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DNA (cytosine-5)-methyltransferase 1 (Dnmt1) (Met-1) (EC 2.1.1.37) (DNA methyltransferase MmuI) (DNA MTase MmuI) (M.MmuI) (MCMT)

 DNMT1_MOUSE             Reviewed;        1620 AA.
P13864; P97413; Q80ZU3; Q9CSC6; Q9QXX6;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
21-FEB-2002, sequence version 5.
22-NOV-2017, entry version 202.
RecName: Full=DNA (cytosine-5)-methyltransferase 1;
Short=Dnmt1;
Short=Met-1;
EC=2.1.1.37;
AltName: Full=DNA methyltransferase MmuI;
Short=DNA MTase MmuI;
Short=M.MmuI;
AltName: Full=MCMT;
Name=Dnmt1; Synonyms=Dnmt, Met1, Uim;
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] (ISOFORM 1).
PubMed=3210246; DOI=10.1016/0022-2836(88)90122-2;
Bestor T.H., Laudano A., Mattaliano R., Ingram V.;
"Cloning and sequencing of a cDNA encoding DNA methyltransferase of
mouse cells. The carboxyl-terminal domain of the mammalian enzymes is
related to bacterial restriction methyltransferases.";
J. Mol. Biol. 203:971-983(1988).
[2]
SEQUENCE REVISION TO N-TERMINUS.
TISSUE=Embryo;
PubMed=8940105; DOI=10.1074/jbc.271.49.31092;
Yoder J.A., Yen R.-W.C., Vertino P.M., Bestor T.H., Baylin S.B.;
"New 5' regions of the murine and human genes for DNA (cytosine-5)-
methyltransferase.";
J. Biol. Chem. 271:31092-31097(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Skeletal muscle;
PubMed=11063128;
Aguirre-Arteta A.M., Grunewald I., Cardoso M.C., Leonhardt H.;
"Expression of an alternative Dnmt1 isoform during muscle
differentiation.";
Cell Growth Differ. 11:551-559(2000).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J;
PubMed=10715201; DOI=10.1006/jmbi.2000.3588;
Margot J.B., Aguirre-Arteta A.M., Di Giacco B.V., Pradhan S.,
Roberts R.J., Cardoso M.C., Leonhardt H.;
"Structure and function of the mouse DNA methyltransferase gene: Dnmt1
shows a tripartite structure.";
J. Mol. Biol. 297:293-300(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-27 AND 119-1619
(ISOFORMS 1 AND 2).
PubMed=9449671;
Mertineit C., Yoder J.A., Taketo T., Laird D.W., Trasler J.M.,
Bestor T.H.;
"Sex-specific exons control DNA methyltransferase in mammalian germ
cells.";
Development 125:889-897(1998).
[7]
NUCLEOTIDE SEQUENCE OF 1-144 (ISOFORMS 1 AND 2), AND PROTEIN SEQUENCE
OF 3-6.
STRAIN=129/Sv, and BALB/cJ; TISSUE=Embryonic stem cell;
PubMed=9830015; DOI=10.1074/jbc.273.49.32725;
Gaudet F., Talbot D., Leonhardt H., Jaenisch R.;
"A short DNA methyltransferase isoform restores methylation in vivo.";
J. Biol. Chem. 273:32725-32729(1998).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-119 (ISOFORM 1).
STRAIN=129/Sv; TISSUE=Embryonic stem cell, and Kidney;
PubMed=8917520; DOI=10.1073/pnas.93.23.12920;
Tucker K.L., Talbot D., Lee M.A., Leonhardt H., Jaenisch R.;
"Complementation of methylation deficiency in embryonic stem cells by
a DNA methyltransferase minigene.";
Proc. Natl. Acad. Sci. U.S.A. 93:12920-12925(1996).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-272 (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[10]
PROTEIN SEQUENCE OF 1108-1154, AND ENZYME REGULATION.
PubMed=1628623;
Bestor T.H.;
"Activation of mammalian DNA methyltransferase by cleavage of a Zn
binding regulatory domain.";
EMBO J. 11:2611-2617(1992).
[11]
PHOSPHORYLATION AT SER-515, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Erythroleukemia;
PubMed=9211941; DOI=10.1074/jbc.272.28.17851;
Glickman J.F., Pavlovich J.G., Reich N.O.;
"Peptide mapping of the murine DNA methyltransferase reveals a major
phosphorylation site and the start of translation.";
J. Biol. Chem. 272:17851-17857(1997).
[12]
INTERACTION WITH HDAC1.
PubMed=10615135; DOI=10.1038/71750;
Fuks F., Burgers W.A., Brehm A., Hughes-Davies L., Kouzarides T.;
"DNA methyltransferase Dnmt1 associates with histone deacetylase
activity.";
Nat. Genet. 24:88-91(2000).
[13]
INTERACTION WITH HDAC2 AND DMAP1.
PubMed=10888872; DOI=10.1038/77023;
Rountree M.R., Bachman K.E., Baylin S.B.;
"DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at
replication foci.";
Nat. Genet. 25:269-277(2000).
[14]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11290321; DOI=10.1016/S0092-8674(01)00280-X;
Howell C.Y., Bestor T.H., Ding F., Latham K.E., Mertineit C.,
Trasler J.M., Chaillet J.R.;
"Genomic imprinting disrupted by a maternal effect mutation in the
Dnmt1 gene.";
Cell 104:829-838(2001).
[15]
ALLOSTERIC REGULATION.
PubMed=11399088; DOI=10.1006/jmbi.2001.4709;
Fatemi M., Hermann A., Pradhan S., Jeltsch A.;
"The activity of the murine DNA methyltransferase Dnmt1 is controlled
by interaction of the catalytic domain with the N-terminal part of the
enzyme leading to an allosteric activation of the enzyme after binding
to methylated DNA.";
J. Mol. Biol. 309:1189-1199(2001).
[16]
FUNCTION.
