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/"; 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; 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 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. DR Genevisible; O15527; HS. 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 //