PRDM6_BOVIN
ID PRDM6_BOVIN Reviewed; 590 AA.
AC A6QPM3;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Putative histone-lysine N-methyltransferase PRDM6;
DE EC=2.1.1.361 {ECO:0000250|UniProtKB:Q3UZD5};
DE AltName: Full=PR domain zinc finger protein 6;
DE AltName: Full=PR domain-containing protein 6;
GN Name=PRDM6;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal spinal cord;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Putative histone methyltransferase that acts as a
CC transcriptional repressor of smooth muscle gene expression. Promotes
CC the transition from differentiated to proliferative smooth muscle by
CC suppressing differentiation and maintaining the proliferative potential
CC of vascular smooth muscle cells. Also plays a role in endothelial cells
CC by inhibiting endothelial cell proliferation, survival and
CC differentiation. It is unclear whether it has histone methyltransferase
CC activity in vivo. According to some authors, it does not act as a
CC histone methyltransferase by itself and represses transcription by
CC recruiting EHMT2/G9a. According to others, it possesses histone
CC methyltransferase activity when associated with other proteins and
CC specifically methylates 'Lys-20' of histone H4 in vitro. 'Lys-20'
CC methylation represents a specific tag for epigenetic transcriptional
CC repression. {ECO:0000250|UniProtKB:Q3UZD5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60344, Rhea:RHEA-COMP:15554, Rhea:RHEA-COMP:15555,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.361;
CC Evidence={ECO:0000250|UniProtKB:Q3UZD5};
CC -!- SUBUNIT: Interacts with HDAC1, HDAC2, HDAC3, CBX1 and EP300.
CC {ECO:0000250|UniProtKB:Q3UZD5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q3UZD5}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; BC149387; AAI49388.1; -; mRNA.
DR RefSeq; NP_001096725.1; NM_001103255.2.
DR AlphaFoldDB; A6QPM3; -.
DR SMR; A6QPM3; -.
DR STRING; 9913.ENSBTAP00000027421; -.
DR PaxDb; A6QPM3; -.
DR Ensembl; ENSBTAT00000027421; ENSBTAP00000027421; ENSBTAG00000020578.
DR GeneID; 519857; -.
DR KEGG; bta:519857; -.
DR CTD; 93166; -.
DR VEuPathDB; HostDB:ENSBTAG00000020578; -.
DR VGNC; VGNC:33298; PRDM6.
DR eggNOG; KOG1721; Eukaryota.
DR eggNOG; KOG2461; Eukaryota.
DR GeneTree; ENSGT00940000155852; -.
DR HOGENOM; CLU_032452_0_0_1; -.
DR InParanoid; A6QPM3; -.
DR OMA; IGPFQGI; -.
DR OrthoDB; 1318335at2759; -.
DR TreeFam; TF106403; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000020578; Expressed in aorta and 72 other tissues.
DR ExpressionAtlas; A6QPM3; baseline.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042054; F:histone methyltransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR CDD; cd19191; PR-SET_PRDM6; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR044416; PRDM6_PR-SET.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00317; SET; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57667; SSF57667; 2.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 2: Evidence at transcript level;
KW Chromatin regulator; Metal-binding; Methyltransferase; Nucleus;
KW Reference proteome; Repeat; Repressor; S-adenosyl-L-methionine;
KW Transcription; Transcription regulation; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..590
FT /note="Putative histone-lysine N-methyltransferase PRDM6"
FT /id="PRO_0000363958"
FT DOMAIN 241..360
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT ZN_FING 468..490
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 496..518
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 524..546
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 552..574
FT /note="C2H2-type 4; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 25..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..61
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 590 AA; 63989 MW; B7D55FF617059231 CRC64;
MLKPGDPGGS AFLKVDPAYL QHWQQLFPHG GGGPLKGGGA AGPLGAPQPL QPPPPPERAE
PQPDSLRPRP ASLSSASSTP ASSSTSASSA SSCAAAAAAA AAAALAGLSA LPVAQLPVFA
PLATVAAEPL PPKDLCLGAT SGPGPSKCGG SGGDGRGVPR FRCSAEELDY YLYGQQRMEI
IPLNQHTSDP NNRCDMCADN RNGECPMHGP LHSLRRLVGT SSAAAAAPPP ELPEWLRDLP
REVCLCTSTV PGLAYGICAA QRIQQGTWIG PFQGVLLPPE KVQAGAVRNT QHLWEIYDQD
GTLQHFIDGG EPSKSSWMRY IRCARHCGEQ NLTVVQYRSN IFYRACIDIP RGTELLVWYN
DSYTSFFGIP LQCIAQDENL NVPSTVMEAM CRQDALQPFN KSSKLSQAPQ QRSVVFPQTP
CGRNFSLLDK SGPLESGFNQ ISVKNQRVLA SPTSTSQLHS EFSDWHLWKC GQCFKTFTQR
ILLQMHVCTQ NPDRPYQCGH CSQSFSQPSE LRNHVVTHSS DRPFKCGYCG RAFAGATTLN
NHIRTHTGEK PFKCERCERS FTQATQLSRH QRMPNECKPI TESPESIEVD