PubMed=15550930; DOI=10.1038/sj.embor.7400295;
Easwaran H.P., Schermelleh L., Leonhardt H., Cardoso M.C.;
"Replication-independent chromatin loading of Dnmt1 during G2 and M
phases.";
EMBO Rep. 5:1181-1186(2004).
[17]
INTERACTION WITH BAZ2A.
PubMed=16085498; DOI=10.1016/j.cub.2005.06.057;
Zhou Y., Grummt I.;
"The PHD finger/bromodomain of NoRC interacts with acetylated histone
H4K16 and is sufficient for rDNA silencing.";
Curr. Biol. 15:1434-1438(2005).
[18]
INTERACTION WITH THE PRC2 COMPLEX.
PubMed=16357870; DOI=10.1038/nature04431;
Vire E., Brenner C., Deplus R., Blanchon L., Fraga M., Didelot C.,
Morey L., Van Eynde A., Bernard D., Vanderwinden J.-M., Bollen M.,
Esteller M., Di Croce L., de Launoit Y., Fuks F.;
"The Polycomb group protein EZH2 directly controls DNA methylation.";
Nature 439:871-874(2006).
[19]
ERRATUM.
Vire E., Brenner C., Deplus R., Blanchon L., Fraga M., Didelot C.,
Morey L., Van Eynde A., Bernard D., Vanderwinden J.-M., Bollen M.,
Esteller M., Di Croce L., de Launoit Y., Fuks F.;
Nature 446:824-824(2006).
[20]
PHOSPHORYLATION AT SER-515, AND MUTAGENESIS OF SER-515.
PubMed=17965600; DOI=10.4161/epi.2.3.4768;
Goyal R., Rathert P., Laser H., Gowher H., Jeltsch A.;
"Phosphorylation of serine-515 activates the mammalian maintenance
methyltransferase Dnmt1.";
Epigenetics 2:155-160(2007).
[21]
FUNCTION, MUTAGENESIS OF GLN-162; PHE-169 AND CYS-1229, AND ACTIVE
SITE.
PubMed=17576694; DOI=10.1093/nar/gkm432;
Schermelleh L., Haemmer A., Spada F., Roesing N., Meilinger D.,
Rothbauer U., Cardoso M.C., Leonhardt H.;
"Dynamics of Dnmt1 interaction with the replication machinery and its
role in postreplicative maintenance of DNA methylation.";
Nucleic Acids Res. 35:4301-4312(2007).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152 AND SER-717, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-717, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-138; SER-140;
SER-146; SER-150; SER-152; SER-240; SER-713 AND SER-717, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
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).
[25]
UBIQUITINATION, DEUBIQUITINATION BY USP7, AND INTERACTION WITH USP7
AND UHRF1.
PubMed=21268065; DOI=10.1002/jcb.22998;
Qin W., Leonhardt H., Spada F.;
"Usp7 and Uhrf1 control ubiquitination and stability of the
maintenance DNA methyltransferase Dnmt1.";
J. Cell. Biochem. 112:439-444(2011).
[26]
PHOSPHORYLATION AT SER-146 BY CSNK1D/CK1, AND INTERACTION WITH CSNK1D.
PubMed=20192920; DOI=10.1042/BJ20091856;
Sugiyama Y., Hatano N., Sueyoshi N., Suetake I., Tajima S.,
Kinoshita E., Kinoshita-Kikuta E., Koike T., Kameshita I.;
"The DNA-binding activity of mouse DNA methyltransferase 1 is
regulated by phosphorylation with casein kinase 1delta/epsilon.";
Biochem. J. 427:489-497(2010).
[27]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1122 AND LYS-1124, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[28]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 731-1602 IN COMPLEX WITH
S-ADENOSYL-L-HOMOCYSTEINE AND DNA, AND AUTOINHIBITORY LINKER.
PubMed=21163962; DOI=10.1126/science.1195380;
Song J., Rechkoblit O., Bestor T.H., Patel D.J.;
"Structure of DNMT1-DNA complex reveals a role for autoinhibition in
maintenance DNA methylation.";
Science 331:1036-1040(2011).
-!- FUNCTION: Methylates CpG residues. Preferentially methylates
hemimethylated DNA. Associates with DNA replication sites in S
phase maintaining the methylation pattern in the newly synthesized
strand, that is essential for epigenetic inheritance. Associates
with chromatin during G2 and M phases to maintain DNA methylation
independently of replication. It is responsible for maintaining
methylation patterns established in development. DNA methylation
is coordinated with methylation of histones. Mediates
transcriptional repression by direct binding to HDAC2. In
association with DNMT3B and via the recruitment of CTCFL/BORIS,
involved in activation of BAG1 gene expression by modulating
dimethylation of promoter histone H3 at H3K4 and H3K9. Probably
forms a corepressor complex required for activated KRAS-mediated
promoter hypermethylation and transcriptional silencing of tumor
suppressor genes (TSGs) or other tumor-related genes in colorectal
cancer (CRC) cells (By similarity). Also required to maintain a
transcriptionally repressive state of genes in undifferentiated
embryonic stem cells (ESCs) (By similarity). Associates at
promoter regions of tumor suppressor genes (TSGs) leading to their
gene silencing (By similarity). Promotes tumor growth (By
similarity). {ECO:0000250|UniProtKB:P26358,
ECO:0000269|PubMed:11290321, ECO:0000269|PubMed:15550930,
ECO:0000269|PubMed:17576694}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA = S-adenosyl-L-
homocysteine + DNA containing 5-methylcytosine.
{ECO:0000255|PROSITE-ProRule:PRU10018}.
