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Werner syndrome ATP-dependent helicase homolog (EC 3.6.4.12) (Exonuclease WRN) (EC 3.1.-.-)

 WRN_MOUSE               Reviewed;        1401 AA.
O09053; O09050; Q80YP9; Q9JKD4; Q9Z241; Q9Z242;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
22-NOV-2017, entry version 165.
RecName: Full=Werner syndrome ATP-dependent helicase homolog;
EC=3.6.4.12 {ECO:0000269|PubMed:17229737};
AltName: Full=Exonuclease WRN;
EC=3.1.-.-;
Name=Wrn;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=BALB/cJ; TISSUE=Spleen, and Testis;
PubMed=9143515; DOI=10.1006/geno.1997.4661;
Imamura O., Ichikawa K., Yamabe Y., Goto M., Sugawara M., Furuichi Y.;
"Cloning of a mouse homologue of the human Werner syndrome gene and
assignment to 8A4 by fluorescence in situ hybridization.";
Genomics 41:298-300(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Paeper B.W., Gayle M., Brady W., Swartz A., Gillett L.A., Alisch R.S.,
Mulligan J., Galas D., Fu Y.-H.;
"Genomic structure of the human Werner's gene and cloning of its mouse
homolog.";
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
TISSUE=Lymph node, and Spleen;
PubMed=10757812; DOI=10.1128/MCB.20.9.3286-3291.2000;
Lombard D.B., Beard C., Johnson B., Marciniak R.A., Dausman J.,
Bronson R., Buhlmann J.E., Lipman R., Curry R., Sharpe A.,
Jaenisch R., Guarente L.;
"Mutations in the WRN Gene in mice accelerate mortality in a p53-null
background.";
Mol. Cell. Biol. 20:3286-3291(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
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).
[6]
SUBCELLULAR LOCATION.
PubMed=9618508; DOI=10.1073/pnas.95.12.6887;
Marciniak R.A., Lombard D.B., Johnson F.B., Guarente L.;
"Nucleolar localization of the Werner syndrome protein in human
cells.";
Proc. Natl. Acad. Sci. U.S.A. 95:6887-6892(1998).
[7]
INTERACTION WITH WRNIP1.
PubMed=11301316; DOI=10.1074/jbc.C100035200;
Kawabe Y., Branzei D., Hayashi T., Suzuki H., Masuko T., Onoda F.,
Heo S.-J., Ikeda H., Shimamoto A., Furuichi Y., Seki M., Enomoto T.;
"A novel protein interacts with the Werner's syndrome gene product
physically and functionally.";
J. Biol. Chem. 276:20364-20369(2001).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 31-238 IN COMPLEX WITH ZINC
IONS AND SULFATE, SUBUNIT, FUNCTION, EXONUCLEASE ACTIVITY, ENZYME
REGULATION, CIRCULAR DICHROISM, AND MUTAGENESIS OF LYS-185; ARG-190
AND TYR-206.
PubMed=17229737; DOI=10.1074/jbc.M609657200;
Choi J.M., Kang S.Y., Bae W.J., Jin K.S., Ree M., Cho Y.;
"Probing the roles of active site residues in the 3'-5' exonuclease of
the Werner syndrome protein.";
J. Biol. Chem. 282:9941-9951(2007).
-!- FUNCTION: Multifunctional enzyme that has both magnesium and ATP-
dependent DNA-helicase activity and 3'->5' exonuclease activity
towards double-stranded DNA with a 5'-overhang. Has no nuclease
activity towards single-stranded DNA or blunt-ended double-
stranded DNA. Binds preferentially to DNA substrates containing
alternate secondary structures, such as replication forks and
Holliday junctions. May play an important role in the dissociation
of joint DNA molecules that can arise as products of homologous
recombination, at stalled replication forks or during DNA repair.
Alleviates stalling of DNA polymerases at the site of DNA lesions.
Important for genomic integrity. Plays a role in the formation of
DNA replication focal centers; stably associates with foci
elements generating binding sites for RP-A (By similarity). Plays
a role in double-strand break repair after gamma-irradiation (By
similarity). {ECO:0000250, ECO:0000269|PubMed:10757812,
ECO:0000269|PubMed:17229737}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000269|PubMed:17229737}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:17229737};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:17229737};
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:17229737};
Note=Binds 2 magnesium ions per subunit. Has high activity with
manganese and zinc ions (in vitro). {ECO:0000269|PubMed:17229737};
-!- ENZYME REGULATION: Zinc ions stimulate the exonuclease activity.
{ECO:0000269|PubMed:17229737}.
