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Endonuclease 8-like 1 (EC 3.2.2.-) (EC 4.2.99.18) (DNA glycosylase/AP lyase Neil1) (DNA-(apurinic or apyrimidinic site) lyase Neil1) (Endonuclease VIII-like 1) (FPG1) (Nei homolog 1) (NEH1) (Nei-like protein 1)

 NEIL1_HUMAN             Reviewed;         390 AA.
Q96FI4; D3DW75; Q6ZRA7; Q86XW7; Q9H6C3;
07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
23-MAY-2018, entry version 153.
RecName: Full=Endonuclease 8-like 1;
EC=3.2.2.-;
EC=4.2.99.18;
AltName: Full=DNA glycosylase/AP lyase Neil1;
AltName: Full=DNA-(apurinic or apyrimidinic site) lyase Neil1;
AltName: Full=Endonuclease VIII-like 1;
AltName: Full=FPG1;
AltName: Full=Nei homolog 1;
Short=NEH1;
AltName: Full=Nei-like protein 1;
Name=NEIL1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
TISSUE=Testis;
PubMed=12200441; DOI=10.1074/jbc.M206884200;
Takao M., Kanno S., Kobayashi K., Zhang Q.-M., Yonei S.,
van der Horst G.T.J., Yasui A.;
"A back-up glycosylase in Nth1 knock-out mice is a functional Nei
(endonuclease VIII) homologue.";
J. Biol. Chem. 277:42205-42213(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-82; ASP-83;
ARG-136 AND ASN-252.
NIEHS SNPs program;
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
MUTAGENESIS OF PRO-2 AND GLU-3, AND FUNCTION.
PubMed=12509226; DOI=10.1016/S1568-7864(02)00036-8;
Bandaru V., Sunkara S., Wallace S.S., Bond J.P.;
"A novel human DNA glycosylase that removes oxidative DNA damage and
is homologous to Escherichia coli endonuclease VIII.";
DNA Repair 1:517-529(2002).
[8]
MUTAGENESIS OF PRO-2, FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
PubMed=11904416; DOI=10.1073/pnas.062053799;
Hazra T.K., Izumi T., Boldogh I., Imhoff B., Kow Y.W., Jaruga P.,
Dizdaroglu M., Mitra S.;
"Identification and characterization of a human DNA glycosylase for
repair of modified bases in oxidatively damaged DNA.";
Proc. Natl. Acad. Sci. U.S.A. 99:3523-3528(2002).
[9]
FUNCTION, AND MUTAGENESIS OF LYS-54.
PubMed=14522990; DOI=10.1074/jbc.M308658200;
Dou H., Mitra S., Hazra T.K.;
"Repair of oxidized bases in DNA bubble structures by human DNA
glycosylases NEIL1 and NEIL2.";
J. Biol. Chem. 278:49679-49684(2003).
[10]
SUBCELLULAR LOCATION.
PubMed=17556049; DOI=10.1016/j.dnarep.2007.04.008;
Hildrestrand G.A., Rolseth V., Bjoras M., Luna L.;
"Human NEIL1 localizes with the centrosomes and condensed chromosomes
during mitosis.";
DNA Repair 6:1425-1433(2007).
[11]
RNA EDITING OF POSITION 242.
PubMed=21068368; DOI=10.1073/pnas.1009231107;
Yeo J., Goodman R.A., Schirle N.T., David S.S., Beal P.A.;
"RNA editing changes the lesion specificity for the DNA repair enzyme
NEIL1.";
Proc. Natl. Acad. Sci. U.S.A. 107:20715-20719(2010).
[12]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-334, AND MUTAGENESIS OF
ARG-277.
PubMed=15232006; DOI=10.1073/pnas.0402051101;
Doublie S., Bandaru V., Bond J.P., Wallace S.S.;
"The crystal structure of human endonuclease VIII-like 1 (NEIL1)
reveals a zincless finger motif required for glycosylase activity.";
Proc. Natl. Acad. Sci. U.S.A. 101:10284-10289(2004).
[13]
VARIANTS GLN-159 AND LYS-181.
PubMed=21697813; DOI=10.1038/ki.2011.148;
Sanna-Cherchi S., Burgess K.E., Nees S.N., Caridi G., Weng P.L.,
Dagnino M., Bodria M., Carrea A., Allegretta M.A., Kim H.R.,
Perry B.J., Gigante M., Clark L.N., Kisselev S., Cusi D., Gesualdo L.,
Allegri L., Scolari F., D'Agati V., Shapiro L.S., Pecoraro C.,
Palomero T., Ghiggeri G.M., Gharavi A.G.;
"Exome sequencing identified MYO1E and NEIL1 as candidate genes for
human autosomal recessive steroid-resistant nephrotic syndrome.";
Kidney Int. 80:389-396(2011).