-!- ENZYME REGULATION: Allosterically regulated. The binding of 5-
methylcytosine-containing DNA to the N-terminal parts of DNMT1
causes an allosteric activation of the catalytic domain by a
direct interaction of its Zn-binding domain with the catalytic
domain. {ECO:0000269|PubMed:1628623}.
-!- SUBUNIT: Homodimer (By similarity). Forms a stable complex with
E2F1, BB1 and HDAC1 (By similarity). Forms a complex with DMAP1
and HDAC2, with direct interaction (PubMed:10888872). Interacts
with the PRC2/EED-EZH2 complex (PubMed:16357870). Probably part of
a corepressor complex containing ZNF304, TRIM28, SETDB1 and DNMT1
(By similarity). Interacts with UHRF1; promoting its recruitment
to hemimethylated DNA (PubMed:21268065). Interacts with USP7,
promoting its deubiquitination (PubMed:21268065). Interacts with
BAZ2A/TIP5 (PubMed:16085498). Interacts with PCNA (By similarity).
Interacts with MBD2 and MBD3 (By similarity). Interacts with
DNMT3A and DNMT3B (By similarity). Interacts with UBC9 (By
similarity). Interacts with HDAC1 (PubMed:10615135). Interacts
with CSNK1D (PubMed:20192920). {ECO:0000250|UniProtKB:P26358,
ECO:0000269|PubMed:10615135, ECO:0000269|PubMed:10888872,
ECO:0000269|PubMed:16085498, ECO:0000269|PubMed:16357870,
ECO:0000269|PubMed:20192920, ECO:0000269|PubMed:21268065}.
-!- INTERACTION:
O09106:Hdac1; NbExp=3; IntAct=EBI-301927, EBI-301912;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11290321}.
Cytoplasm {ECO:0000269|PubMed:11290321}. Note=It is nucleoplasmic
through most of the cell cycle and associates with replication
foci during S-phase. In germ cells, spermatogonia, preleptotene
and leptotene spermatocytes all express high levels of nuclear
protein, while the protein is not detected in pachytene
spermatocytes, despite the fact they expressed high levels of
mRNA. In females, the protein is not detected in non-growing
oocytes, in contrast to the growing oocytes. During the growing,
the protein is no longer detectable in nuclei but accumulates to
very high levels first throughout the cytoplasm. At the time of
ovulation, all the protein is cytoplasmic and is actively
associated with the oocyte cortex. After fecondation, in the
preimplantation embryo, the protein remains cytoplasmic and after
implantation, it is exclusively nuclear in all tissue types.
Isoform 2 is sequestered in the cytoplasm of maturing oocytes and
of preimplantation embryos, except for the 8-cell stage, while
isoform 1 is exclusively nuclear.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Long;
IsoId=P13864-1; Sequence=Displayed;
Name=2; Synonyms=Short;
IsoId=P13864-2; Sequence=VSP_005619;
-!- TISSUE SPECIFICITY: Isoform 1 is expressed in embryonic stem cells
and in somatic tissues. Isoform 2 is expressed in oocytes,
preimplantation embryos, testis and in skeletal muscle during
myogenesis.
-!- DEVELOPMENTAL STAGE: In germ cells, it is present at high levels
in spermatogonia and spermatocytes until the pachytene stage,
where it falls to undetectable levels. The transient drop at the
pachytene stage coincides with the disappearance of the 5.2 kb
mRNA and the accumulation of a larger 6.0 kb mRNA. Oocytes
accumulate very large amounts of Dnmt1 protein during the growth
phase.
-!- DOMAIN: The N-terminal part is required for homodimerization and
acts as a regulatory domain.
-!- DOMAIN: The CXXC-type zinc finger specifically binds to
unmethylated CpG dinucleotides, positioning the autoinhibitory
linker between the DNA and the active site, thus providing a
mechanism to ensure that only hemimethylated CpG dinucleotides
undergo methylation. {ECO:0000269|PubMed:21163962}.
-!- PTM: Sumoylated. {ECO:0000250}.
-!- PTM: Phosphorylation at Ser-146 by CK1 reduces DNA-binding
activity. {ECO:0000269|PubMed:17965600,
ECO:0000269|PubMed:20192920, ECO:0000269|PubMed:9211941}.
-!- PTM: Acetylation on multiple lysines, mainly by KAT2B/PCAF,
regulates cell cycle G(2)/M transition. Deacetylation of Lys-1352
and Lys-1418 by SIRT1 increases methyltransferase activity (By
similarity). {ECO:0000250}.
-!- PTM: Phosphorylation of Ser-152 by CDKs is important for enzymatic
activity and protein stability. Phosphorylation of Ser-140 by AKT1
prevents methylation by SETD7 therebye increasing DNMT1 stability
(By similarity). {ECO:0000250}.
-!- PTM: Methylation at Lys-139 by SETD7 promotes DNMT1 proteasomal
degradation. {ECO:0000250}.
-!- PTM: Ubiquitinated by UHRF1; interaction with USP7 counteracts
ubiquitination by UHRF1 by promoting deubiquitination and
preventing degradation by the proteasome.
{ECO:0000269|PubMed:21268065}.
-!- MISCELLANEOUS: There are three 5' exons, one specific to the
oocyte (1c), one specific to the pachytene spermatocyte and also
found in skeletal muscle (1b) and one found in somatic cells (1a).
Three different mRNAs can be produced which give rise to two
different translation products: isoform 1 (mRNAs-1a) and isoform 2
(mRNA-1b or -1c). Association of DNMT1 with the replication
machinery is not strictly required for maintaining global
methylation but still enhances methylation efficiency by 2-fold.
Pre-existing cytosine methylation at CpG and non-CpG sites
enhances methylation activity.
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. C5-methyltransferase family.
