F4R; -. DR PDBsum; 1F6O; -. DR PDBsum; 3QI5; -. DR PDBsum; 3UBY; -. DR PDBsum; 7XFH; -. DR PDBsum; 7XFJ; -. DR PDBsum; 7XFM; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; DNA damage; DNA repair; KW Hydrolase; Mitochondrion; Mitochondrion nucleoid; Nucleus; Phosphoprotein; KW Proteomics identification; Reference proteome; Transit peptide. FT TRANSIT 1..17 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 18..298 FT /note="DNA-3-methyladenine glycosylase" FT /id="PRO_0000100065" FT REGION 1..65 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 9..25 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 78 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 252 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..17 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_046678" FT VAR_SEQ 1..12 FT /note="MVTPALQMKKPK -> MPARSGA (in isoform 2 and isoform FT 3)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:8475094, ECO:0000303|Ref.3" FT /id="VSP_003249" FT VAR_SEQ 195..196 FT /note="QL -> HV (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:8475094" FT /id="VSP_035485" FT VARIANT 22 FT /note="K -> Q (in dbSNP:rs3176383)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_019138" FT VARIANT 64 FT /note="P -> L (in dbSNP:rs2308315)" FT /id="VAR_014831" FT VARIANT 71 FT /note="Y -> H (in dbSNP:rs2266607)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_014832" FT VARIANT 93 FT /note="Q -> R (in dbSNP:rs25671)" FT /id="VAR_050096" FT VARIANT 120 FT /note="R -> C (in dbSNP:rs2308313)" FT /id="VAR_014833" FT VARIANT 141 FT /note="R -> Q (in dbSNP:rs2308312)" FT /id="VAR_014834" FT VARIANT 258 FT /note="A -> V (in dbSNP:rs769193)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_014835" FT VARIANT 298 FT /note="A -> S (in dbSNP:rs2234949)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_014836" FT CONFLICT 13 FT /note="Q -> QV (in Ref. 5; AAK61213)" FT /evidence="ECO:0000305" FT CONFLICT 29..31 FT /note="GQP -> ARA (in Ref. 9; AAB19537)" FT /evidence="ECO:0000305" FT CONFLICT 44 FT /note="Q -> R (in Ref. 9; AAB19537)" FT /evidence="ECO:0000305" FT CONFLICT 69..71 FT /note="GPY -> SKD (in Ref. 10; AAA58369/CAA39875)" FT /evidence="ECO:0000305" FT CONFLICT 82 FT /note="H -> L (in Ref. 10; AAA58369/CAA39875)" FT /evidence="ECO:0000305" FT CONFLICT 134 FT /note="A -> P (in Ref. 1; AAA58627)" FT /evidence="ECO:0000305" FT CONFLICT 287 FT /note="V -> E (in Ref. 10; AAA58369)" FT /evidence="ECO:0000305" FT HELIX 82..84 FT /evidence="ECO:0007829|PDB:1F6O" FT HELIX 88..91 FT /evidence="ECO:0007829|PDB:3UBY" FT HELIX 95..101 FT /evidence="ECO:0007829|PDB:3UBY" FT TURN 102..104 FT /evidence="ECO:0007829|PDB:3UBY" FT STRAND 106..110 FT /evidence="ECO:0007829|PDB:3UBY" FT TURN 112..114 FT /evidence="ECO:0007829|PDB:7XFH" FT STRAND 116..127 FT /evidence="ECO:0007829|PDB:3UBY" FT STRAND 129..131 FT /evidence="ECO:0007829|PDB:1F6O" FT HELIX 138..140 FT /evidence="ECO:0007829|PDB:3UBY" FT HELIX 145..150 FT /evidence="ECO:0007829|PDB:3UBY" FT STRAND 152..154 FT /evidence="ECO:0007829|PDB:7XFM" FT STRAND 155..161 FT /evidence="ECO:0007829|PDB:3UBY" FT TURN 162..164 FT /evidence="ECO:0007829|PDB:3UBY" FT STRAND 165..171 FT /evidence="ECO:0007829|PDB:3UBY" FT STRAND 173..176 FT /evidence="ECO:0007829|PDB:7XFH" FT STRAND 178..188 FT /evidence="ECO:0007829|PDB:3UBY" FT HELIX 190..199 FT /evidence="ECO:0007829|PDB:3UBY" FT HELIX 208..210 FT /evidence="ECO:0007829|PDB:1F6O" FT HELIX 211..213 FT /evidence="ECO:0007829|PDB:3UBY" FT STRAND 215..217 FT /evidence="ECO:0007829|PDB:3UBY" FT HELIX 218..224 FT /evidence="ECO:0007829|PDB:3UBY" FT HELIX 229..231 FT /evidence="ECO:0007829|PDB:3UBY" FT TURN 236..238 FT /evidence="ECO:0007829|PDB:3UBY" FT STRAND 240..245 FT /evidence="ECO:0007829|PDB:3UBY" FT HELIX 246..248 FT /evidence="ECO:0007829|PDB:1F6O" FT HELIX 253..255 FT /evidence="ECO:0007829|PDB:3UBY" FT STRAND 256..259 FT /evidence="ECO:0007829|PDB:3UBY" FT STRAND 262..264 FT /evidence="ECO:0007829|PDB:7XFM" FT TURN 268..272 FT /evidence="ECO:0007829|PDB:3UBY" FT STRAND 276..279 FT /evidence="ECO:0007829|PDB:3UBY" FT TURN 290..292 FT /evidence="ECO:0007829|PDB:3UBY" SQ SEQUENCE 298 AA; 32869 MW; BEA8C4CB250D572B CRC64; MVTPALQMKK PKQFCRRMGQ KKQRPARAGQ PHSSSDAAQA PAEQPHSSSD AAQAPCPRER CLGPPTTPGP YRSIYFSSPK GHLTRLGLEF FDQPAVPLAR AFLGQVLVRR LPNGTELRGR IVETEAYLGP EDEAAHSRGG RQTPRNRGMF MKPGTLYVYI IYGMYFCMNI SSQGDGACVL LRALEPLEGL ETMRQLRSTL RKGTASRVLK DRELCSGPSK LCQALAINKS FDQRDLAQDE AVWLERGPLE PSEPAVVAAA RVGVGHAGEW ARKPLRFYVR GSPWVSVVDR VAEQDTQA //