ID OGG1_HUMAN Reviewed; 345 AA.
AC O15527; A8K1E3; O00390; O00670; O00705; O14876; O95488; P78554; Q9BW42;
AC Q9UIK0; Q9UIK1; Q9UIK2; Q9UL34; Q9Y2C0; Q9Y2C1; Q9Y6C3; Q9Y6C4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 27-MAR-2024, entry version 232.
DE RecName: Full=N-glycosylase/DNA lyase;
DE Includes:
DE RecName: Full=8-oxoguanine DNA glycosylase;
DE EC=3.2.2.-;
DE Includes:
DE RecName: Full=DNA-(apurinic or apyrimidinic site) lyase;
DE Short=AP lyase;
DE EC=4.2.99.18;
GN Name=OGG1; Synonyms=MMH, MUTM, OGH1;
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] (ISOFORMS 1A; 1B AND 2A).
RC TISSUE=Colon;
RX PubMed=9187114;
RA Aburatani H., Hippo Y., Ishida T., Takashima R., Matsuba C., Kodama T.,
RA Takao M., Yasui A., Yamamoto K., Asano M., Fukasawa K., Yoshinari T.,
RA Inoue H., Otsuka E., Nishimura S.;
RT "Cloning and characterization of mammalian 8-hydroxyguanine-specific DNA
RT glycosylase/apurinic, apyrimidinic lyase, a functional mutM homologue.";
RL Cancer Res. 57:2151-2156(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A).
RX PubMed=9207108; DOI=10.1073/pnas.94.14.7429;
RA Rosenquist T.A., Zharkov D.O., Grollman A.P.;
RT "Cloning and characterization of a mammalian 8-oxoguanine DNA
RT glycosylase.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:7429-7434(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2A).
RX PubMed=9223306; DOI=10.1073/pnas.94.15.8016;
RA Roldan-Arjona T., Wei Y.-F., Carter K.C., Klungland A., Anselmino C.,
RA Wang R.-P., Augustus M., Lindahl T.;
RT "Molecular cloning and functional expression of a human cDNA encoding the
RT antimutator enzyme 8-hydroxyguanine-DNA glycosylase.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:8016-8020(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A).
RX PubMed=9223305; DOI=10.1073/pnas.94.15.8010;
RA Radicella J.P., Dherin C., Desmaze C., Fox M.S., Boiteux S.;
RT "Cloning and characterization of hOGG1, a human homolog of the OGG1 gene of
RT Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:8010-8015(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A), ACTIVE SITE, AND MUTAGENESIS OF
RP LYS-249.
RX PubMed=9197244; DOI=10.1016/s0960-9822(06)00187-4;
RA Lu R., Nash H.M., Verdine G.L.;
RT "A mammalian DNA repair enzyme that excises oxidatively damaged guanines
RT maps to a locus frequently lost in lung cancer.";
RL Curr. Biol. 7:397-407(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A).
RX PubMed=9190902; DOI=10.1038/sj.onc.1201139;
RA Arai K., Morishita K., Shinmura K., Kohno T., Taniwaki M., Ohwada S.,
RA Yokota J.;
RT "Cloning of a human homolog of the yeast OGG1 gene that is involved in the
RT repair of oxidative DNA damage.";
RL Oncogene 14:2857-2861(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A).
RX PubMed=9348312; DOI=10.1084/jem.186.9.1547;
RA Kuo F.C., Sklar J.L.;
RT "Augmented expression of a human gene for 8-oxoguanine DNA glycosylase
RT (MutM) in B lymphocytes of the dark zone in lymph node germinal centers.";
RL J. Exp. Med. 186:1547-1556(1997).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A).
RX PubMed=9321410; DOI=10.1093/emboj/16.20.6314;
RA Bjoras M., Luna L., Johnsen B.E., Hoff E., Haug T., Rognes T., Seeberg E.;
RT "Opposite base-dependent reactions of a human base excision repair enzyme
RT on DNA containing 7,8-dihydro-8-oxoguanine and abasic sites.";
RL EMBO J. 16:6314-6322(1997).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Dhenaut A., Boiteux S., Radicella J.;
RT "Genomic structure and promoter characterization of the human 8-OH-guanine
RT glycosylase gene (OGG1) gene.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=10449904; DOI=10.1159/000015299;
RA Ishida T., Hippo Y., Nakahori Y., Matsushita I., Kodama T., Nishimura S.,
RA Aburatani H.;
RT "Structure and chromosome location of human OGG1.";
RL Cytogenet. Cell Genet. 85:232-236(1999).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RX PubMed=10233168; DOI=10.1091/mbc.10.5.1637;
RA Nishioka K., Ohtsubo T., Oda H., Fujiwara T., Kang D., Sugimachi K.,
RA Nakabeppu Y.;
RT "Expression and differential intracellular localization of two major forms
RT of human 8-Oxoguanine DNA glycosylase encoded by alternatively spliced OGG1
RT mRNAs.";
RL Mol. Biol. Cell 10:1637-1652(1999).