{ECO:0000255|PROSITE-ProRule:PRU01016}.
-!- SEQUENCE CAUTION:
Sequence=AAC52900.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; X14805; CAA32910.1; -; mRNA.
EMBL; AF175432; AAF97695.1; -; mRNA.
EMBL; AF162282; AAF19352.1; -; mRNA.
EMBL; AF175431; AAF60965.1; -; Genomic_DNA.
EMBL; AF175412; AAF60965.1; JOINED; Genomic_DNA.
EMBL; AF175413; AAF60965.1; JOINED; Genomic_DNA.
EMBL; AF175414; AAF60965.1; JOINED; Genomic_DNA.
EMBL; AF244089; AAF60965.1; JOINED; Genomic_DNA.
EMBL; AF244090; AAF60965.1; JOINED; Genomic_DNA.
EMBL; AF175416; AAF60965.1; JOINED; Genomic_DNA.
EMBL; AF175417; AAF60965.1; JOINED; Genomic_DNA.
EMBL; AF175418; AAF60965.1; JOINED; Genomic_DNA.
EMBL; AF175419; AAF60965.1; JOINED; Genomic_DNA.
EMBL; AF175420; AAF60965.1; JOINED; Genomic_DNA.
EMBL; AF175421; AAF60965.1; JOINED; Genomic_DNA.
EMBL; AF175422; AAF60965.1; JOINED; Genomic_DNA.
EMBL; AF175423; AAF60965.1; JOINED; Genomic_DNA.
EMBL; AF234317; AAF60965.1; JOINED; Genomic_DNA.
EMBL; AF175424; AAF60965.1; JOINED; Genomic_DNA.
EMBL; AF175425; AAF60965.1; JOINED; Genomic_DNA.
EMBL; AF175426; AAF60965.1; JOINED; Genomic_DNA.
EMBL; AF234318; AAF60965.1; JOINED; Genomic_DNA.
EMBL; AF175427; AAF60965.1; JOINED; Genomic_DNA.
EMBL; AF175428; AAF60965.1; JOINED; Genomic_DNA.
EMBL; AF175429; AAF60965.1; JOINED; Genomic_DNA.
EMBL; AF175430; AAF60965.1; JOINED; Genomic_DNA.
EMBL; BC048148; AAH48148.2; -; mRNA.
EMBL; AF036007; AAC40061.1; -; mRNA.
EMBL; AF036008; AAC53551.1; -; Genomic_DNA.
EMBL; U70051; AAC52900.1; ALT_INIT; mRNA.
EMBL; AK013247; BAB28743.1; -; mRNA.
CCDS; CCDS57654.1; -. [P13864-2]
CCDS; CCDS57655.1; -. [P13864-1]
PIR; S01845; S01845.
RefSeq; NP_001186360.2; NM_001199431.1. [P13864-1]
RefSeq; NP_001186361.1; NM_001199432.1.
RefSeq; NP_001186362.1; NM_001199433.1. [P13864-2]
RefSeq; NP_001300940.1; NM_001314011.1.
RefSeq; NP_034196.5; NM_010066.4.
UniGene; Mm.128580; -.
UniGene; Mm.485562; -.
PDB; 3AV4; X-ray; 2.75 A; A=291-1620.
PDB; 3AV5; X-ray; 3.25 A; A=291-1620.
PDB; 3AV6; X-ray; 3.09 A; A=291-1620.
PDB; 3PT6; X-ray; 3.00 A; A/B=650-1602.
PDB; 3PT9; X-ray; 2.50 A; A=731-1602.
PDB; 4DA4; X-ray; 2.60 A; A/B=731-1602.
PDB; 5GUT; X-ray; 2.10 A; A=731-1602.
PDB; 5GUV; X-ray; 3.08 A; A=731-1602.
PDB; 5WY1; X-ray; 3.27 A; A=291-1620.
PDBsum; 3AV4; -.
PDBsum; 3AV5; -.
PDBsum; 3AV6; -.
PDBsum; 3PT6; -.
PDBsum; 3PT9; -.
PDBsum; 4DA4; -.
PDBsum; 5GUT; -.
PDBsum; 5GUV; -.
PDBsum; 5WY1; -.
ProteinModelPortal; P13864; -.
SMR; P13864; -.
BioGrid; 199259; 22.
CORUM; P13864; -.
IntAct; P13864; 9.
MINT; MINT-4093291; -.
STRING; 10090.ENSMUSP00000004202; -.
BindingDB; P13864; -.
ChEMBL; CHEMBL3351195; -.
REBASE; 2844; M.MmuDnmt1.
iPTMnet; P13864; -.
PhosphoSitePlus; P13864; -.
SwissPalm; P13864; -.
EPD; P13864; -.
MaxQB; P13864; -.
PaxDb; P13864; -.
PeptideAtlas; P13864; -.
PRIDE; P13864; -.
Ensembl; ENSMUST00000004202; ENSMUSP00000004202; ENSMUSG00000004099. [P13864-1]
Ensembl; ENSMUST00000216540; ENSMUSP00000150433; ENSMUSG00000004099. [P13864-2]
GeneID; 13433; -.
KEGG; mmu:13433; -.
UCSC; uc009ojo.2; mouse. [P13864-1]
CTD; 1786; -.
MGI; MGI:94912; Dnmt1.
eggNOG; ENOG410IF68; Eukaryota.
eggNOG; COG0270; LUCA.
GeneTree; ENSGT00390000005100; -.
HOVERGEN; HBG051384; -.
InParanoid; P13864; -.
KO; K00558; -.
OMA; WAMEGGM; -.
OrthoDB; EOG091G02YU; -.
PhylomeDB; P13864; -.
TreeFam; TF328926; -.
BRENDA; 2.1.1.37; 3474.
