ID PRDM2_RAT Reviewed; 1706 AA.
AC Q63755;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-APR-2013, entry version 98.
DE RecName: Full=PR domain zinc finger protein 2;
DE EC=2.1.1.43;
DE AltName: Full=PR domain-containing protein 2;
DE AltName: Full=Retinoblastoma protein-interacting zinc finger protein;
DE AltName: Full=Zinc finger protein RIZ;
GN Name=Prdm2; Synonyms=Riz;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=7538672; DOI=10.1073/pnas.92.10.4467;
RA Buyse I.M., Shao G., Huang S.;
RT "The retinoblastoma protein binds to RIZ, a zinc-finger protein that
RT shares an epitope with the adenovirus E1A protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:4467-4471(1995).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent histone
CC methyltransferase that specifically methylates 'Lys-9' of histone
CC H3. May function as a DNA-binding transcription factor. Binds to
CC the macrophage-specific TPA-responsive element (MTE) of the HMOX1
CC (heme oxygenase 1) gene and may act as a transcriptional activator
CC of this gene (By similarity).
CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC -!- SUBUNIT: Binds to the retinoblastoma protein (RB). Interacts with
CC GATA3 (By similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC -!- SIMILARITY: Contains 8 C2H2-type zinc fingers.
CC -!- SIMILARITY: Contains 1 SET domain.
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DR EMBL; U17837; AAA74468.1; -; mRNA.
DR IPI; IPI00327589; -.
DR RefSeq; NP_001071116.1; NM_001077648.1.
DR UniGene; Rn.202632; -.
DR ProteinModelPortal; Q63755; -.
DR SMR; Q63755; 1-160.
DR DIP; DIP-473N; -.
DR STRING; 10116.ENSRNOP00000046011; -.
DR PhosphoSite; Q63755; -.
DR PaxDb; Q63755; -.
DR PRIDE; Q63755; -.
DR GeneID; 313678; -.
DR KEGG; rno:313678; -.
DR UCSC; RGD:1594531; rat.
DR CTD; 7799; -.
DR RGD; 1594531; Prdm2.
DR eggNOG; NOG258873; -.
DR HOGENOM; HOG000231078; -.
DR HOVERGEN; HBG053671; -.
DR InParanoid; Q63755; -.
DR KO; K11432; -.
DR OrthoDB; EOG48D0TG; -.
DR NextBio; 666643; -.
DR ArrayExpress; Q63755; -.
DR Genevestigator; Q63755; -.
DR GermOnline; ENSRNOG00000033522; Rattus norvegicus.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0034968; P:histone lysine methylation; IEA:GOC.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0032355; P:response to estradiol stimulus; IDA:RGD.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 3.30.160.60; -; 1.
DR InterPro; IPR009170; RIZ_retinblastoma-bd_prot.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR007087; Znf_C2H2.
DR InterPro; IPR015880; Znf_C2H2-like.
DR InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF00096; zf-C2H2; 2.
DR PIRSF; PIRSF002395; RIZ_SET; 1.
DR SMART; SM00317; SET; 1.
DR SMART; SM00355; ZnF_C2H2; 8.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 2: Evidence at transcript level;
KW Activator; Complete proteome; DNA-binding; Metal-binding;
KW Methyltransferase; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Transferase; Zinc; Zinc-finger.
FT CHAIN 1 1706 PR domain zinc finger protein 2.
FT /FTId=PRO_0000047759.
FT DOMAIN 26 144 SET.
FT ZN_FING 355 377 C2H2-type 1.
FT ZN_FING 385 407 C2H2-type 2.
FT ZN_FING 476 499 C2H2-type 3.
FT ZN_FING 1123 1145 C2H2-type 4.
FT ZN_FING 1151 1174 C2H2-type 5.
FT ZN_FING 1180 1203 C2H2-type 6.
FT ZN_FING 1321 1343 C2H2-type 7; atypical.
FT ZN_FING 1443 1465 C2H2-type 8; atypical.
FT COMPBIAS 246 327 Glu-rich.
FT COMPBIAS 893 1067 Pro-rich.
FT COMPBIAS 1472 1565 Ser-rich.