-!- SUBUNIT: Monomer, and homooligomer. May exist as homodimer,
homotrimer, homotetramer and/or homohexamer. Homotetramer, or
homohexamer, when bound to DNA. Interacts via its N-terminal
domain with WRNIP1. Interacts with PCNA; EXO1 and SUPV3L1 (By
similarity). Interacts with PML (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9618508}.
Nucleus, nucleolus {ECO:0000250}. Nucleus, nucleoplasm
{ECO:0000250}. Note=Gamma-irradiation leads to its translocation
from nucleoli to nucleoplasm and PML regulates the irradiation-
induced WRN relocation. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed ubiquitously in most organs at a low
level, highly expressed in testis, ovary and spleen.
{ECO:0000269|PubMed:10757812, ECO:0000269|PubMed:9143515}.
-!- PTM: Phosphorylated by PRKDC.
-!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
{ECO:0000305}.
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EMBL; D86527; BAA20270.1; -; mRNA.
EMBL; D86526; BAA20269.1; -; mRNA.
EMBL; AF091215; AAC78077.1; -; mRNA.
EMBL; AF091216; AAC72359.1; -; Genomic_DNA.
EMBL; AF241636; AAF64490.1; -; mRNA.
EMBL; AC153789; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC115809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC050921; AAH50921.1; -; mRNA.
EMBL; BC060700; AAH60700.1; -; mRNA.
CCDS; CCDS22229.1; -.
PIR; T17452; T17452.
PIR; T30247; T30247.
RefSeq; NP_001116294.1; NM_001122822.1.
RefSeq; NP_035851.3; NM_011721.4.
RefSeq; XP_006509154.1; XM_006509091.3.
RefSeq; XP_017168151.1; XM_017312662.1.
UniGene; Mm.228805; -.
PDB; 2E6L; X-ray; 2.20 A; A=31-238.
PDB; 2E6M; X-ray; 2.00 A; A=31-238.
PDBsum; 2E6L; -.
PDBsum; 2E6M; -.
ProteinModelPortal; O09053; -.
SMR; O09053; -.
DIP; DIP-27642N; -.
STRING; 10090.ENSMUSP00000033990; -.
iPTMnet; O09053; -.
PhosphoSitePlus; O09053; -.
MaxQB; O09053; -.
PaxDb; O09053; -.
PeptideAtlas; O09053; -.
PRIDE; O09053; -.
Ensembl; ENSMUST00000033990; ENSMUSP00000033990; ENSMUSG00000031583.
Ensembl; ENSMUST00000033991; ENSMUSP00000033991; ENSMUSG00000031583.
GeneID; 22427; -.
KEGG; mmu:22427; -.
UCSC; uc009ljw.1; mouse.
CTD; 7486; -.
MGI; MGI:109635; Wrn.
eggNOG; KOG0351; Eukaryota.
eggNOG; KOG4373; Eukaryota.
eggNOG; COG0514; LUCA.
GeneTree; ENSGT00550000074520; -.
HOGENOM; HOG000146447; -.
HOVERGEN; HBG000325; -.
InParanoid; O09053; -.
KO; K10900; -.
OMA; SHFEDKQ; -.
OrthoDB; EOG091G0B07; -.
TreeFam; TF312852; -.
Reactome; R-MMU-5685938; HDR through Single Strand Annealing (SSA).
Reactome; R-MMU-5685942; HDR through Homologous Recombination (HRR).
Reactome; R-MMU-5693554; Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
Reactome; R-MMU-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
Reactome; R-MMU-5693579; Homologous DNA Pairing and Strand Exchange.
Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
Reactome; R-MMU-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-MMU-69473; G2/M DNA damage checkpoint.
EvolutionaryTrace; O09053; -.
PRO; PR:O09053; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000031583; -.
CleanEx; MM_WRN; -.
ExpressionAtlas; O09053; baseline and differential.
Genevisible; O09053; MM.
GO; GO:0005813; C:centrosome; ISO:MGI.
GO; GO:0000781; C:chromosome, telomeric region; IMP:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0032389; C:MutLalpha complex; IEA:Ensembl.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0016607; C:nuclear speck; ISO:MGI.
GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005657; C:replication fork; IMP:BHF-UCL.
GO; GO:0043138; F:3'-5' DNA helicase activity; ISO:MGI.
GO; GO:0008408; F:3'-5' exonuclease activity; IDA:MGI.
GO; GO:0070337; F:3'-flap-structured DNA binding; ISO:MGI.
GO; GO:1905773; F:8-hydroxy-2'-deoxyguanosine DNA binding; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0043140; F:ATP-dependent 3'-5' DNA helicase activity; IBA:GO_Central.
