3MG_HUMAN
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 03-AUG-2022, entry version 224.
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 -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/mpg/";
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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_001015052.2. [P29372-4]
DR RefSeq; NP_001015054.1; NM_001015054.2. [P29372-5]
DR RefSeq; NP_002425.2; NM_002434.3. [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 PDBsum; 1BNK; -.
DR PDBsum; 1EWN; -.
DR PDBsum; 1F4R; -.
DR PDBsum; 1F6O; -.
DR PDBsum; 3QI5; -.
DR PDBsum; 3UBY; -.
DR AlphaFoldDB; P29372; -.
DR SMR; P29372; -.
DR BioGRID; 110490; 95.
DR IntAct; P29372; 23.
DR MINT; P29372; -.
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; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P29372; -.
DR PhosphoSitePlus; P29372; -.
DR SwissPalm; P29372; -.
DR BioMuta; MPG; -.
DR EPD; P29372; -.
DR jPOST; P29372; -.
DR MassIVE; P29372; -.
DR MaxQB; P29372; -.
DR PaxDb; P29372; -.
DR PeptideAtlas; P29372; -.
DR PRIDE; P29372; -.
DR ProteomicsDB; 33913; -.
DR ProteomicsDB; 54553; -. [P29372-1]
DR ProteomicsDB; 54554; -. [P29372-2]
DR ProteomicsDB; 62987; -.
DR TopDownProteomics; P29372-1; -. [P29372-1]
DR Antibodypedia; 1865; 419 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 CTD; 4350; -.
DR DisGeNET; 4350; -.
DR GeneCards; MPG; -.
DR HGNC; HGNC:7211; MPG.
DR HPA; ENSG00000103152; Low tissue specificity.
DR MIM; 156565; gene.
DR neXtProt; NX_P29372; -.
DR OpenTargets; ENSG00000103152; -.
DR PharmGKB; PA30917; -.
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; 1500650at2759; -.
DR PhylomeDB; P29372; -.
DR TreeFam; TF331768; -.
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 BioGRID-ORCS; 4350; 7 hits in 1077 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 192 other tissues.
DR ExpressionAtlas; P29372; baseline and differential.
DR Genevisible; P29372; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:UniProtKB-SubCell.
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:0019104; F:DNA N-glycosylase activity; TAS:Reactome.
DR GO; GO:0008725; F:DNA-3-methyladenine glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0052822; F:DNA-3-methylguanine glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0052821; F:DNA-7-methyladenine glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0043916; F:DNA-7-methylguanine glycosylase activity; IEA:UniProtKB-EC.
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 dealkylation involved in DNA repair; TAS:ProtInc.
DR CDD; cd00540; AAG; 1.
DR Gene3D; 3.10.300.10; -; 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 PANTHER; PTHR10429; PTHR10429; 1.
DR Pfam; PF02245; Pur_DNA_glyco; 1.
DR SUPFAM; SSF50486; SSF50486; 1.
DR TIGRFAMs; TIGR00567; 3mg; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; DNA damage; DNA repair;
KW Hydrolase; Mitochondrion; Mitochondrion nucleoid; Nucleus; Phosphoprotein;
KW 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 27..51
FT /note="Polar 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 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 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 178..188
FT /evidence="ECO:0007829|PDB:3UBY"
FT HELIX 190..199
FT /evidence="ECO:0007829|PDB:3UBY"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:3UBY"
FT STRAND 214..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 253..255
FT /evidence="ECO:0007829|PDB:3UBY"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:3UBY"
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