SQ SEQUENCE 1706 AA; 187555 MW; 55EA419491D2D68C CRC64;
MHQNTESVAA TETLAEVPEH VLRGLPEEVR LFPSAVDKTR IGVWATKPIL KGKKFGPFVG
DKKKRSQVRN NVYMWEVYYP NLGWMCIDAT DPEKGNWLRY VNWACSGEEQ NLFPLEINRA
IYYKTLKPIA PGEELLVWYN GEDNPEIAAA IEEERASARS KRSSPKSRRG KKKSHENKNK
GIRTHPTQLK ASELDSTFAN MRGSAEGPKE EDERPLASAP EQPAPLPEVG NQDAVPQVAI
PLPACEPQPE VDGKQEVTDC EVNDVEEEEL EEEEELEEEE EEELGEDGVE EADMPNESSA
KEPEIRCEEK PEDLLEEPQS MSNEAREDSP DVTPPPHTPR AREEANGDVL ETFMFPCQHC
ERKFATKQGL ERHMHIHIST INHAFKCKYC GKRFGTQINR RRHERRHETG LKRRPSMTLQ
SSEDPDDGKG ENVTSKDESS PPQLGQDCLI LNSEKTSQEV LNSSFVEENG EVKELHPCKY
CKKVFGTHTN MRRHQRRVHE RHLIPKGVRR KGGLLEEPQP PAEQAPPSQN VYVPSTEPEE
EGETDDVYIM DISSNISENL NYYIDGKIQT NSSTSNCDVI EMESNSAHLY GIDCLLTPVT
VEITQNIKST QVSVTDDLLK DSPSSTNCES KKRRTASPPV LPKIKTETES DSTAPSCSLS
LPLSISTAEV VSFHKEKGVY LSSKLKQLLQ TQDKLTLPAG FSAAEIPKLG PVCASAPASM
LPVTSSRFKR RTSSPPSSPQ HSPALRDFGK PNDGKAAWTD TVLTSKKPKL ESRSDSPAWS
LSGRDERETG SPPCFDEYKI SKEWAASSTF SSVCNQQPLD LSSGVKQKSE GTGKTPVPWE
SVLDLSVHKK PCDSEGKEFK ENHLAQPAAK KKKPTTCMLQ KVLLNEYNGV SLPTETTPEV
TRSPSPCKSP DTQPDPELGP DSSCSVPTAE SPPEVVGPSS PPLQTASLSS GQLPPLLTPT
EPSSPPPCPP VLTVATPPPP LLPTVPLSHP SSDASPQQCP SPFSNTTAQS PLPILSPTVS
PSPSPIPPVE PLMSAASPGP PTLSSSSSSS SSFPSSSCSS TSPSPPPLSA VSSVVSSGDN
LEASLPAVTF KQEESESEGL KPKEEAPPAG GQSVVQETFS KNFICNVCES PFLSIKDLTK
HLSVHAEEWP FKCEFCVQLF KVKTDLSEHR FLLHGVGNIF VCSVCKKEFA FLCNLQQHQR
DLHPDEVCTH HEFESGTLRP QNFTDPSKAN VEHMPSLPEE PLETSREEEL NDSSEELYTT
IKIMASGIKT KDPDVRLGLN QHYPSFKPPP FQYHHRNPMG IGVTATNFTT HNIPQTFTTA
IRCTKCGKGV DNMPELHKHI LACASASDKK RYTPKKNPVP LKQTVQPKNG VVVLDNSGKN
AFRRMGQPKR LSFNVELGKM SPNKLKLSAL KKKNQLVQKA ILQKNRAAKQ KADLRDTSEA
SSHICPYCDR EFTYIGSLNK HAAFSCPKKP LSPSKRKVSH SSKKGGHASS SSSDRNSSCH
PRRRTADTEI KMQSTQAPLG KTRARSTGPA QASLPSSSFR SRQNVKFAAS VKSKKASSSS
LRNSSPIRMA KITHVEGKKP KAVAKSHSAQ LSSKSSRGLH VRVQKSKAVI QSKTALASKR
RTDRFIVKSR ERSGGPITRS LQLAAAADLS ESRREDSSAR HELKDFSYSL RLASRCGSST
ASYITRQCRK VKAAAATPFQ GPFLKE
//