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1A), AND VARIANT CYS-326.
RC TISSUE=Brain;
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 [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-229; VAL-288; ASN-322
RP AND CYS-326.
RG NIEHS SNPs program;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [15]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT CYS-326.
RC TISSUE=Eye;
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 [16]
RP REVIEW.
RX PubMed=10775435; DOI=10.1006/abbi.2000.1773;
RA Boiteux S., Radicella J.P.;
RT "The human OGG1 gene: structure, functions, and its implication in the
RT process of carcinogenesis.";
RL Arch. Biochem. Biophys. 377:1-8(2000).
RN [17]
RP SUBCELLULAR LOCATION.
RX PubMed=17148573; DOI=10.1242/jcs.03312;
RA Campalans A., Amouroux R., Bravard A., Epe B., Radicella J.P.;
RT "UVA irradiation induces relocalisation of the DNA repair protein hOGG1 to
RT nuclear speckles.";
RL J. Cell Sci. 120:23-32(2007).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 12-327 OF MUTANT GLN-247 IN
RP COMPLEX WITH DNA, AND CHARACTERIZATION OF VARIANT HIS-154.
RX PubMed=10706276; DOI=10.1038/35002510;
RA Bruner S.D., Norman D.P.G., Verdine G.L.;
RT "Structural basis for recognition and repair of the endogenous mutagen 8-
RT oxoguanine in DNA.";
RL Nature 403:859-866(2000).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH DNA AND
RP 8-OXO-GUANINE.
RX PubMed=11902834; DOI=10.1006/jmbi.2002.5400;
RA Bjoras M., Seeberg E., Luna L., Pearl L.H., Barrett T.E.;
RT "Reciprocal 'flipping'; underlies substrate recognition and catalytic
RT activation by the human 8-oxo-guanine DNA glycosylase.";
RL J. Mol. Biol. 317:171-177(2002).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 12-327 OF MUTANTS ASN-268; GLU-268
RP AND GLN-268 IN COMPLEX WITH DNA, AND MUTAGENESIS OF ASP-268.
RX PubMed=12578369; DOI=10.1021/bi026823d;
RA Norman D.P.G., Chung S.J., Verdine G.L.;
RT "Structural and biochemical exploration of a critical amino acid in human
RT 8-oxoguanine glycosylase.";
RL Biochemistry 42:1564-1572(2003).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 12-327 IN COMPLEX WITH DNA AND
RP 8-OXO-GUANINE.
RX PubMed=12592398; DOI=10.1038/nsb902;
RA Fromme J.C., Bruner S.D., Yang W., Karplus M., Verdine G.L.;
RT "Product-assisted catalysis in base-excision DNA repair.";
RL Nat. Struct. Biol. 10:204-211(2003).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 12-325 OF MUTANT GLU-268 IN
RP COMPLEX WITH DNA.
RX PubMed=15610848; DOI=10.1016/j.chembiol.2004.09.014;
RA Chung S.J., Verdine G.L.;
RT "Structures of end products resulting from lesion processing by a DNA
RT glycosylase/lyase.";
RL Chem. Biol. 11:1643-1649(2004).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) OF 12-327 OF MUTANTS
RP ALA-42/ALA-270/ALA-315/PHE-315 IN COMPLEXES WITH DNA.
RX PubMed=17114185; DOI=10.1074/jbc.m608989200;
RA Radom C.T., Banerjee A., Verdine G.L.;
RT "Structural characterization of human 8-oxoguanine DNA glycosylase variants
RT bearing active site mutations.";
RL J. Biol. Chem. 282:9182-9194(2007).
RN [24]
RP VARIANT HIS-154.
RX PubMed=9765618; DOI=10.1111/j.1349-7006.1998.tb00635.x;
RA Shinmura K., Kohno T., Kasai H., Koda K., Sugimura H., Yokota J.;
RT "Infrequent mutations of the hOGG1 gene, that is involved in the excision
RT of 8-hydroxyguanine in damaged DNA, in human gastric cancer.";
RL Jpn. J. Cancer Res. 89:825-828(1998).
RN [25]
RP VARIANTS SER-85; GLN-131 AND THR-232, AND CHARACTERIZATION OF VARIANT
RP GLN-131.
RX PubMed=9662341; DOI=10.1038/sj.onc.1202096;
RA Chevillard S., Radicella J.P., Levalois C., Lebeau J., Poupon M.-F.,
RA Oudard S., Dutrillaux B., Boiteux S.;
RT "Mutations in OGG1, a gene involved in the repair of oxidative DNA damage,
RT are found in human lung and kidney tumours.";
RL Oncogene 16:3083-3086(1998).