GO; GO:0004003; F:ATP-dependent DNA helicase activity; ISO:MGI.
GO; GO:0016887; F:ATPase activity; ISO:MGI.
GO; GO:0000405; F:bubble DNA binding; ISO:MGI.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0003677; F:DNA binding; ISO:MGI.
GO; GO:0003678; F:DNA helicase activity; ISO:MGI.
GO; GO:0004527; F:exonuclease activity; ISO:MGI.
GO; GO:0061749; F:forked DNA-dependent helicase activity; ISO:MGI.
GO; GO:0000400; F:four-way junction DNA binding; ISO:MGI.
GO; GO:0009378; F:four-way junction helicase activity; ISO:MGI.
GO; GO:0051880; F:G-quadruplex DNA binding; ISO:MGI.
GO; GO:0004386; F:helicase activity; ISO:MGI.
GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
GO; GO:0032403; F:protein complex binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0061821; F:telomeric D-loop binding; ISO:MGI.
GO; GO:0000403; F:Y-form DNA binding; ISO:MGI.
GO; GO:0006284; P:base-excision repair; ISO:MGI.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0007569; P:cell aging; ISO:MGI.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
GO; GO:0071480; P:cellular response to gamma radiation; ISS:UniProtKB.
GO; GO:0009267; P:cellular response to starvation; ISO:MGI.
GO; GO:0032508; P:DNA duplex unwinding; ISO:MGI.
GO; GO:0006259; P:DNA metabolic process; IMP:MGI.
GO; GO:0006260; P:DNA replication; IMP:BHF-UCL.
GO; GO:0000731; P:DNA synthesis involved in DNA repair; ISO:MGI.
GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
GO; GO:0044806; P:G-quadruplex DNA unwinding; IMP:BHF-UCL.
GO; GO:0010259; P:multicellular organism aging; IGI:MGI.
GO; GO:0032066; P:nucleolus to nucleoplasm transport; ISO:MGI.
GO; GO:0051345; P:positive regulation of hydrolase activity; ISO:MGI.
GO; GO:0098530; P:positive regulation of strand invasion; ISO:MGI.
GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI.
GO; GO:0040009; P:regulation of growth rate; IMP:MGI.
GO; GO:0031297; P:replication fork processing; ISO:MGI.
GO; GO:0001302; P:replicative cell aging; IMP:MGI.
GO; GO:0006979; P:response to oxidative stress; ISO:MGI.
GO; GO:0010225; P:response to UV-C; ISO:MGI.
GO; GO:0000723; P:telomere maintenance; IMP:MGI.
GO; GO:0061820; P:telomeric D-loop disassembly; ISO:MGI.
CDD; cd00079; HELICc; 1.
Gene3D; 1.10.10.10; -; 1.
Gene3D; 3.30.420.10; -; 1.
InterPro; IPR002562; 3'-5'_exonuclease_dom.
InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR029491; Helicase_HTH.
InterPro; IPR010997; HRDC-like_sf.
InterPro; IPR002121; HRDC_dom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR032284; RecQ_Zn-bd.
InterPro; IPR012337; RNaseH-like_sf.
InterPro; IPR036397; RNaseH_sf.
InterPro; IPR018982; RQC_domain.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF00270; DEAD; 1.
Pfam; PF01612; DNA_pol_A_exo1; 1.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF00570; HRDC; 1.
Pfam; PF14493; HTH_40; 1.
Pfam; PF16124; RecQ_Zn_bind; 1.
Pfam; PF09382; RQC; 1.
SMART; SM00474; 35EXOc; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SMART; SM00341; HRDC; 1.
SMART; SM00956; RQC; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF47819; SSF47819; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF53098; SSF53098; 1.
TIGRFAMs; TIGR00614; recQ_fam; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS50967; HRDC; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome; DNA damage; DNA repair;
DNA-binding; Exonuclease; Helicase; Hydrolase; Isopeptide bond;
Magnesium; Metal-binding; Multifunctional enzyme; Nuclease;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
Ubl conjugation; Zinc.
CHAIN 1 1401 Werner syndrome ATP-dependent helicase
homolog.
/FTId=PRO_0000205046.
DOMAIN 51 223 3'-5' exonuclease.
DOMAIN 522 688 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 713 866 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 1115 1194 HRDC. {ECO:0000255|PROSITE-
ProRule:PRU00328}.
NP_BIND 535 542 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 1 271 Interaction with WRNIP1.
{ECO:0000269|PubMed:11301316}.
REGION 952 958 Interaction with DNA. {ECO:0000250}.