Reactome; R-MMU-212300; PRC2 methylates histones and DNA.
Reactome; R-MMU-573389; NoRC negatively regulates rRNA expression.
ChiTaRS; Dnmt1; mouse.
EvolutionaryTrace; P13864; -.
PRO; PR:P13864; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000004099; -.
CleanEx; MM_DNMT1; -.
ExpressionAtlas; P13864; baseline and differential.
Genevisible; P13864; MM.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0000792; C:heterochromatin; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005721; C:pericentric heterochromatin; IDA:UniProtKB.
GO; GO:0005657; C:replication fork; IDA:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IDA:MGI.
GO; GO:0051718; F:DNA (cytosine-5-)-methyltransferase activity, acting on CpG substrates; TAS:Reactome.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0009008; F:DNA-methyltransferase activity; ISO:MGI.
GO; GO:0008327; F:methyl-CpG binding; IDA:MGI.
GO; GO:0008168; F:methyltransferase activity; IDA:UniProtKB.
GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:MGI.
GO; GO:0008270; F:zinc ion binding; IDA:MGI.
GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:MGI.
GO; GO:0000183; P:chromatin silencing at rDNA; TAS:Reactome.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0006306; P:DNA methylation; IDA:MGI.
GO; GO:0043045; P:DNA methylation involved in embryo development; IMP:MGI.
GO; GO:0032776; P:DNA methylation on cytosine; IMP:MGI.
GO; GO:0016458; P:gene silencing; IDA:UniProtKB.
GO; GO:0010216; P:maintenance of DNA methylation; IMP:UniProtKB.
GO; GO:0051573; P:negative regulation of histone H3-K9 methylation; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; ISO:MGI.
GO; GO:0090309; P:positive regulation of methylation-dependent chromatin silencing; ISS:UniProtKB.
GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; IGI:MGI.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR001025; BAH_dom.
InterPro; IPR018117; C5_DNA_meth_AS.
InterPro; IPR001525; C5_MeTfrase.
InterPro; IPR031303; C5_meth_CS.
InterPro; IPR022702; Cytosine_MeTrfase1_RFD.
InterPro; IPR010506; DMAP1-bd.
InterPro; IPR017198; DNMT1-like.
InterPro; IPR029063; SAM-dependent_MTases.
InterPro; IPR002857; Znf_CXXC.
Pfam; PF01426; BAH; 2.
Pfam; PF06464; DMAP_binding; 1.
Pfam; PF12047; DNMT1-RFD; 1.
Pfam; PF02008; zf-CXXC; 1.
PIRSF; PIRSF037404; DNMT1; 1.
PRINTS; PR00105; C5METTRFRASE.
SMART; SM00439; BAH; 2.
SMART; SM01137; DMAP_binding; 1.
SUPFAM; SSF53335; SSF53335; 2.
PROSITE; PS51038; BAH; 2.
PROSITE; PS00094; C5_MTASE_1; 1.
PROSITE; PS00095; C5_MTASE_2; 1.
PROSITE; PS51679; SAM_MT_C5; 1.
PROSITE; PS51058; ZF_CXXC; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Allosteric enzyme;
Alternative splicing; Chromatin regulator; Complete proteome;
Cytoplasm; Direct protein sequencing; DNA-binding; Isopeptide bond;
Metal-binding; Methylation; Methyltransferase; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Repressor;
S-adenosyl-L-methionine; Transcription; Transcription regulation;
Transferase; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 1620 DNA (cytosine-5)-methyltransferase 1.
/FTId=PRO_0000088035.
DOMAIN 18 106 DMAP-interaction.
DOMAIN 758 884 BAH 1. {ECO:0000255|PROSITE-
ProRule:PRU00370}.
DOMAIN 976 1103 BAH 2. {ECO:0000255|PROSITE-
ProRule:PRU00370}.
REPEAT 1112 1113 1.
REPEAT 1114 1115 2.
REPEAT 1116 1117 3.
REPEAT 1118 1119 4.
REPEAT 1120 1121 5.
REPEAT 1122 1123 6.
REPEAT 1124 1125 7; approximate.
DOMAIN 1142 1601 SAM-dependent MTase C5-type.
{ECO:0000255|PROSITE-ProRule:PRU01016}.
ZN_FING 649 695 CXXC-type. {ECO:0000255|PROSITE-
ProRule:PRU00509}.
REGION 1 343 Interaction with the PRC2/EED-EZH2
complex.
REGION 1 145 Interaction with DNMT3A. {ECO:0000250}.
REGION 1 120 Interaction with DMAP1.
{ECO:0000269|PubMed:10888872}.
REGION 147 217 Interaction with DNMT3B. {ECO:0000250}.
REGION 161 172 Interaction with PCNA.
REGION 305 609 Interaction with the PRC2/EED-EZH2
complex.
REGION 328 556 DNA replication foci-targeting sequence.
{ECO:0000250}.
REGION 696 813 Interaction with HDAC1.
{ECO:0000269|PubMed:10615135}.
REGION 696 757 Autoinhibitory linker.
REGION 1112 1125 7 X 2 AA tandem repeats of K-G.
REGION 1124 1620 Interaction with the PRC2/EED-EZH2
complex.
REGION 1142 1620 Catalytic.
REGION 1153 1154 S-adenosyl-L-methionine binding.
{ECO:0000244|PDB:3PT6,
ECO:0000244|PDB:3PT9,
ECO:0000244|PDB:4DA4,
ECO:0000269|PubMed:21163962}.
REGION 1171 1172 S-adenosyl-L-methionine binding.
{ECO:0000244|PDB:3PT6,
ECO:0000244|PDB:3PT9,
ECO:0000244|PDB:4DA4,
ECO:0000269|PubMed:21163962}.