RN [26]
RP CHARACTERIZATION OF VARIANT CYS-326.
RX PubMed=10497264; DOI=10.1093/nar/27.20.4001;
RA Dherin C., Radicella J.P., Dizdaroglu M., Boiteux S.;
RT "Excision of oxidatively damaged DNA bases by the human alpha-hOgg1 protein
RT and the polymorphic alpha-hOgg1(Ser326Cys) protein which is frequently
RT found in human populations.";
RL Nucleic Acids Res. 27:4001-4007(1999).
RN [27]
RP CHARACTERIZATION OF VARIANTS GLN-46 AND HIS-154.
RX PubMed=10908322; DOI=10.1093/nar/28.14.2672;
RA Audebert M., Radicella J.P., Dizdaroglu M.;
RT "Effect of single mutations in the OGG1 gene found in human tumors on the
RT substrate specificity of the ogg1 protein.";
RL Nucleic Acids Res. 28:2672-2678(2000).
RN [28]
RP CHARACTERIZATION OF VARIANT GLU-12.
RX PubMed=12509224; DOI=10.1016/s1568-7864(02)00034-4;
RA Audebert M., Charbonnier J.-B., Boiteux S., Radicella J.P.;
RT "Mitochondrial targeting of human 8-oxoguanine DNA glycosylase hOGG1 is
RT impaired by a somatic mutation found in kidney cancer.";
RL DNA Repair 1:497-505(2002).
CC -!- FUNCTION: DNA repair enzyme that incises DNA at 8-oxoG residues.
CC Excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-
CC methylformamidopyrimidine (FAPY) from damaged DNA. Has a beta-lyase
CC activity that nicks DNA 3' to the lesion.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-
CC deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-
CC dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-
CC 2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-
CC COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695,
CC ChEBI:CHEBI:167181; EC=4.2.99.18;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:17148573}. Nucleus speckle
CC {ECO:0000269|PubMed:17148573}. Nucleus matrix
CC {ECO:0000269|PubMed:17148573}. Note=Together with APEX1 is recruited to
CC nuclear speckles in UVA-irradiated cells.
CC -!- SUBCELLULAR LOCATION: [Isoform 1A]: Nucleus.
CC -!- SUBCELLULAR LOCATION: [Isoform 2A]: Mitochondrion.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1A; Synonyms=Alpha;
CC IsoId=O15527-1; Sequence=Displayed;
CC Name=1B;
CC IsoId=O15527-2; Sequence=VSP_003746;
CC Name=1C;
CC IsoId=O15527-3; Sequence=VSP_003747;
CC Name=2A; Synonyms=Beta;
CC IsoId=O15527-4; Sequence=VSP_003748;
CC Name=2B;
CC IsoId=O15527-5; Sequence=VSP_003749;
CC Name=2C;
CC IsoId=O15527-6; Sequence=VSP_003750, VSP_003751;
CC Name=2D;
CC IsoId=O15527-7; Sequence=VSP_003752;
CC Name=2E;
CC IsoId=O15527-8; Sequence=VSP_003753;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DISEASE: Renal cell carcinoma (RCC) [MIM:144700]: Renal cell carcinoma
CC is a heterogeneous group of sporadic or hereditary carcinoma derived
CC from cells of the proximal renal tubular epithelium. It is
CC subclassified into clear cell renal carcinoma (non-papillary
CC carcinoma), papillary renal cell carcinoma, chromophobe renal cell
CC carcinoma, collecting duct carcinoma with medullary carcinoma of the
CC kidney, and unclassified renal cell carcinoma. Clear cell renal cell
CC carcinoma is the most common subtype. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the type-1 OGG1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB84013.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/ogg1/";
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DR EMBL; U88527; AAB68614.1; -; mRNA.
DR EMBL; U88620; AAB68615.1; -; mRNA.
DR EMBL; U96710; AAB81132.1; -; mRNA.
DR EMBL; Y13277; CAA73726.1; -; mRNA.
DR EMBL; Y11731; CAA72414.1; -; mRNA.
DR EMBL; AF003595; AAB61340.1; -; mRNA.
DR EMBL; AB000410; BAA19103.1; -; mRNA.
DR EMBL; AF026691; AAB84013.1; ALT_INIT; mRNA.
DR EMBL; Y11838; CAA72536.1; -; mRNA.
DR EMBL; AJ131341; CAA10351.1; -; Genomic_DNA.
DR EMBL; AF088282; AAD41680.1; -; Genomic_DNA.
DR EMBL; AF088282; AAD41681.1; -; Genomic_DNA.
