PRDM8_MOUSE
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 03-AUG-2022, entry version 115.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., 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 steroidogenesis.";
RL Biochem. Biophys. Res. Commun. 388:131-136(2009).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INTERACTION WITH
RP 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., Kim T.K.,
RA Salogiannis J., Hu L., Cohen S., Lin Y., Harrar D., McInnes R.R.,
RA Greenberg M.E.;
RT "Bhlhb5 and Prdm8 form a repressor complex involved in neuronal circuit
RT 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 OFF-cone
RT 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 acting on
CC 'Lys-9' of histone H3 (PubMed:19646955). Histone methyltransferase
CC activity has not been confirmed in other species. Involved in the
CC control of steroidogenesis through transcriptional repression of
CC steroidogenesis marker genes such as CYP17A1 and LHCGR
CC (PubMed:19646955). Forms with BHLHE22 a transcriptional repressor
CC complex controlling genes involved in neural development and neuronal
CC differentiation (PubMed:22284184). In the retina, it is required for
CC rod bipolar and type 2 OFF-cone bipolar cell survival
CC (PubMed:26023183). {ECO:0000269|PubMed:19646955,
CC ECO:0000269|PubMed:22284184, ECO:0000269|PubMed:26023183}.
CC -!- SUBUNIT: Interacts with BHLHE22 (PubMed:22284184). Interacts with EPM2A
CC and NHLRC1. This interaction sequesters EPM2A and NHLRC1 to the nucleus
CC (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, retina
CC (PubMed:19646955, PubMed:22284184). Highest expression is observed in
CC the retina and hippocampus; moderately expressed in the cortex and
CC cerebellum. In the retina, it is expressed in bipolar and amacrine
CC cells (PubMed:26023183). {ECO:0000269|PubMed:19646955,
CC ECO:0000269|PubMed:22284184, ECO:0000269|PubMed:26023183}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice lacking PRDM8 shows absence of the
CC corticospinal tract, agenesis of the corpus callosum and hippocampal
CC commissure; they have an abnormal itching behavior that results in the
CC formation of skin lesions, and occasionally display an unusual movement
CC in which they walk on their forepaws (PubMed:22284184). PRDM8-null mice
CC also have a non-progressive defect in retinal responses, and loss of
CC rod bipolar and type 2 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 methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; AK036202; BAC29345.1; -; mRNA.
DR RefSeq; NP_084223.2; NM_029947.2.
DR AlphaFoldDB; 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 ProteomicsDB; 289888; -.
DR DNASU; 77630; -.
DR GeneID; 77630; -.
DR KEGG; mmu:77630; -.
DR CTD; 56978; -.
DR MGI; MGI:1924880; Prdm8.
DR eggNOG; KOG1721; Eukaryota.
DR eggNOG; KOG2461; Eukaryota.
DR InParanoid; Q8BZ97; -.
DR OrthoDB; 1327331at2759; -.
DR PhylomeDB; Q8BZ97; -.
DR BioGRID-ORCS; 77630; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q8BZ97; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BZ97; protein.
DR GO; GO:0035097; C:histone methyltransferase complex; IC:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO: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 GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd19192; PR-SET_PRDM8; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR044402; PRDM8_PR/SET.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
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 DNA-binding; Metal-binding; Methyltransferase; Neurogenesis; Nucleus;
KW Reference proteome; Repeat; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..687
FT /note="PR domain zinc finger protein 8"
FT /id="PRO_0000047765"
FT DOMAIN 16..131
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT ZN_FING 154..182
FT /note="C2H2-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 624..647
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 184..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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