MOTIF 632 635 DEAH box.
COMPBIAS 1387 1390 Poly-Ser.
METAL 76 76 Magnesium 1; catalytic.
{ECO:0000244|PDB:2E6L,
ECO:0000269|PubMed:17229737}.
METAL 76 76 Magnesium 2; catalytic.
{ECO:0000244|PDB:2E6L,
ECO:0000269|PubMed:17229737}.
METAL 78 78 Magnesium 1; catalytic.
{ECO:0000244|PDB:2E6L,
ECO:0000269|PubMed:17229737}.
METAL 210 210 Magnesium 1; catalytic.
{ECO:0000244|PDB:2E6L,
ECO:0000269|PubMed:17229737}.
SITE 139 139 Interaction with DNA. {ECO:0000250}.
SITE 1002 1002 Interaction with DNA. {ECO:0000250}.
MOD_RES 419 419 Phosphoserine.
{ECO:0000250|UniProtKB:Q14191}.
MOD_RES 433 433 Phosphoserine.
{ECO:0000250|UniProtKB:Q14191}.
MOD_RES 444 444 Phosphoserine.
{ECO:0000250|UniProtKB:Q14191}.
MOD_RES 1098 1098 Phosphoserine.
{ECO:0000250|UniProtKB:Q14191}.
MOD_RES 1364 1364 Phosphoserine.
{ECO:0000250|UniProtKB:Q14191}.
CROSSLNK 148 148 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q14191}.
CROSSLNK 235 235 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q14191}.
CROSSLNK 246 246 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q14191}.
MUTAGEN 185 185 K->A: Loss of exonuclease activity.
{ECO:0000269|PubMed:17229737}.
MUTAGEN 190 190 R->A: Strongly reduced exonuclease
activity. {ECO:0000269|PubMed:17229737}.
MUTAGEN 206 206 Y->F: Loss of exonuclease activity.
{ECO:0000269|PubMed:17229737}.
CONFLICT 101 101 S -> N (in Ref. 1; BAA20269/BAA20270, 2;
AAC72359 and 3; AAF64490). {ECO:0000305}.
CONFLICT 228 228 A -> V (in Ref. 1; BAA20269/BAA20270, 2;
AAC72359 and 3; AAF64490). {ECO:0000305}.
CONFLICT 250 250 S -> L (in Ref. 1; BAA20269/BAA20270, 2;
AAC72359 and 3; AAF64490). {ECO:0000305}.
CONFLICT 452 452 V -> M (in Ref. 1; BAA20269/BAA20270, 2;
AAC72359 and 3; AAF64490). {ECO:0000305}.
CONFLICT 459 459 T -> K (in Ref. 1; BAA20269/BAA20270, 2;
AAC72359 and 3; AAF64490). {ECO:0000305}.
CONFLICT 468 468 R -> C (in Ref. 1; BAA20269/BAA20270, 2;
AAC72359 and 3; AAF64490). {ECO:0000305}.
CONFLICT 619 619 Q -> K (in Ref. 1; BAA20269/BAA20270, 2;
AAC72359 and 3; AAF64490). {ECO:0000305}.
CONFLICT 800 800 K -> Q (in Ref. 1; BAA20270/BAA20269).
{ECO:0000305}.
CONFLICT 844 844 L -> H (in Ref. 2; AAC72359).
{ECO:0000305}.
CONFLICT 955 988 NSQRLPDKYRGHRLFGAGKEQAESWWKTLSHHLI -> VSV
SVIAPGTVSDSAFHCVAMALAFFRWLTSNPC (in Ref.
2; AAC72359). {ECO:0000305}.
CONFLICT 1021 1021 S -> L (in Ref. 1; BAA20269/BAA20270 and
3; AAF64490). {ECO:0000305}.
CONFLICT 1145 1145 T -> A (in Ref. 1; BAA20270/BAA20269).
{ECO:0000305}.
CONFLICT 1181 1181 L -> V (in Ref. 1; BAA20270/BAA20269).
{ECO:0000305}.
CONFLICT 1182 1182 E -> G (in Ref. 1; BAA20269/BAA20270 and
3; AAF64490). {ECO:0000305}.
CONFLICT 1252 1252 A -> V (in Ref. 1; BAA20269/BAA20270 and
3; AAF64490). {ECO:0000305}.
CONFLICT 1308 1308 L -> I (in Ref. 1; BAA20269/BAA20270 and
3; AAF64490). {ECO:0000305}.
CONFLICT 1356 1356 A -> V (in Ref. 1; BAA20269/BAA20270 and
3; AAF64490). {ECO:0000305}.