DR EMBL; AF088282; AAD41682.1; -; Genomic_DNA.
DR EMBL; AB019528; BAA76635.1; -; mRNA.
DR EMBL; AB019529; BAA76636.1; -; mRNA.
DR EMBL; AB019530; BAA76637.1; -; mRNA.
DR EMBL; AB019531; BAA76638.1; -; mRNA.
DR EMBL; AB019532; BAA76639.1; -; mRNA.
DR EMBL; AK289858; BAF82547.1; -; mRNA.
DR EMBL; AF521807; AAM74236.1; -; Genomic_DNA.
DR EMBL; AC022382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000657; AAH00657.1; -; mRNA.
DR CCDS; CCDS2576.1; -. [O15527-4]
DR CCDS; CCDS2577.1; -. [O15527-5]
DR CCDS; CCDS2578.1; -. [O15527-6]
DR CCDS; CCDS2579.1; -. [O15527-7]
DR CCDS; CCDS2580.1; -. [O15527-3]
DR CCDS; CCDS2581.1; -. [O15527-1]
DR CCDS; CCDS43046.1; -. [O15527-2]
DR CCDS; CCDS46742.1; -. [O15527-8]
DR PIR; T45069; T45069.
DR RefSeq; NP_002533.1; NM_002542.5. [O15527-1]
DR RefSeq; NP_058212.1; NM_016819.3. [O15527-2]
DR RefSeq; NP_058213.1; NM_016820.3. [O15527-3]
DR RefSeq; NP_058214.1; NM_016821.2. [O15527-4]
DR RefSeq; NP_058434.1; NM_016826.2. [O15527-5]
DR RefSeq; NP_058436.1; NM_016827.2. [O15527-6]
DR RefSeq; NP_058437.1; NM_016828.2. [O15527-7]
DR RefSeq; NP_058438.1; NM_016829.2. [O15527-8]
DR PDB; 1EBM; X-ray; 2.10 A; A=12-325.
DR PDB; 1FN7; X-ray; 2.60 A; A=12-325.
DR PDB; 1HU0; X-ray; 2.35 A; A=12-327.
DR PDB; 1KO9; X-ray; 2.15 A; A=1-345.
DR PDB; 1LWV; X-ray; 2.30 A; A=12-327.
DR PDB; 1LWW; X-ray; 2.10 A; A=12-327.
DR PDB; 1LWY; X-ray; 2.01 A; A=12-327.
DR PDB; 1M3H; X-ray; 2.05 A; A=12-325.
DR PDB; 1M3Q; X-ray; 1.90 A; A=12-325.
DR PDB; 1N39; X-ray; 2.20 A; A=12-325.
DR PDB; 1N3A; X-ray; 2.20 A; A=12-325.
DR PDB; 1N3C; X-ray; 2.70 A; A=12-325.
DR PDB; 1YQK; X-ray; 2.50 A; A=12-327.
DR PDB; 1YQL; X-ray; 2.60 A; A=12-327.
DR PDB; 1YQM; X-ray; 2.50 A; A=12-327.
DR PDB; 1YQR; X-ray; 2.43 A; A=12-327.
DR PDB; 2I5W; X-ray; 2.60 A; A=12-323.
DR PDB; 2NOB; X-ray; 2.10 A; A=12-327.
DR PDB; 2NOE; X-ray; 2.20 A; A=12-327.
DR PDB; 2NOF; X-ray; 2.35 A; A=12-327.
DR PDB; 2NOH; X-ray; 2.01 A; A=12-327.
DR PDB; 2NOI; X-ray; 2.35 A; A=12-327.
DR PDB; 2NOL; X-ray; 2.57 A; A=12-327.
DR PDB; 2NOZ; X-ray; 2.43 A; A=12-327.
DR PDB; 2XHI; X-ray; 1.55 A; A=1-345.
DR PDB; 3IH7; X-ray; 3.10 A; A=12-325.
DR PDB; 3KTU; X-ray; 2.30 A; A=12-325.
DR PDB; 5AN4; X-ray; 1.60 A; A=12-323.
DR PDB; 6RLW; X-ray; 2.00 A; AAA/BBB/CCC/DDD/EEE=11-327.
DR PDB; 6W0M; X-ray; 2.37 A; A=12-325.
DR PDB; 6W0R; X-ray; 2.35 A; A=12-323.
DR PDB; 6W13; X-ray; 2.38 A; A=12-325.
DR PDB; 7AYY; X-ray; 2.00 A; AAA/BBB/CCC/DDD/EEE=11-327.
DR PDBsum; 1EBM; -.
DR PDBsum; 1FN7; -.
DR PDBsum; 1HU0; -.
DR PDBsum; 1KO9; -.