REGION 1193 1194 S-adenosyl-L-methionine binding.
{ECO:0000244|PDB:3PT6,
ECO:0000244|PDB:3PT9,
ECO:0000269|PubMed:21163962}.
MOTIF 175 202 Nuclear localization signal.
{ECO:0000255}.
ACT_SITE 1229 1229 {ECO:0000269|PubMed:17576694}.
METAL 359 359 Zinc. {ECO:0000250}.
METAL 362 362 Zinc. {ECO:0000250}.
METAL 420 420 Zinc. {ECO:0000250}.
METAL 424 424 Zinc. {ECO:0000250}.
BINDING 1149 1149 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000244|PDB:3PT6,
ECO:0000244|PDB:4DA4,
ECO:0000269|PubMed:21163962}.
BINDING 1582 1582 S-adenosyl-L-methionine; via amide
nitrogen. {ECO:0000244|PDB:3PT6,
ECO:0000244|PDB:3PT9,
ECO:0000244|PDB:4DA4,
ECO:0000269|PubMed:21163962}.
MOD_RES 15 15 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 70 70 N6,N6-dimethyllysine; by EHMT2.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 138 138 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 139 139 N6-methyllysine; by SETD7.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 140 140 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 146 146 Phosphoserine; by CK1.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:20192920}.
MOD_RES 150 150 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 152 152 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 164 164 Phosphothreonine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 171 171 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 240 240 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 255 255 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 372 372 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 515 515 Phosphoserine.
{ECO:0000269|PubMed:17965600,
ECO:0000269|PubMed:9211941}.
MOD_RES 555 555 Phosphoserine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 713 713 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 717 717 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 735 735 Phosphoserine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 752 752 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 882 882 Phosphoserine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 895 895 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 961 961 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 965 965 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 979 979 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 1114 1114 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 1116 1116 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 1118 1118 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 1120 1120 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 1122 1122 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 1124 1124 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 1352 1352 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 1418 1418 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
CROSSLNK 255 255 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P26358}.
CROSSLNK 1611 1611 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P26358}.
VAR_SEQ 1 118 Missing (in isoform 2).
{ECO:0000303|PubMed:10715201,
ECO:0000303|PubMed:11063128,
ECO:0000303|PubMed:9449671}.
/FTId=VSP_005619.
MUTAGEN 162 162 Q->E: Abolishes interaction with PCNA. No
effect on activity.
{ECO:0000269|PubMed:17576694}.
MUTAGEN 169 169 F->S: Abolishes interaction with PCNA. No
effect on activity.
{ECO:0000269|PubMed:17576694}.
MUTAGEN 515 515 S->A: Loss of activity. No effect on DNA-
binding capacity.
{ECO:0000269|PubMed:17965600}.
MUTAGEN 515 515 S->E: Slightly reduces activity.
{ECO:0000269|PubMed:17965600}.
MUTAGEN 1229 1229 C->W: Loss of activity.
{ECO:0000269|PubMed:17576694}.
CONFLICT 146 147 SV -> F (in Ref. 1; CAA32910 and 6;
AAC40061). {ECO:0000305}.
CONFLICT 299 309 AEPEQVAPETP -> VRARAGSSRDS (in Ref. 1;
CAA32910 and 6; AAC40061). {ECO:0000305}.
CONFLICT 936 936 V -> C (in Ref. 1; CAA32910 and 6;
AAC40061). {ECO:0000305}.
CONFLICT 947 947 P -> R (in Ref. 1; CAA32910 and 6;
AAC40061). {ECO:0000305}.
CONFLICT 969 976 NETLYPEH -> KENPVPRDT (in Ref. 1;
CAA32910 and 6; AAC40061). {ECO:0000305}.
CONFLICT 987 987 S -> R (in Ref. 1; CAA32910 and 6;
AAC40061). {ECO:0000305}.
CONFLICT 1046 1046 Y -> C (in Ref. 1; CAA32910 and 6;
AAC40061). {ECO:0000305}.
CONFLICT 1068 1068 G -> R (in Ref. 1; CAA32910 and 6;
AAC40061). {ECO:0000305}.
CONFLICT 1429 1429 R -> P (in Ref. 1; CAA32910 and 6;
AAC40061). {ECO:0000305}.
CONFLICT 1456 1456 H -> D (in Ref. 1; CAA32910 and 6;
AAC40061). {ECO:0000305}.
TURN 360 362 {ECO:0000244|PDB:3AV4}.
STRAND 365 367 {ECO:0000244|PDB:5WY1}.
HELIX 383 387 {ECO:0000244|PDB:3AV4}.
STRAND 406 408 {ECO:0000244|PDB:3AV5}.
STRAND 410 419 {ECO:0000244|PDB:3AV4}.
STRAND 423 425 {ECO:0000244|PDB:3AV6}.
TURN 432 436 {ECO:0000244|PDB:3AV4}.
STRAND 440 445 {ECO:0000244|PDB:3AV4}.
STRAND 454 458 {ECO:0000244|PDB:3AV6}.
STRAND 459 465 {ECO:0000244|PDB:3AV4}.
STRAND 469 473 {ECO:0000244|PDB:3AV4}.
STRAND 475 479 {ECO:0000244|PDB:3AV4}.
STRAND 482 486 {ECO:0000244|PDB:3AV4}.
STRAND 491 494 {ECO:0000244|PDB:3AV4}.
TURN 499 501 {ECO:0000244|PDB:3AV4}.
HELIX 502 524 {ECO:0000244|PDB:3AV4}.
HELIX 530 539 {ECO:0000244|PDB:3AV4}.
HELIX 553 558 {ECO:0000244|PDB:3AV4}.
HELIX 560 573 {ECO:0000244|PDB:3AV4}.