-!- FUNCTION: Involved in base excision repair of DNA damaged by
oxidation or by mutagenic agents. Acts as DNA glycosylase that
recognizes and removes damaged bases. Has a preference for
oxidized pyrimidines, such as thymine glycol, formamidopyrimidine
(Fapy) and 5-hydroxyuracil. Has marginal activity towards 8-
oxoguanine. Has AP (apurinic/apyrimidinic) lyase activity and
introduces nicks in the DNA strand. Cleaves the DNA backbone by
beta-delta elimination to generate a single-strand break at the
site of the removed base with both 3'- and 5'-phosphates. Has DNA
glycosylase/lyase activity towards mismatched uracil and thymine,
in particular in U:C and T:C mismatches. Specifically binds 5-
hydroxymethylcytosine (5hmC), suggesting that it acts as a
specific reader of 5hmC. {ECO:0000269|PubMed:11904416,
ECO:0000269|PubMed:12200441, ECO:0000269|PubMed:12509226,
ECO:0000269|PubMed:14522990}.
-!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
apyrimidinic site in DNA is broken by a beta-elimination reaction,
leaving a 3'-terminal unsaturated sugar and a product with a
terminal 5'-phosphate. {ECO:0000255|PROSITE-ProRule:PRU00392}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:17556049}.
Nucleus {ECO:0000269|PubMed:17556049}. Chromosome
{ECO:0000269|PubMed:17556049}. Note=During mitosis, associates
with centrosomes and condensed chromatin.
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11904416}.
-!- INDUCTION: Up-regulated during S-phase.
{ECO:0000269|PubMed:11904416}.
-!- RNA EDITING: Modified_positions=242 {ECO:0000269|PubMed:21068368};
Note=The edited form removes thymine glycol from duplex DNA 30
times more slowly than the form encoded in the genome, whereas
editing enhances repair of the guanidinohydantoin lesion by NEIL1.
The recoding site is a preferred editing site for the RNA editing
adenosine deaminase ADAR1.;
-!- SIMILARITY: Belongs to the FPG family. {ECO:0000255|PROSITE-
ProRule:PRU00392}.
-!- SEQUENCE CAUTION:
Sequence=AK128372; Type=Miscellaneous discrepancy; Note=Erroneous CDS prediction.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/NEIL1ID41519ch15q24.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/neil1/";
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EMBL; AB079068; BAC06476.1; -; mRNA.
EMBL; AK026055; BAB15337.1; -; mRNA.
EMBL; AK128372; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AY257544; AAO74826.1; -; Genomic_DNA.
EMBL; AC068338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471136; EAW99255.1; -; Genomic_DNA.
EMBL; CH471136; EAW99260.1; -; Genomic_DNA.
EMBL; BC010876; AAH10876.1; -; mRNA.
CCDS; CCDS10278.1; -.
RefSeq; NP_001243481.1; NM_001256552.1.
RefSeq; NP_078884.2; NM_024608.3.
RefSeq; XP_005254716.1; XM_005254659.4.
RefSeq; XP_006720743.1; XM_006720680.1.
RefSeq; XP_006720744.1; XM_006720681.1.
RefSeq; XP_011520304.1; XM_011522002.1.
RefSeq; XP_011520305.1; XM_011522003.2.
RefSeq; XP_011520306.1; XM_011522004.2.
UniGene; Hs.512732; -.
PDB; 1TDH; X-ray; 2.10 A; A=1-390.
PDB; 4NRV; X-ray; 2.60 A; A=2-290.
PDB; 5ITQ; X-ray; 1.48 A; A=1-290.
PDB; 5ITR; X-ray; 2.46 A; A/B/C=1-390.
PDB; 5ITT; X-ray; 2.53 A; A/B/C=1-390.
PDB; 5ITU; X-ray; 2.41 A; A/B/C=1-390.
PDB; 5ITX; X-ray; 2.65 A; A/B/E=1-390.
PDB; 5ITY; X-ray; 2.48 A; A/B/C=1-390.
PDBsum; 1TDH; -.
PDBsum; 4NRV; -.
PDBsum; 5ITQ; -.
PDBsum; 5ITR; -.
PDBsum; 5ITT; -.
PDBsum; 5ITU; -.
PDBsum; 5ITX; -.
PDBsum; 5ITY; -.
ProteinModelPortal; Q96FI4; -.
SMR; Q96FI4; -.
BioGrid; 122787; 5.
CORUM; Q96FI4; -.
STRING; 9606.ENSP00000347170; -.
DrugBank; DB03754; Tris.
iPTMnet; Q96FI4; -.
PhosphoSitePlus; Q96FI4; -.
BioMuta; NEIL1; -.
