ID   D4A005_RAT              Unreviewed;      1262 AA.
AC   D4A005;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   08-OCT-2025, sequence version 5.
DT   02-SEP-2026, entry version 112.
DE   RecName: Full=[histone H3]-lysine(9) N-methyltransferase {ECO:0000256|ARBA:ARBA00066816};
DE            EC=2.1.1.367 {ECO:0000256|ARBA:ARBA00066816};
GN   Name=Ehmt1 {ECO:0000313|Ensembl:ENSRNOP00000063511.5,
GN   ECO:0000313|RGD:1307588};
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 {ECO:0000313|Ensembl:ENSRNOP00000063511.5, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000063511.5}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000063511.5};
RA   Doris P.A., Kalbfleisch T., Li K., Howe K., Wood J.;
RT   "GRCr8: a new rat reference genome assembly contstructed from accurate long
RT   reads and long range scaffolding.";
RL   Submitted (JAN-2024) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000063511.5}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000063511.5};
RG   Ensembl;
RL   Submitted (JAN-2026) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = N(6)-
CC         methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine + H(+);
CC         Xref=Rhea:RHEA:60280, Rhea:RHEA-COMP:15542, Rhea:RHEA-COMP:15546,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.367;
CC         Evidence={ECO:0000256|ARBA:ARBA00094048};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60281;
CC         Evidence={ECO:0000256|ARBA:ARBA00094048};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine
CC         = N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-
CC         homocysteine + H(+); Xref=Rhea:RHEA:60284, Rhea:RHEA-COMP:15541,
CC         Rhea:RHEA-COMP:15542, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929, ChEBI:CHEBI:61976;
CC         Evidence={ECO:0000256|ARBA:ARBA00093936};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60285;
CC         Evidence={ECO:0000256|ARBA:ARBA00093936};
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   RefSeq; XP_017447361.1; XM_017591872.3.
DR   AlphaFoldDB; D4A005; -.
DR   PeptideAtlas; D4A005; -.
DR   Ensembl; ENSRNOT00000066777.5; ENSRNOP00000063511.5; ENSRNOG00000007242.9.
DR   GeneID; 362078; -.
DR   AGR; RGD:1307588; -.
DR   CTD; 79813; -.
DR   RGD; 1307588; Ehmt1.
DR   VEuPathDB; HostDB:ENSRNOG00000007242; -.
DR   eggNOG; KOG1082; Eukaryota.
DR   GeneTree; ENSGT00940000156002; -.
DR   HOGENOM; CLU_005790_3_0_1; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000007242; Expressed in thymus and 19 other cell types or tissues.
DR   ExpressionAtlas; D4A005; baseline and differential.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0070742; F:C2H2 zinc finger domain binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0046976; F:histone H3K27 methyltransferase activity; IEA:UniProtKB-ARBA.
DR   GO; GO:0140948; F:histone H3K9 monomethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0002039; F:p53 binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006346; P:DNA methylation-dependent constitutive heterochromatin formation; IEA:UniProtKB-ARBA.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:UniProtKB-ARBA.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR   CDD; cd20905; EHMT_ZBD; 1.
DR   CDD; cd10535; SET_EHMT1; 1.
DR   FunFam; 2.170.270.10:FF:000005; Euchromatic histone-lysine N-methyltransferase 2; 1.
DR   FunFam; 1.25.40.20:FF:000029; histone-lysine N-methyltransferase EHMT1 isoform X2; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR043550; EHMT1/EHMT2.
DR   InterPro; IPR047762; EHMT_CRR.
DR   InterPro; IPR007728; Pre-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR038035; SET_EHMT1.
DR   PANTHER; PTHR46307; G9A, ISOFORM B; 1.
DR   PANTHER; PTHR46307:SF2; HISTONE-LYSINE N-METHYLTRANSFERASE EHMT1; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF13637; Ank_4; 1.
DR   Pfam; PF21533; EHMT1-2_CRR; 1.