HELIX 581 583 {ECO:0000244|PDB:3AV4}.
HELIX 585 593 {ECO:0000244|PDB:3AV4}.
HELIX 625 635 {ECO:0000244|PDB:3AV4}.
STRAND 657 659 {ECO:0000244|PDB:3AV4}.
TURN 660 663 {ECO:0000244|PDB:3AV4}.
TURN 671 675 {ECO:0000244|PDB:3PT6}.
TURN 677 680 {ECO:0000244|PDB:3PT6}.
HELIX 690 692 {ECO:0000244|PDB:3PT6}.
HELIX 695 704 {ECO:0000244|PDB:3AV4}.
STRAND 734 739 {ECO:0000244|PDB:3PT9}.
STRAND 741 743 {ECO:0000244|PDB:3PT9}.
STRAND 745 751 {ECO:0000244|PDB:5GUT}.
STRAND 753 755 {ECO:0000244|PDB:5GUT}.
STRAND 758 760 {ECO:0000244|PDB:5GUT}.
STRAND 765 768 {ECO:0000244|PDB:5GUT}.
STRAND 774 776 {ECO:0000244|PDB:4DA4}.
STRAND 778 788 {ECO:0000244|PDB:5GUT}.
STRAND 793 802 {ECO:0000244|PDB:5GUT}.
HELIX 803 805 {ECO:0000244|PDB:5GUT}.
HELIX 809 811 {ECO:0000244|PDB:5GUT}.
STRAND 816 827 {ECO:0000244|PDB:5GUT}.
HELIX 828 830 {ECO:0000244|PDB:5GUT}.
STRAND 831 835 {ECO:0000244|PDB:5GUT}.
STRAND 837 839 {ECO:0000244|PDB:3PT9}.
HELIX 846 848 {ECO:0000244|PDB:5GUT}.
STRAND 868 874 {ECO:0000244|PDB:5GUT}.
TURN 875 878 {ECO:0000244|PDB:5GUT}.
STRAND 879 881 {ECO:0000244|PDB:5GUT}.
TURN 890 895 {ECO:0000244|PDB:3PT9}.
HELIX 898 910 {ECO:0000244|PDB:5GUT}.
STRAND 913 920 {ECO:0000244|PDB:5GUT}.
STRAND 922 924 {ECO:0000244|PDB:3AV5}.
STRAND 925 932 {ECO:0000244|PDB:5GUT}.
STRAND 935 938 {ECO:0000244|PDB:5GUT}.
STRAND 942 945 {ECO:0000244|PDB:5GUT}.
HELIX 947 949 {ECO:0000244|PDB:5GUT}.
TURN 970 972 {ECO:0000244|PDB:5GUT}.
HELIX 976 979 {ECO:0000244|PDB:5GUT}.
STRAND 996 1008 {ECO:0000244|PDB:5GUT}.
STRAND 1011 1023 {ECO:0000244|PDB:5GUT}.
HELIX 1027 1029 {ECO:0000244|PDB:5GUT}.
TURN 1031 1036 {ECO:0000244|PDB:5GUT}.
TURN 1037 1039 {ECO:0000244|PDB:3PT6}.
STRAND 1044 1047 {ECO:0000244|PDB:5GUT}.
STRAND 1051 1055 {ECO:0000244|PDB:5GUT}.
HELIX 1056 1058 {ECO:0000244|PDB:5GUT}.
STRAND 1061 1067 {ECO:0000244|PDB:5GUT}.
HELIX 1068 1070 {ECO:0000244|PDB:5GUT}.
HELIX 1075 1081 {ECO:0000244|PDB:5GUT}.
STRAND 1085 1091 {ECO:0000244|PDB:5GUT}.
TURN 1094 1096 {ECO:0000244|PDB:5GUT}.
STRAND 1098 1100 {ECO:0000244|PDB:4DA4}.
HELIX 1104 1106 {ECO:0000244|PDB:5GUT}.
STRAND 1142 1147 {ECO:0000244|PDB:5GUT}.
HELIX 1153 1161 {ECO:0000244|PDB:5GUT}.
STRAND 1163 1170 {ECO:0000244|PDB:5GUT}.
HELIX 1174 1183 {ECO:0000244|PDB:5GUT}.
STRAND 1187 1190 {ECO:0000244|PDB:5GUT}.
HELIX 1194 1202 {ECO:0000244|PDB:5GUT}.
TURN 1217 1219 {ECO:0000244|PDB:5GUT}.
STRAND 1221 1225 {ECO:0000244|PDB:5GUT}.
TURN 1230 1232 {ECO:0000244|PDB:4DA4}.
STRAND 1234 1236 {ECO:0000244|PDB:3AV4}.
HELIX 1240 1247 {ECO:0000244|PDB:5GUT}.
HELIX 1250 1261 {ECO:0000244|PDB:5GUT}.
STRAND 1264 1271 {ECO:0000244|PDB:5GUT}.
HELIX 1272 1275 {ECO:0000244|PDB:5GUT}.
HELIX 1277 1293 {ECO:0000244|PDB:5GUT}.
STRAND 1296 1303 {ECO:0000244|PDB:5GUT}.
HELIX 1304 1307 {ECO:0000244|PDB:5GUT}.
STRAND 1314 1321 {ECO:0000244|PDB:5GUT}.
HELIX 1339 1341 {ECO:0000244|PDB:5GUT}.
STRAND 1346 1348 {ECO:0000244|PDB:5GUT}.
STRAND 1351 1353 {ECO:0000244|PDB:5GUT}.
HELIX 1370 1374 {ECO:0000244|PDB:5GUT}.
STRAND 1375 1377 {ECO:0000244|PDB:3PT6}.
STRAND 1387 1390 {ECO:0000244|PDB:5GUT}.