DR PDBsum; 1LWV; -.
DR PDBsum; 1LWW; -.
DR PDBsum; 1LWY; -.
DR PDBsum; 1M3H; -.
DR PDBsum; 1M3Q; -.
DR PDBsum; 1N39; -.
DR PDBsum; 1N3A; -.
DR PDBsum; 1N3C; -.
DR PDBsum; 1YQK; -.
DR PDBsum; 1YQL; -.
DR PDBsum; 1YQM; -.
DR PDBsum; 1YQR; -.
DR PDBsum; 2I5W; -.
DR PDBsum; 2NOB; -.
DR PDBsum; 2NOE; -.
DR PDBsum; 2NOF; -.
DR PDBsum; 2NOH; -.
DR PDBsum; 2NOI; -.
DR PDBsum; 2NOL; -.
DR PDBsum; 2NOZ; -.
DR PDBsum; 2XHI; -.
DR PDBsum; 3IH7; -.
DR PDBsum; 3KTU; -.
DR PDBsum; 5AN4; -.
DR PDBsum; 6RLW; -.
DR PDBsum; 6W0M; -.
DR PDBsum; 6W0R; -.
DR PDBsum; 6W13; -.
DR PDBsum; 7AYY; -.
DR AlphaFoldDB; O15527; -.
DR SMR; O15527; -.
DR BioGRID; 111018; 15.
DR IntAct; O15527; 6.
DR MINT; O15527; -.
DR STRING; 9606.ENSP00000306561; -.
DR BindingDB; O15527; -.
DR ChEMBL; CHEMBL3396944; -.
DR iPTMnet; O15527; -.
DR PhosphoSitePlus; O15527; -.
DR BioMuta; OGG1; -.
DR EPD; O15527; -.
DR jPOST; O15527; -.
DR MassIVE; O15527; -.
DR MaxQB; O15527; -.
DR PaxDb; 9606-ENSP00000306561; -.
DR PeptideAtlas; O15527; -.
DR ProteomicsDB; 48726; -. [O15527-1]
DR ProteomicsDB; 48727; -. [O15527-2]
DR ProteomicsDB; 48728; -. [O15527-3]
DR ProteomicsDB; 48729; -. [O15527-4]
DR ProteomicsDB; 48730; -. [O15527-5]
DR ProteomicsDB; 48731; -. [O15527-6]
DR ProteomicsDB; 48732; -. [O15527-7]
DR ProteomicsDB; 48733; -. [O15527-8]
DR Pumba; O15527; -.
DR Antibodypedia; 25518; 542 antibodies from 39 providers.
DR CPTC; O15527; 1 antibody.
DR DNASU; 4968; -.
DR Ensembl; ENST00000302003.11; ENSP00000305584.7; ENSG00000114026.22. [O15527-3]
DR Ensembl; ENST00000302008.12; ENSP00000305527.8; ENSG00000114026.22. [O15527-7]
DR Ensembl; ENST00000302036.12; ENSP00000306561.7; ENSG00000114026.22. [O15527-4]
DR Ensembl; ENST00000339511.9; ENSP00000345520.5; ENSG00000114026.22. [O15527-2]
DR Ensembl; ENST00000344629.12; ENSP00000342851.7; ENSG00000114026.22. [O15527-1]
DR Ensembl; ENST00000352937.6; ENSP00000344899.6; ENSG00000114026.22. [O15527-5]
DR Ensembl; ENST00000383826.9; ENSP00000373337.5; ENSG00000114026.22. [O15527-6]
DR Ensembl; ENST00000449570.6; ENSP00000403598.2; ENSG00000114026.22. [O15527-8]
DR GeneID; 4968; -.
DR KEGG; hsa:4968; -.
DR MANE-Select; ENST00000344629.12; ENSP00000342851.7; NM_002542.6; NP_002533.1.
DR UCSC; uc003bsh.4; human. [O15527-1]
DR AGR; HGNC:8125; -.
DR CTD; 4968; -.
DR DisGeNET; 4968; -.
DR GeneCards; OGG1; -.
DR HGNC; HGNC:8125; OGG1.
DR HPA; ENSG00000114026; Low tissue specificity.
DR MalaCards; OGG1; -.
DR MIM; 144700; phenotype.
DR MIM; 601982; gene.
DR neXtProt; NX_O15527; -.
DR OpenTargets; ENSG00000114026; -.
DR Orphanet; 422526; Hereditary clear cell renal cell carcinoma.
DR PharmGKB; PA31912; -.
DR VEuPathDB; HostDB:ENSG00000114026; -.
DR eggNOG; KOG2875; Eukaryota.
DR GeneTree; ENSGT00640000091554; -.
DR HOGENOM; CLU_027543_1_1_1; -.