DMDM; 56404654; -.
PaxDb; Q96FI4; -.
PeptideAtlas; Q96FI4; -.
PRIDE; Q96FI4; -.
DNASU; 79661; -.
Ensembl; ENST00000355059; ENSP00000347170; ENSG00000140398.
Ensembl; ENST00000564784; ENSP00000457352; ENSG00000140398.
Ensembl; ENST00000569035; ENSP00000455730; ENSG00000140398.
GeneID; 79661; -.
KEGG; hsa:79661; -.
UCSC; uc002bad.5; human.
CTD; 79661; -.
DisGeNET; 79661; -.
EuPathDB; HostDB:ENSG00000140398.13; -.
GeneCards; NEIL1; -.
H-InvDB; HIX0202149; -.
HGNC; HGNC:18448; NEIL1.
HPA; HPA054084; -.
MIM; 608844; gene.
neXtProt; NX_Q96FI4; -.
OpenTargets; ENSG00000140398; -.
PharmGKB; PA38334; -.
eggNOG; ENOG410IEAW; Eukaryota.
eggNOG; ENOG410ZTEH; LUCA.
GeneTree; ENSGT00390000016671; -.
HOGENOM; HOG000067872; -.
HOVERGEN; HBG052592; -.
InParanoid; Q96FI4; -.
KO; K10567; -.
OMA; HLASHFV; -.
OrthoDB; EOG091G07LM; -.
PhylomeDB; Q96FI4; -.
TreeFam; TF333272; -.
Reactome; R-HSA-110328; Recognition and association of DNA glycosylase with site containing an affected pyrimidine.
Reactome; R-HSA-110329; Cleavage of the damaged pyrimidine.
Reactome; R-HSA-5649702; APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway.
SIGNOR; Q96FI4; -.
ChiTaRS; NEIL1; human.
EvolutionaryTrace; Q96FI4; -.
GeneWiki; NEIL1; -.
GenomeRNAi; 79661; -.
PRO; PR:Q96FI4; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000140398; -.
CleanEx; HS_NEIL1; -.
ExpressionAtlas; Q96FI4; baseline and differential.
Genevisible; Q96FI4; HS.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
GO; GO:0019104; F:DNA N-glycosylase activity; TAS:Reactome.
GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; TAS:Reactome.
GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IDA:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006284; P:base-excision repair; IDA:UniProtKB.
GO; GO:0045008; P:depyrimidination; TAS:Reactome.
GO; GO:0032074; P:negative regulation of nuclease activity; IDA:UniProtKB.
GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
Gene3D; 3.20.190.10; -; 1.
InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
InterPro; IPR015371; Endonuclease-VIII_DNA-bd.
InterPro; IPR012319; FPG_cat.
InterPro; IPR035937; MutM-like_N-ter.
InterPro; IPR010979; Ribosomal_S13-like_H2TH.
Pfam; PF01149; Fapy_DNA_glyco; 1.
Pfam; PF06831; H2TH; 1.
Pfam; PF09292; Neil1-DNA_bind; 1.
SMART; SM00898; Fapy_DNA_glyco; 1.
SMART; SM01232; H2TH; 1.
SUPFAM; SSF46946; SSF46946; 1.
SUPFAM; SSF81624; SSF81624; 1.
PROSITE; PS51068; FPG_CAT; 1.
1: Evidence at protein level;
3D-structure; Chromosome; Complete proteome; Cytoplasm; Cytoskeleton;
DNA damage; DNA repair; DNA-binding; Glycosidase; Hydrolase; Lyase;
Multifunctional enzyme; Nucleus; Polymorphism; Reference proteome;
RNA editing.
INIT_MET 1 1 Removed.
CHAIN 2 390 Endonuclease 8-like 1.
/FTId=PRO_0000170905.
ACT_SITE 2 2 Schiff-base intermediate with DNA.
{ECO:0000305}.
ACT_SITE 3 3 Proton donor. {ECO:0000305}.
ACT_SITE 54 54 Proton donor; for beta-elimination
activity. {ECO:0000305}.
ACT_SITE 339 339 Proton donor; for delta-elimination
activity. {ECO:0000305}.
BINDING 176 176 DNA. {ECO:0000250}.
BINDING 339 339 DNA. {ECO:0000250}.
VARIANT 82 82 S -> C (in dbSNP:rs5745905).
{ECO:0000269|Ref.3}.
/FTId=VAR_020580.
VARIANT 83 83 G -> D (in dbSNP:rs5745906).
{ECO:0000269|Ref.3}.
/FTId=VAR_020581.
VARIANT 136 136 C -> R (in dbSNP:rs5745907).
{ECO:0000269|Ref.3}.
/FTId=VAR_020582.
VARIANT 159 159 R -> Q (in dbSNP:rs769880000).