STRAND 45 50 {ECO:0000244|PDB:2E6M}.
HELIX 53 66 {ECO:0000244|PDB:2E6M}.
STRAND 72 78 {ECO:0000244|PDB:2E6M}.
STRAND 93 97 {ECO:0000244|PDB:2E6M}.
STRAND 99 106 {ECO:0000244|PDB:2E6M}.
HELIX 108 110 {ECO:0000244|PDB:2E6M}.
HELIX 116 122 {ECO:0000244|PDB:2E6M}.
STRAND 127 133 {ECO:0000244|PDB:2E6M}.
HELIX 134 145 {ECO:0000244|PDB:2E6M}.
STRAND 151 154 {ECO:0000244|PDB:2E6M}.
HELIX 155 162 {ECO:0000244|PDB:2E6M}.
HELIX 171 179 {ECO:0000244|PDB:2E6M}.
HELIX 187 190 {ECO:0000244|PDB:2E6M}.
STRAND 196 198 {ECO:0000244|PDB:2E6M}.
HELIX 201 222 {ECO:0000244|PDB:2E6M}.
SEQUENCE 1401 AA; 157204 MW; 66DF2252B17C24C3 CRC64;
METTSLQRKF PEWMSMQSQR CATEEKACVQ KSVLEDNLPF LEFPGSIVYS YEASDCSFLS
EDISMRLSDG DVVGFDMEWP PIYKPGKRSR VAVIQLCVSE SKCYLFHISS MSVFPQGLKM
LLENKSIKKA GVGIEGDQWK LLRDFDVKLE SFVELTDVAN EKLKCAETWS LNGLVKHVLG
KQLLKDKSIR CSNWSNFPLT EDQKLYAATD AYAGLIIYQK LGNLGDTAQV FALNKAEENL
PLEMKKQLNS ISEEMRDLAN RFPVTCRNLE TLQRVPVILK SISENLCSLR KVICGPTNTE
TRLKPGSSFN LLSSEDSAAA GEKEKQIGKH STFAKIKEEP WDPELDSLVK QEEVDVFRNQ
VKQEKGESEN EIEDNLLRED MERTCVIPSI SENELQDLEQ QAKEEKYNDV SHQLSEHLSP
NDDENDSSYI IESDEDLEME MLKSLENLNS DVVEPTHSTW LEMGTNGRLP PEEEDGHGNE
AIKEEQEEED HLLPEPNAKQ INCLKTYFGH SSFKPVQWKV IHSVLEERRD NVVVMATGYG
KSLCFQYPPV YTGKIGIVIS PLISLMEDQV LQLELSNVPA CLLGSAQSKN ILGDVKLGKY
RVIYITPEFC SGNLDLLQQL DSSIGITLIA VDEAHCISEW GHDFRSSFRM LGSLKTALPL
VPVIALSATA SSSIREDIIS CLNLKDPQIT CTGFDRPNLY LEVGRKTGNI LQDLKPFLVR
KASSAWEFEG PTIIYCPSRK MTEQVTAELG KLNLACRTYH AGMKISERKD VHHRFLRDEI
QCVVATVAFG MGINKADIRK VIHYGAPKEM ESYYQEIGRA GRDGLQSSCH LLWAPADFNT
SRNLLIEIHD EKFRLYKLKM MVKMEKYLHS SQCRRRIILS HFEDKCLQKA SLDIMGTEKC
CDNCRPRLNH CLTANNSEDA SQDFGPQAFQ LLSAVDILQE KFGIGIPILF LRGSNSQRLP
DKYRGHRLFG AGKEQAESWW KTLSHHLIAE GFLVEVPKEN KYIKTCSLTK KGRKWLGEAS
SQSPPSLLLQ ANEEMFPRKV LLPSSNPVSP ETTQHSSNQN PAGLTTKQSN LERTHSYKVP
EKVSSGTNIP KKSAVMPSPG TSSSPLEPAI SAQELDARTG LYARLVEARQ KHANKMDVPP
AILATNKVLL DMAKMRPTTV ENMKQIDGVS EGKAALLAPL LEVIKHFCQV TSVQTDLLSS
AKPHKEQEKS QEMEKKDCSL PQSVAVTYTL FQEKKMPLHS IAENRLLPLT AAGMHLAQAV
KAGYPLDMER AGLTPETWKI IMDVIRNPPI NSDMYKVKLI RMLVPENLDT YLIHMAIEIL
QSGSDSRTQP PCDSSRKRRF PSSAESCESC KESKEAVTET KASSSESKRK LPEWFAKGNV
PSADTGSSSS MAKTKKKGLF S


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