DR InParanoid; O15527; -.
DR OMA; GYAQEYL; -.
DR OrthoDB; 118473at2759; -.
DR PhylomeDB; O15527; -.
DR TreeFam; TF323702; -.
DR BRENDA; 3.2.2.23; 2681.
DR BRENDA; 4.2.99.18; 2681.
DR PathwayCommons; O15527; -.
DR Reactome; R-HSA-110328; Recognition and association of DNA glycosylase with site containing an affected pyrimidine.
DR Reactome; R-HSA-110329; Cleavage of the damaged pyrimidine.
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 Reactome; R-HSA-5649702; APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway.
DR Reactome; R-HSA-9656255; Defective OGG1 Substrate Binding.
DR Reactome; R-HSA-9656256; Defective OGG1 Substrate Processing.
DR Reactome; R-HSA-9657050; Defective OGG1 Localization. [O15527-4]
DR SignaLink; O15527; -.
DR SIGNOR; O15527; -.
DR BioGRID-ORCS; 4968; 19 hits in 1165 CRISPR screens.
DR ChiTaRS; OGG1; human.
DR EvolutionaryTrace; O15527; -.
DR GeneWiki; Oxoguanine_glycosylase; -.
DR GenomeRNAi; 4968; -.
DR Pharos; O15527; Tchem.
DR PRO; PR:O15527; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O15527; Protein.
DR Bgee; ENSG00000114026; Expressed in cortical plate and 202 other cell types or tissues.
DR ExpressionAtlas; O15527; baseline and differential.
DR Genevisible; O15527; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0034039; F:8-oxo-7,8-dihydroguanine DNA N-glycosylase activity; IMP:CACAO.
DR GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB.
DR GO; GO:0004519; F:endonuclease activity; TAS:ProtInc.
DR GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
DR GO; GO:0032357; F:oxidized purine DNA binding; IDA:UniProtKB.
DR GO; GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; TAS:Reactome.
DR GO; GO:0006284; P:base-excision repair; TAS:ProtInc.
DR GO; GO:0006285; P:base-excision repair, AP site formation; IBA:GO_Central.
DR GO; GO:0071276; P:cellular response to cadmium ion; IEA:Ensembl.
DR GO; GO:0045007; P:depurination; TAS:Reactome.
DR GO; GO:0045008; P:depyrimidination; TAS:Reactome.
DR GO; GO:0006974; P:DNA damage response; IGI:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:1901291; P:negative regulation of double-strand break repair via single-strand annealing; IDA:MGI.
DR GO; GO:0006289; P:nucleotide-excision repair; IDA:MGI.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:UniProtKB.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0051593; P:response to folic acid; IEA:Ensembl.
DR GO; GO:0009416; P:response to light stimulus; IEA:Ensembl.
DR GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
DR GO; GO:0009314; P:response to radiation; IDA:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR CDD; cd00056; ENDO3c; 1.
DR Gene3D; 3.30.310.40; -; 1.
DR Gene3D; 1.10.1670.10; Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal); 1.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR003265; HhH-GPD_domain.
DR InterPro; IPR023170; HhH_base_excis_C.
DR InterPro; IPR004577; Ogg1.
DR InterPro; IPR012904; OGG_N.
DR NCBIfam; TIGR00588; ogg; 1.
DR PANTHER; PTHR10242; 8-OXOGUANINE DNA GLYCOSYLASE; 1.
DR PANTHER; PTHR10242:SF2; N-GLYCOSYLASE_DNA LYASE; 1.
DR Pfam; PF00730; HhH-GPD; 1.
DR Pfam; PF07934; OGG_N; 1.
DR SMART; SM00478; ENDO3c; 1.
DR SUPFAM; SSF48150; DNA-glycosylase; 1.
DR SUPFAM; SSF55945; TATA-box binding protein-like; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA damage; DNA repair; Glycosidase;
KW Hydrolase; Lyase; Mitochondrion; Multifunctional enzyme; Nucleus;
KW Reference proteome.