{ECO:0000269|PubMed:21697813}.
/FTId=VAR_065963.
VARIANT 181 181 E -> K (found in a patient with nephrotic
syndrome also carrying mutation P-159 in
MYO1E; dbSNP:rs749636951).
{ECO:0000269|PubMed:21697813}.
/FTId=VAR_065964.
VARIANT 182 182 I -> M (in dbSNP:rs7183491).
/FTId=VAR_020583.
VARIANT 242 242 K -> R (in RNA edited version).
/FTId=VAR_065018.
VARIANT 252 252 D -> N (in dbSNP:rs5745926).
{ECO:0000269|Ref.3}.
/FTId=VAR_020584.
MUTAGEN 2 2 P->T: Loss of glycosylase and AP lyase
activity. {ECO:0000269|PubMed:11904416,
ECO:0000269|PubMed:12509226}.
MUTAGEN 2 2 Missing: Loss of glycosylase activity.
{ECO:0000269|PubMed:11904416,
ECO:0000269|PubMed:12509226}.
MUTAGEN 3 3 E->Q: Loss of glycosylase and AP lyase
activity. {ECO:0000269|PubMed:12509226}.
MUTAGEN 54 54 K->L: Loss of glycosylase activity.
{ECO:0000269|PubMed:14522990}.
MUTAGEN 277 277 R->A: Strongly reduced glycosylase
activity. Has little effect on AP lyase
activity. {ECO:0000269|PubMed:15232006}.
CONFLICT 147 147 N -> S (in Ref. 2; BAB15337).
{ECO:0000305}.
HELIX 4 18 {ECO:0000244|PDB:5ITQ}.
STRAND 23 26 {ECO:0000244|PDB:5ITQ}.
STRAND 41 52 {ECO:0000244|PDB:5ITQ}.
STRAND 55 62 {ECO:0000244|PDB:5ITQ}.
STRAND 73 78 {ECO:0000244|PDB:5ITQ}.
TURN 80 82 {ECO:0000244|PDB:5ITQ}.
STRAND 83 89 {ECO:0000244|PDB:5ITQ}.
HELIX 90 92 {ECO:0000244|PDB:5ITQ}.
STRAND 97 103 {ECO:0000244|PDB:5ITQ}.
STRAND 105 107 {ECO:0000244|PDB:5ITQ}.
STRAND 110 116 {ECO:0000244|PDB:5ITQ}.
STRAND 122 127 {ECO:0000244|PDB:5ITQ}.
TURN 137 139 {ECO:0000244|PDB:5ITQ}.
HELIX 141 150 {ECO:0000244|PDB:5ITQ}.
TURN 151 153 {ECO:0000244|PDB:5ITQ}.
HELIX 155 158 {ECO:0000244|PDB:5ITQ}.
HELIX 161 164 {ECO:0000244|PDB:5ITQ}.
TURN 168 170 {ECO:0000244|PDB:5ITQ}.
HELIX 176 186 {ECO:0000244|PDB:5ITQ}.
HELIX 194 198 {ECO:0000244|PDB:5ITQ}.
HELIX 199 201 {ECO:0000244|PDB:5ITQ}.
HELIX 212 218 {ECO:0000244|PDB:5ITQ}.
TURN 219 221 {ECO:0000244|PDB:5ITQ}.
HELIX 225 240 {ECO:0000244|PDB:5ITQ}.
HELIX 243 245 {ECO:0000244|PDB:5ITU}.
HELIX 249 259 {ECO:0000244|PDB:5ITQ}.
STRAND 269 272 {ECO:0000244|PDB:5ITQ}.
STRAND 278 283 {ECO:0000244|PDB:5ITQ}.
SEQUENCE 390 AA; 43684 MW; B2B058486C4EF835 CRC64;
MPEGPELHLA SQFVNEACRA LVFGGCVEKS SVSRNPEVPF ESSAYRISAS ARGKELRLIL
SPLPGAQPQQ EPLALVFRFG MSGSFQLVPR EELPRHAHLR FYTAPPGPRL ALCFVDIRRF
GRWDLGGKWQ PGRGPCVLQE YQQFRENVLR NLADKAFDRP ICEALLDQRF FNGIGNYLRA
EILYRLKIPP FEKARSVLEA LQQHRPSPEL TLSQKIRTKL QNPDLLELCH SVPKEVVQLG
GKGYGSESGE EDFAAFRAWL RCYGMPGMSS LQDRHGRTIW FQGDPGPLAP KGRKSRKKKS
KATQLSPEDR VEDALPPSKA PSRTRRAKRD LPKRTATQRP EGTSLQQDPE APTVPKKGRR
KGRQAASGHC RPRKVKADIP SLEPEGTSAS


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