DNM3L_RAT
ID DNM3L_RAT Reviewed; 422 AA.
AC Q1LZ50;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=DNA (cytosine-5)-methyltransferase 3-like;
GN Name=Dnmt3l;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP IDENTIFICATION.
RX PubMed=15203217; DOI=10.1016/j.ygeno.2004.02.004;
RA Lees-Murdock D.J., McLoughlin G.A., McDaid J.R., Quinn L.M., O'Doherty A.,
RA Hiripi L., Hack C.J., Walsh C.P.;
RT "Identification of 11 pseudogenes in the DNA methyltransferase gene family
RT in rodents and humans and implications for the functional loci.";
RL Genomics 84:193-204(2004).
CC -!- FUNCTION: Catalytically inactive regulatory factor of DNA
CC methyltransferases that can either promote or inhibit DNA methylation
CC depending on the context. Essential for the function of DNMT3A and
CC DNMT3B: activates DNMT3A and DNMT3B by binding to their catalytic
CC domain. Acts by accelerating the binding of DNA and S-adenosyl-L-
CC methionine (AdoMet) to the methyltransferases and dissociates from the
CC complex after DNA binding to the methyltransferases (By similarity).
CC Recognizes unmethylated histone H3 lysine 4 (H3K4me0) and induces de
CC novo DNA methylation by recruitment or activation of DNMT3 (By
CC similarity). Plays a key role in embryonic stem cells and germ cells.
CC In germ cells, required for the methylation of imprinted loci together
CC with DNMT3A. In male germ cells, specifically required to methylate
CC retrotransposons, preventing their mobilization. Plays a key role in
CC embryonic stem cells (ESCs) by acting both as an positive and negative
CC regulator of DNA methylation. While it promotes DNA methylation of
CC housekeeping genes together with DNMT3A and DNMT3B, it also acts as an
CC inhibitor of DNA methylation at the promoter of bivalent genes.
CC Interacts with the EZH2 component of the PRC2/EED-EZH2 complex,
CC preventing interaction of DNMT3A and DNMT3B with the PRC2/EED-EZH2
CC complex, leading to maintain low methylation levels at the promoters of
CC bivalent genes. Promotes differentiation of ESCs into primordial germ
CC cells by inhibiting DNA methylation at the promoter of RHOX5, thereby
CC activating its expression (By similarity).
CC {ECO:0000250|UniProtKB:Q9CWR8, ECO:0000250|UniProtKB:Q9UJW3}.
CC -!- SUBUNIT: Homodimer (By similarity). Heterotetramer composed of 1 DNMT3A
CC homodimer and 2 DNMT3L subunits (DNMT3L-DNMT3A-DNMT3A-DNMT3L) (By
CC similarity). Interacts with histone H3 (via N-terminus); interaction is
CC strongly inhibited by methylation at lysine 4 (H3K4me) (By similarity).
CC Interacts with EZH2; the interaction is direct (By similarity).
CC Interacts with SPOCD1 (By similarity). {ECO:0000250|UniProtKB:Q9CWR8,
CC ECO:0000250|UniProtKB:Q9UJW3}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR EMBL; AABR03116801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03116733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BN000398; CAE52320.1; -; mRNA.
DR RefSeq; NP_001003964.1; NM_001003964.1.
DR AlphaFoldDB; Q1LZ50; -.
DR SMR; Q1LZ50; -.
DR STRING; 10116.ENSRNOP00000001610; -.
DR PhosphoSitePlus; Q1LZ50; -.
DR PaxDb; Q1LZ50; -.
DR GeneID; 309680; -.
DR KEGG; rno:309680; -.
DR CTD; 29947; -.
DR RGD; 1303239; Dnmt3l.
DR eggNOG; ENOG502SIGQ; Eukaryota.
DR InParanoid; Q1LZ50; -.
DR OrthoDB; 1015783at2759; -.
DR PhylomeDB; Q1LZ50; -.
DR PRO; PR:Q1LZ50; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:1902494; C:catalytic complex; ISO:RGD.
DR GO; GO:0000794; C:condensed nuclear chromosome; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0035098; C:ESC/E(Z) complex; ISO:RGD.
DR GO; GO:0000792; C:heterochromatin; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0008047; F:enzyme activator activity; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0090116; P:C-5 methylation of cytosine; ISO:RGD.
DR GO; GO:0060718; P:chorionic trophoblast cell differentiation; ISO:RGD.
DR GO; GO:0006306; P:DNA methylation; ISO:RGD.
DR GO; GO:0043046; P:DNA methylation involved in gamete generation; ISS:UniProtKB.
DR GO; GO:0032776; P:DNA methylation on cytosine; ISS:UniProtKB.
DR GO; GO:0071514; P:genomic imprinting; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0007141; P:male meiosis I; ISS:UniProtKB.
DR GO; GO:0032259; P:methylation; ISO:RGD.
DR GO; GO:1905642; P:negative regulation of DNA methylation; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0010529; P:negative regulation of transposition; ISO:RGD.
DR GO; GO:0001890; P:placenta development; ISO:RGD.
DR GO; GO:1905643; P:positive regulation of DNA methylation; ISS:UniProtKB.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR GO; GO:0048863; P:stem cell differentiation; ISS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025766; ADD.
DR InterPro; IPR040552; DNMT3_ADD.
DR InterPro; IPR030486; DNMT3L.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR23068:SF13; PTHR23068:SF13; 1.
DR Pfam; PF17980; ADD_DNMT3; 1.
DR PROSITE; PS51533; ADD; 1.
PE 2: Evidence at transcript level;
KW Differentiation; Metal-binding; Nucleus; Reference proteome;
KW Spermatogenesis; Zinc; Zinc-finger.
FT CHAIN 1..422
FT /note="DNA (cytosine-5)-methyltransferase 3-like"
FT /id="PRO_0000281744"
FT DOMAIN 76..208
FT /note="ADD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00865"
FT ZN_FING 87..117
FT /note="GATA-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00865"
FT ZN_FING 128..184
FT /note="PHD-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00865"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 422 AA; 48279 MW; BFA7A78D1E7CBD90 CRC64;
MGSRETPSSC SKTHETLNLE TPESSSTDPD SPLEEQWPKS APDLKEEDSM DMVLEDSKEP
LTPSSPPTGR EVIRYEVNVN QRNIEDICLC CGSLQVYAQH PLFEGGICAP CKDKFLETLF
LYDEDGHQSY CTICCSGHTL FICESPDCTR CYCFECVDIL VGPGTSERIN AMACWVCFLC
LPFSRSGLLQ RRKKWRHQLK AFHDREGASP VEIYKTVSAW KRQPVRVLSL FGNIDKELKS
LGFLESSSGS EGGTLKYVED VTNVVRREVE KWGPFDLVYG STQPLGYSCD RCPGWYMFQF
HRILQYARPR QDSQQPFFWI FVDNLLLTED DQETTVRFLQ TEAVTLQDVR GRVLQNAMRV
WSNIPGLKSK HADLTPKEEQ SLQTQVRTRS KLAAQKVDSL VKYCLLPLRE YFKYFSQNSL
PL