FT CHAIN 1..345
FT /note="N-glycosylase/DNA lyase"
FT /id="PRO_0000058591"
FT REGION 324..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 249
FT /note="Schiff-base intermediate with DNA"
FT /evidence="ECO:0000269|PubMed:9197244"
FT BINDING 149
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000269|PubMed:10706276,
FT ECO:0000269|PubMed:11902834, ECO:0000269|PubMed:12578369,
FT ECO:0000269|PubMed:12592398, ECO:0000269|PubMed:15610848"
FT BINDING 154
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000269|PubMed:10706276,
FT ECO:0000269|PubMed:11902834, ECO:0000269|PubMed:12578369,
FT ECO:0000269|PubMed:12592398, ECO:0000269|PubMed:15610848"
FT BINDING 204
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000269|PubMed:10706276,
FT ECO:0000269|PubMed:11902834, ECO:0000269|PubMed:12578369,
FT ECO:0000269|PubMed:12592398, ECO:0000269|PubMed:15610848"
FT BINDING 266
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT BINDING 268
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT BINDING 270
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000269|PubMed:10706276,
FT ECO:0000269|PubMed:11902834, ECO:0000269|PubMed:12578369,
FT ECO:0000269|PubMed:12592398, ECO:0000269|PubMed:15610848"
FT BINDING 287
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000269|PubMed:10706276,
FT ECO:0000269|PubMed:11902834, ECO:0000269|PubMed:12578369,
FT ECO:0000269|PubMed:12592398, ECO:0000269|PubMed:15610848"
FT BINDING 315
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT BINDING 319
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT VAR_SEQ 191..195
FT /note="EVEAH -> PWQCI (in isoform 2C)"
FT /evidence="ECO:0000305"
FT /id="VSP_003750"
FT VAR_SEQ 196..345
FT /note="Missing (in isoform 2C)"
FT /evidence="ECO:0000305"
FT /id="VSP_003751"
FT VAR_SEQ 250..345
FT /note="VADCICLMALDKPQAVPVDVHMWHIAQRDYSWHPTTSQAKGPSPQTNKELGN
FT FFRSLWGPYAGWAQAVLFSADLRQSRHAQEPPAKRRKGSKGPEG -> GLLGNAFDGHQ
FT LLRPLIFCQDHLREGPPIGRGDSQGEELEPQLPSSLSSIPYGFCDHCWTKDVDDPPLVT
FT HPSPGSRDGHMTQAWPVKVVSPLATVIGHVMQASLLAL (in isoform 2B)"
FT /evidence="ECO:0000305"
FT /id="VSP_003749"
FT VAR_SEQ 317..345
FT /note="VLFSADLRQSRHAQEPPAKRRKGSKGPEG -> VSVPRCPP (in
FT isoform 1B)"
FT /evidence="ECO:0000303|PubMed:9187114"
FT /id="VSP_003746"
FT VAR_SEQ 317..345
FT /note="VLFSADLRQSRHAQEPPAKRRKGSKGPEG -> TPPSYRCCSVPTCANPAML
FT RSHQQSAERVPKGRKARWGTLDKEIPQAPSPPFPTSLSPSPPSLMLGRGLPVTTSKARH
FT PQIKQSVCTTRWGGGY (in isoform 1C)"
FT /evidence="ECO:0000305"
FT /id="VSP_003747"
FT VAR_SEQ 317..345
FT /note="VLFSADLRQSRHAQEPPAKRRKGSKGPEG -> GLLGNAFDGHQLLRPLIFC
FT QDHLREGPPIGRGDSQGEELEPQLPSSLSSIPYGFCDHCWTKDVDDPPLVTHPSPGSRD
FT GHMTQAWPVKVVSPLATVIGHVMQASLLAL (in isoform 2A)"
FT /evidence="ECO:0000303|PubMed:9187114,
FT ECO:0000303|PubMed:9223306"
FT /id="VSP_003748"
FT VAR_SEQ 317..345
FT /note="VLFSADLRQSRHAQEPPAKRRKGSKGPEG -> LCQVITTFMTFLGPHRLDQ
FT MPPEELQTSSSRLGGPPWQCI (in isoform 2D)"
FT /evidence="ECO:0000305"
FT /id="VSP_003752"
FT VAR_SEQ 317..345
FT /note="VLFSADLRQSRHAQEPPAKRRKGSKGPEG -> AGSDAS (in isoform
FT 2E)"
FT /evidence="ECO:0000305"
FT /id="VSP_003753"
FT VARIANT 12
FT /note="G -> E (found in a kidney cancer sample; no effect
FT on activity; abolishes mitochondrial localization;
FT dbSNP:rs772520254)"
FT /evidence="ECO:0000269|PubMed:12509224"
FT /id="VAR_024831"
FT VARIANT 46
FT /note="R -> Q (found in a clear cell renal cell carcinoma
FT sample; somatic mutation; diminished activity;
FT dbSNP:rs104893751)"
FT /evidence="ECO:0000269|PubMed:10908322"
FT /id="VAR_009519"
FT VARIANT 85
FT /note="A -> S (found in a lung cancer sample;
FT dbSNP:rs17050550)"
FT /evidence="ECO:0000269|PubMed:9662341"
FT /id="VAR_024832"
FT VARIANT 131
FT /note="R -> Q (found in a lung cancer sample; loss of
FT activity; dbSNP:rs747638147)"
FT /evidence="ECO:0000269|PubMed:9662341"
FT /id="VAR_024833"
FT VARIANT 154