HELIX 1398 1404 {ECO:0000244|PDB:5GUT}.
STRAND 1411 1413 {ECO:0000244|PDB:5GUT}.
HELIX 1422 1429 {ECO:0000244|PDB:5GUT}.
STRAND 1433 1436 {ECO:0000244|PDB:3AV5}.
HELIX 1439 1441 {ECO:0000244|PDB:5GUT}.
HELIX 1450 1452 {ECO:0000244|PDB:5GUT}.
STRAND 1454 1456 {ECO:0000244|PDB:5GUT}.
TURN 1465 1467 {ECO:0000244|PDB:5GUT}.
STRAND 1477 1479 {ECO:0000244|PDB:5GUT}.
HELIX 1480 1483 {ECO:0000244|PDB:5GUT}.
STRAND 1489 1491 {ECO:0000244|PDB:3AV4}.
STRAND 1495 1498 {ECO:0000244|PDB:5GUT}.
HELIX 1501 1505 {ECO:0000244|PDB:5GUT}.
HELIX 1506 1512 {ECO:0000244|PDB:5GUT}.
TURN 1513 1516 {ECO:0000244|PDB:5GUT}.
STRAND 1525 1527 {ECO:0000244|PDB:3AV4}.
STRAND 1536 1538 {ECO:0000244|PDB:5GUT}.
STRAND 1544 1549 {ECO:0000244|PDB:5GUT}.
HELIX 1552 1558 {ECO:0000244|PDB:5GUT}.
HELIX 1571 1580 {ECO:0000244|PDB:5GUT}.
HELIX 1584 1596 {ECO:0000244|PDB:5GUT}.
TURN 1607 1611 {ECO:0000244|PDB:5WY1}.
SEQUENCE 1620 AA; 183189 MW; 4F9A98CEAF09F037 CRC64;
MPARTAPARV PALASPAGSL PDHVRRRLKD LERDGLTEKE CVREKLNLLH EFLQTEIKSQ
LCDLETKLHK EELSEEGYLA KVKSLLNKDL SLENGTHTLT QKANGCPANG SRPTWRAEMA
DSNRSPRSRP KPRGPRRSKS DSDTLSVETS PSSVATRRTT RQTTITAHFT KGPTKRKPKE
ESEEGNSAES AAEERDQDKK RRVVDTESGA AAAVEKLEEV TAGTQLGPEE PCEQEDDNRS
LRRHTRELSL RRKSKEDPDR EARPETHLDE DEDGKKDKRS SRPRSQPRDP AAKRRPKEAE
PEQVAPETPE DRDEDEREEK RRKTTRKKLE SHTVPVQSRS ERKAAQSKSV IPKINSPKCP
ECGQHLDDPN LKYQQHPEDA VDEPQMLTSE KLSIYDSTST WFDTYEDSPM HRFTSFSVYC
SRGHLCPVDT GLIEKNVELY FSGCAKAIHD ENPSMEGGIN GKNLGPINQW WLSGFDGGEK
VLIGFSTAFA EYILMEPSKE YEPIFGLMQE KIYISKIVVE FLQNNPDAVY EDLINKIETT
VPPSTINVNR FTEDSLLRHA QFVVSQVESY DEAKDDDETP IFLSPCMRAL IHLAGVSLGQ
RRATRRVMGA TKEKDKAPTK ATTTKLVYQI FDTFFSEQIE KYDKEDKENA MKRRRCGVCE
VCQQPECGKC KACKDMVKFG GTGRSKQACL KRRCPNLAVK EADDDEEADD DVSEMPSPKK
LHQGKKKKQN KDRISWLGQP MKIEENRTYY QKVSIDEEML EVGDCVSVIP DDSSKPLYLA
RVTALWEDKN GQMMFHAHWF CAGTDTVLGA TSDPLELFLV GECENMQLSY IHSKVKVIYK
APSENWAMEG GTDPETTLPG AEDGKTYFFQ LWYNQEYARF ESPPKTQPTE DNKHKFCLSC
IRLAELRQKE MPKVLEQIEE VDGRVYCSSI TKNGVVYRLG DSVYLPPEAF TFNIKVASPV
KRPKKDPVNE TLYPEHYRKY SDYIKGSNLD APEPYRIGRI KEIHCGKKKG KVNEADIKLR
LYKFYRPENT HRSYNGSYHT DINMLYWSDE EAVVNFSDVQ GRCTVEYGED LLESIQDYSQ
GGPDRFYFLE AYNSKTKNFE DPPNHARSPG NKGKGKGKGK GKGKHQVSEP KEPEAAIKLP
KLRTLDVFSG CGGLSEGFHQ AGISETLWAI EMWDPAAQAF RLNNPGTTVF TEDCNVLLKL
VMAGEVTNSL GQRLPQKGDV EMLCGGPPCQ GFSGMNRFNS RTYSKFKNSL VVSFLSYCDY
YRPRFFLLEN VRNFVSYRRS MVLKLTLRCL VRMGYQCTFG VLQAGQYGVA QTRRRAIILA
AAPGEKLPLF PEPLHVFAPR ACQLSVVVDD KKFVSNITRL SSGPFRTITV RDTMSDLPEI
QNGASNSEIP YNGEPLSWFQ RQLRGSHYQP ILRDHICKDM SPLVAARMRH IPLFPGSDWR
DLPNIQVRLG DGVIAHKLQY TFHDVKNGYS STGALRGVCS CAEGKACDPE SRQFSTLIPW
CLPHTGNRHN HWAGLYGRLE WDGFFSTTVT NPEPMGKQGR VLHPEQHRVV SVRECARSQG
FPDSYRFFGN ILDRHRQVGN AVPPPLAKAI GLEIKLCLLS SARESASAAV KAKEEAATKD


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