GenomeNet

Database: UniProt
Entry: Q8BZ97
LinkDB: Q8BZ97
Original site: Q8BZ97 
ID   PRDM8_MOUSE             Reviewed;         687 AA.
AC   Q8BZ97;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JAN-2019, entry version 104.
DE   RecName: Full=PR domain zinc finger protein 8;
DE            EC=2.1.1.-;
DE   AltName: Full=PR domain-containing protein 8;
GN   Name=Prdm8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=19646955; DOI=10.1016/j.bbrc.2009.07.134;
RA   Eom G.H., Kim K., Kim S.M., Kee H.J., Kim J.Y., Jin H.M., Kim J.R.,
RA   Kim J.H., Choe N., Kim K.B., Lee J., Kook H., Kim N., Seo S.B.;
RT   "Histone methyltransferase PRDM8 regulates mouse testis
RT   steroidogenesis.";
RL   Biochem. Biophys. Res. Commun. 388:131-136(2009).
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INTERACTION
RP   WITH BHLHE22.
RX   PubMed=22284184; DOI=10.1016/j.neuron.2011.09.035;
RA   Ross S.E., McCord A.E., Jung C., Atan D., Mok S.I., Hemberg M.,
RA   Kim T.K., Salogiannis J., Hu L., Cohen S., Lin Y., Harrar D.,
RA   McInnes R.R., Greenberg M.E.;
RT   "Bhlhb5 and Prdm8 form a repressor complex involved in neuronal
RT   circuit assembly.";
RL   Neuron 73:292-303(2012).
RN   [4]
RP   TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=26023183; DOI=10.1073/pnas.1505870112;
RA   Jung C.C., Atan D., Ng D., Ploder L., Ross S.E., Klein M., Birch D.G.,
RA   Diez E., McInnes R.R.;
RT   "Transcription factor PRDM8 is required for rod bipolar and type 2
RT   OFF-cone bipolar cell survival and amacrine subtype identity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:E3010-E3019(2015).
CC   -!- FUNCTION: Probable histone methyltransferase, preferentially
CC       acting on 'Lys-9' of histone H3 (PubMed:19646955). Histone
CC       methyltransferase activity has not been confirmed in other
CC       species. Involved in the control of steroidogenesis through
CC       transcriptional repression of steroidogenesis marker genes such as
CC       CYP17A1 and LHCGR (PubMed:19646955). Forms with BHLHE22 a
CC       transcriptional repressor complex controlling genes involved in
CC       neural development and neuronal differentiation (PubMed:22284184).
CC       In the retina, it is required for rod bipolar and type 2 OFF-cone
CC       bipolar cell survival (PubMed:26023183).
CC       {ECO:0000269|PubMed:19646955, ECO:0000269|PubMed:22284184,
CC       ECO:0000269|PubMed:26023183}.
CC   -!- SUBUNIT: Interacts with BHLHE22 (PubMed:22284184). Interacts with
CC       EPM2A and NHLRC1. This interaction sequesters EPM2A and NHLRC1 to
CC       the nucleus (By similarity). {ECO:0000250|UniProtKB:Q9NQV8,
CC       ECO:0000269|PubMed:22284184}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19646955}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain, heart, liver, testes,
CC       retina (PubMed:19646955, PubMed:22284184). Highest expression is
CC       observed in the retina and hippocampus; moderately expressed in
CC       the cortex and cerebellum. In the retina, it is expressed in
CC       bipolar and amacrine cells (PubMed:26023183).
CC       {ECO:0000269|PubMed:19646955, ECO:0000269|PubMed:22284184,
CC       ECO:0000269|PubMed:26023183}.
CC   -!- DISRUPTION PHENOTYPE: Knockout mice lacking PRDM8 shows absence of
CC       the corticospinal tract, agenesis of the corpus callosum and
CC       hippocampal commissure; they have an abnormal itching behavior
CC       that results in the formation of skin lesions, and occasionally
CC       display an unusual movement in which they walk on their forepaws
CC       (PubMed:22284184). PRDM8-null mice also have a non-progressive
CC       defect in retinal responses, and loss of rod bipolar and type 2
CC       OFF-cone bipolar cells (PubMed:26023183).
CC       {ECO:0000269|PubMed:22284184, ECO:0000269|PubMed:26023183}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
DR   EMBL; AK036202; BAC29345.1; -; mRNA.