DR   Pfam; PF05033; Pre-SET; 1.
DR   Pfam; PF00856; SET; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 7.
DR   SMART; SM00468; PreSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 5.
DR   PROSITE; PS50088; ANK_REPEAT; 5.
DR   PROSITE; PS50867; PRE_SET; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:D4A005};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   REPEAT          736..768
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          769..801
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          802..826
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          836..868
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          902..934
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          1024..1087
FT                   /note="Pre-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50867"
FT   DOMAIN          1090..1207
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   REGION          46..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          146..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          352..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          617..651
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1238..1262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..103
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..120
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..162
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..191
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        356..374
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..405
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        406..428
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..464
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1206
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00190"
SQ   SEQUENCE   1262 AA;  138268 MW;  AE81C22796BF4DEB CRC64;
     MARGRGGATL RARAMAAADA EQAVLAKQET KQDCCMKTEL LREDTLMAAD EGSTEKQAGE
     TPMAADGETN GSCEKSGDIS HPNAPKHTQE NTRASPQEGT NRVSRVAENG VSERDTEVGK
     QNHVTADDFM QTSVIGSNGY FLNKPALQGQ PLRTPNTLNS SLPGHAAKTL PGGASKCRTP
     SALPQTPTTA PTVPGEGSAD TEDRKPTASG TDVRVHRARK TMPKSILGLH AASKDHREVQ
     DHKEPKEDIN RNISECGRQQ LLPTFPALHQ SLPQNQCYMA TTKSQTACLP FVLAAAVSRK
     KKRRMGTYSL VPKKKTKVLK QRTVIEMFKS ITHSTVGAKG EKVLDDSALH VNGESLEMDS
     EEEDSEELED EEDRGAEQAA AFPTEDSRTS KESMSETDRA AKMDGDSEEE QESPDTGEDE
     DGGDESDLSS ESSIKKKFLK RRGKTDSPWI KPARKRRRRS RKKPSSMLGS EACKSSPGSM
     EQAALGDSAG YMEVSLDSLD LRVRGILSSQ TENEGLANGP DVLETDGLHE VPLCSCRMET
     PKSREISTLA NNQCMATESV DHEGNFMECQ PESSISHRFH KDCASRVNNA SYCPHCGEET
     SKAKEVTIAK ADTTSTVTLA PGQEKSLAAE GRADTTTGSI AGAPEDEKSQ STVTQAPECF
     DPAGPAGFVR PTSGFSQGPG KETLESALIA LDSEKPKKLR FHPKQLYFSA RQGELQKVLL
     MLVDGIDPNF KMEHQSKRSP LHAAAEAGHV DICHMLVQAG ANIDTCSEDQ RTPLMEAAEN
     NHLDAVKYLI KAGAQVDPKD AEGSTCLHLA AKKGHYDVVQ YLLSNGQMDV NCQDDGGWTP
     MIWATEYKHV DLVKLLLSKG SDINIRDNEE NICLHWAAFS GCVDIAEILL AAKCDLHAVN
     IHGDSPLHIA ARENRYDCVV LFLSRDSDVT LKNKEGETPL QCASLNSQVW SALQMSKALQ
     DSAPDKPVAV EKTVSRDIAR GYERIPIPCV NAVDSELCPT NYKYVSQNCV TSPMNIDRNI
     THLQYCVCVD DCSSSTCMCG QLSMRCWYDK DGRLLPEFNM AEPPLIFECN HACSCWRNCR
     NRVVQNGLRA RLQLYRTQDM GWGVRSLQDI PLGTFVCEYV GELISDSEAD VREEDSYLFD
     LDNKDGEVYC IDARFYGNVS RFINHHCEPN LVPVRVFMSH QDLRFPRIAF FSTRLIQAGE
     QLGFDYGERF WDVKGKLFSC RCGSPKCRHS SAALAQRQAS AAQEAQENGL PDTSSAAAAD
     PL
//