FT /note="R -> H (found in a gastric cancer sample; no effect
FT on base-excision activity; alters substrate specificity and
FT strongly increases mutagenic mis-repair; dbSNP:rs56053615)"
FT /evidence="ECO:0000269|PubMed:10706276,
FT ECO:0000269|PubMed:10908322, ECO:0000269|PubMed:9765618"
FT /id="VAR_009520"
FT VARIANT 229
FT /note="R -> Q (in dbSNP:rs1805373)"
FT /evidence="ECO:0000269|Ref.13"
FT /id="VAR_014487"
FT VARIANT 232
FT /note="S -> T (found in a kidney cancer sample)"
FT /evidence="ECO:0000269|PubMed:9662341"
FT /id="VAR_024834"
FT VARIANT 288
FT /note="A -> V (in dbSNP:rs3219012)"
FT /evidence="ECO:0000269|Ref.13"
FT /id="VAR_018890"
FT VARIANT 320
FT /note="S -> T (in dbSNP:rs1801128)"
FT /id="VAR_014488"
FT VARIANT 322
FT /note="D -> N (in dbSNP:rs3219014)"
FT /evidence="ECO:0000269|Ref.13"
FT /id="VAR_018891"
FT VARIANT 326
FT /note="S -> C (in dbSNP:rs1052133)"
FT /evidence="ECO:0000269|PubMed:10497264,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.13"
FT /id="VAR_009521"
FT MUTAGEN 249
FT /note="K->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9197244"
FT MUTAGEN 268
FT /note="D->E,Q: No effect on activity."
FT /evidence="ECO:0000269|PubMed:12578369"
FT MUTAGEN 268
FT /note="D->N: Decreases activity about 65-fold."
FT /evidence="ECO:0000269|PubMed:12578369"
FT CONFLICT 47
FT /note="W -> WW (in Ref. 9; CAA10351)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="G -> E (in Ref. 9; CAA10351)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="A -> ATPPSLQ (in Ref. 2; AAB81132)"
FT /evidence="ECO:0000305"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:1EBM"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:2XHI"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:2XHI"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:2XHI"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:2XHI"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:2XHI"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:2XHI"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:2XHI"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:2XHI"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:2XHI"
FT STRAND 70..78
FT /evidence="ECO:0007829|PDB:2XHI"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:2XHI"
FT HELIX 90..99
FT /evidence="ECO:0007829|PDB:2XHI"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:2XHI"
FT HELIX 106..116
FT /evidence="ECO:0007829|PDB:2XHI"
FT HELIX 118..126
FT /evidence="ECO:0007829|PDB:2XHI"
FT HELIX 137..145
FT /evidence="ECO:0007829|PDB:2XHI"
FT TURN 146..149
FT /evidence="ECO:0007829|PDB:2XHI"
FT HELIX 152..166
FT /evidence="ECO:0007829|PDB:2XHI"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:2XHI"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:2XHI"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:2XHI"
FT HELIX 192..198
FT /evidence="ECO:0007829|PDB:2XHI"
FT HELIX 204..217
FT /evidence="ECO:0007829|PDB:2XHI"
FT HELIX 222..226
FT /evidence="ECO:0007829|PDB:2XHI"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:2XHI"
FT HELIX 233..240
FT /evidence="ECO:0007829|PDB:2XHI"
FT HELIX 248..258
FT /evidence="ECO:0007829|PDB:2XHI"
FT HELIX 269..279
FT /evidence="ECO:0007829|PDB:2XHI"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:5AN4"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:1M3Q"
FT HELIX 293..307
FT /evidence="ECO:0007829|PDB:2XHI"
FT HELIX 311..323
FT /evidence="ECO:0007829|PDB:2XHI"
SQ SEQUENCE 345 AA; 38782 MW; C284106ADEEC1FDD CRC64;
MPARALLPRR MGHRTLASTP ALWASIPCPR SELRLDLVLP SGQSFRWREQ SPAHWSGVLA
DQVWTLTQTE EQLHCTVYRG DKSQASRPTP DELEAVRKYF QLDVTLAQLY HHWGSVDSHF
QEVAQKFQGV RLLRQDPIEC LFSFICSSNN NIARITGMVE RLCQAFGPRL IQLDDVTYHG
FPSLQALAGP EVEAHLRKLG LGYRARYVSA SARAILEEQG GLAWLQQLRE SSYEEAHKAL
CILPGVGTKV ADCICLMALD KPQAVPVDVH MWHIAQRDYS WHPTTSQAKG PSPQTNKELG
NFFRSLWGPY AGWAQAVLFS ADLRQSRHAQ EPPAKRRKGS KGPEG
//