DR   RefSeq; NP_084223.2; NM_029947.2.
DR   UniGene; Mm.332511; -.
DR   ProteinModelPortal; Q8BZ97; -.
DR   BioGrid; 218812; 1.
DR   STRING; 10090.ENSMUSP00000108583; -.
DR   iPTMnet; Q8BZ97; -.
DR   PhosphoSitePlus; Q8BZ97; -.
DR   MaxQB; Q8BZ97; -.
DR   PaxDb; Q8BZ97; -.
DR   PRIDE; Q8BZ97; -.
DR   GeneID; 77630; -.
DR   KEGG; mmu:77630; -.
DR   CTD; 56978; -.
DR   MGI; MGI:1924880; Prdm8.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; KOG2461; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   HOVERGEN; HBG053674; -.
DR   InParanoid; Q8BZ97; -.
DR   KO; K20797; -.
DR   OrthoDB; 1327331at2759; -.
DR   PhylomeDB; Q8BZ97; -.
DR   PRO; PR:Q8BZ97; -.
DR   Proteomes; UP000000589; Unplaced.
DR   GO; GO:0035097; C:histone methyltransferase complex; IC:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042054; F:histone methyltransferase activity; IDA:MGI.
DR   GO; GO:0046974; F:histone methyltransferase activity (H3-K9 specific); IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003714; F:transcription corepressor activity; IMP:MGI.
DR   GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IMP:MGI.
DR   GO; GO:0021540; P:corpus callosum morphogenesis; IMP:MGI.
DR   GO; GO:0021957; P:corticospinal tract morphogenesis; IMP:MGI.
DR   GO; GO:0051567; P:histone H3-K9 methylation; IDA:MGI.
DR   GO; GO:0016571; P:histone methylation; IDA:MGI.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR   GO; GO:0022008; P:neurogenesis; IDA:MGI.
DR   GO; GO:0014003; P:oligodendrocyte development; IBA:GO_Central.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; DNA-binding; Metal-binding; Methyltransferase;
KW   Neurogenesis; Nucleus; Reference proteome; Repeat;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Zinc; Zinc-finger.
FT   CHAIN         1    687       PR domain zinc finger protein 8.
FT                                /FTId=PRO_0000047765.
FT   DOMAIN       16    131       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   ZN_FING     154    182       C2H2-type 1; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   ZN_FING     624    647       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   COMPBIAS    202    207       Poly-Gly.
FT   COMPBIAS    210    219       Poly-Gln.
FT   COMPBIAS    284    488       Gly-rich.
FT   COMPBIAS    539    597       Ala-rich.
SQ   SEQUENCE   687 AA;  70886 MW;  B33B2DEBC3512B3E CRC64;
     MEDSGIQRGI WDGDAKAVQQ CLTDIFTSVY TTCDIPENAI FGPCVLSHTS LYDSIAFVAL
     KSTDKRTVPY IFRVDTSAAN GSSEGLMWLR LVQSARDKEE QNLEAYIKNG QLFYRSLRRI
     AKDEELLVWY GKELTELLLL CPSRAHKMNG SSPYTCLECS QRFQFEFPYV AHLRFRCPKR
     LHSTDANPQD EQGGGLGTKD HGGGGGGKEQ QQQQQQQQQE APLIPGPKFC KAGPIHHYPA
     SSPEASNPPG SAGASSAKPS TDFHNLAREL ENSRGNSSCV AAPGVGSGGS GHQEAELSPD
     GVATGGCKGK RRFPEEAAAE GGGAGLAGGR ARFSERPLAT SKEELVCTPQ QYRAAGSYFG
     LEENGRLFAP PSPETGEAKR SAFVEVKKAG RAVGLQEEAA ATDGAGGTAE DPDAGGGVAG
     GGSNGSSTPA AGSPGAPEKL LAPRPGGSLP GRLEGGSPAR GSAFTSVSQL GGGGGAGTAG
     TAGGSGGGQT AASDERKSAF SQPARSFSQL SPLVLGQKLG ALEPCHPGDG VGPTRLYPAA
     ADPLAVKLQG AADLNGACGP LASGGGGGLP KQSPFLYATA FWPKSSAAAA AAAAAAAGPL
     QLQLPSALTL LPPSFTSLCL PAQNWCAKCN ASFRMTSDLV YHMRSHHKKE YAMEPLVKAA
     AGGETQVPHL QRVLQGASPP VPAHDLA
//
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