PRD15_MOUSE
ID PRD15_MOUSE Reviewed; 1174 AA.
AC E9Q8T2; E9Q6A1; Q3UML7;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=PR domain zinc finger protein 15 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000305};
DE AltName: Full=PR domain-containing protein 15 {ECO:0000305};
GN Name=Prdm15 {ECO:0000312|MGI:MGI:1930121};
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] (ISOFORM 2).
RC TISSUE=Lung;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=28740264; DOI=10.1038/ng.3922;
RA Mzoughi S., Zhang J., Hequet D., Teo S.X., Fang H., Xing Q.R., Bezzi M.,
RA Seah M.K.Y., Ong S.L.M., Shin E.M., Wollmann H., Wong E.S.M.,
RA Al-Haddawi M., Stewart C.L., Tergaonkar V., Loh Y.H., Dunn N.R.,
RA Messerschmidt D.M., Guccione E.;
RT "PRDM15 safeguards naive pluripotency by transcriptionally regulating WNT
RT and MAPK-ERK signaling.";
RL Nat. Genet. 49:1354-1363(2017).
CC -!- FUNCTION: Sequence-specific DNA-binding transcriptional regulator.
CC Plays a role as a molecular node in a transcriptional network
CC regulating embryonic development and cell fate decision. Stimulates the
CC expression of upstream key transcriptional activators and repressors of
CC the Wnt/beta-catenin and MAPK/ERK pathways, respectively, that are
CC essential for naive pluripotency and self-renewal maintenance of
CC embryonic stem cells (ESCs). Specifically promotes SPRY1 and RSPO1
CC transcription activation through recognition and direct binding of a
CC specific DNA sequence in their promoter regions. Also plays a role in
CC induced pluripotent stem cells (iPSCs) reprogramming. Involved in early
CC embryo development. {ECO:0000269|PubMed:28740264}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28740264}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=E9Q8T2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=E9Q8T2-2; Sequence=VSP_059647;
CC -!- TISSUE SPECIFICITY: Expressed in embryonic stem cells (ESCs) (at
CC protein level). {ECO:0000269|PubMed:28740264}.
CC -!- DISRUPTION PHENOTYPE: Mice die before birth and show early
CC postimplantation developmental defect. Display reduced embryonic stem
CC cells (ESCs) proliferation and self-renewal capacity. Show altered
CC transcription of naive pluripotency and self-renewal modulator genes.
CC {ECO:0000269|PubMed:28740264}.
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DR EMBL; AK144820; BAE26081.1; -; mRNA.
DR EMBL; AC121560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS49926.1; -. [E9Q8T2-1]
DR CCDS; CCDS88979.1; -. [E9Q8T2-2]
DR RefSeq; NP_659038.2; NM_144789.2. [E9Q8T2-1]
DR RefSeq; XP_006522932.1; XM_006522869.3. [E9Q8T2-2]
DR AlphaFoldDB; E9Q8T2; -.
DR SMR; E9Q8T2; -.
DR STRING; 10090.ENSMUSP00000093533; -.
DR iPTMnet; E9Q8T2; -.
DR PhosphoSitePlus; E9Q8T2; -.
DR MaxQB; E9Q8T2; -.
DR PaxDb; E9Q8T2; -.
DR PRIDE; E9Q8T2; -.
DR ProteomicsDB; 316119; -. [E9Q8T2-1]
DR ProteomicsDB; 363369; -.
DR Antibodypedia; 9262; 104 antibodies from 20 providers.
DR Ensembl; ENSMUST00000095849; ENSMUSP00000093533; ENSMUSG00000014039. [E9Q8T2-1]
DR Ensembl; ENSMUST00000121584; ENSMUSP00000113791; ENSMUSG00000014039. [E9Q8T2-2]
DR GeneID; 114604; -.
DR KEGG; mmu:114604; -.
DR UCSC; uc012ajc.1; mouse. [E9Q8T2-1]
DR CTD; 63977; -.
DR MGI; MGI:1930121; Prdm15.
DR VEuPathDB; HostDB:ENSMUSG00000014039; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000157890; -.
DR HOGENOM; CLU_004140_2_0_1; -.
DR InParanoid; E9Q8T2; -.
DR OMA; PVPKFTH; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; E9Q8T2; -.
DR TreeFam; TF331419; -.
DR BioGRID-ORCS; 114604; 7 hits in 77 CRISPR screens.
DR ChiTaRS; Prdm15; mouse.
DR PRO; PR:E9Q8T2; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; E9Q8T2; protein.
DR Bgee; ENSMUSG00000014039; Expressed in superior cervical ganglion and 239 other tissues.
DR ExpressionAtlas; E9Q8T2; baseline and differential.
DR Genevisible; E9Q8T2; MM.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IMP:UniProtKB.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:2000035; P:regulation of stem cell division; IMP:UniProtKB.
DR CDD; cd19199; PR-SET_PRDM15; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR044409; PRDM15_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; PF00096; zf-C2H2; 6.
DR SMART; SM00355; ZnF_C2H2; 17.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 16.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 15.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Developmental protein; DNA-binding;
KW Isopeptide bond; Metal-binding; Methyltransferase; Nucleus;
KW Reference proteome; Repeat; Repressor; S-adenosyl-L-methionine;
KW Transcription; Transcription regulation; Transferase; Ubl conjugation;
KW Zinc; Zinc-finger.
FT CHAIN 1..1174
FT /note="PR domain zinc finger protein 15"
FT /id="PRO_0000444718"
FT DOMAIN 75..185
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT ZN_FING 402..424
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 434..457
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 468..486
FT /note="C2H2-type 3; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 495..517
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 522..544
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 571..593
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 598..620
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 661..684
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 689..711
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 725..747
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 753..775
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 781..803
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 809..831
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 837..859
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 865..888
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 252..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 957..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1147..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1157..1174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 552
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P57071"
FT VAR_SEQ 1..26
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_059647"
FT CONFLICT 298
FT /note="R -> I (in Ref. 1; BAE26081)"
FT /evidence="ECO:0000305"
FT CONFLICT 609
FT /note="R -> L (in Ref. 1; BAE26081)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1174 AA; 132870 MW; 2C12468F8E056D76 CRC64;
MCPPTIWEKG GQVGARWSLR APEVSAMAED GSEEIMFIWC EDCSQYHDSE CPELGPVVMV
KDSFVLSRAR SSLPSNLEIR RLDDGAEGVF AVTQLVKRTQ FGPFESRRVA KWEKESAFPL
KVFQKDGHPV CFDTSNEDDC NWMMLVRPAL EPGHQNLTAY QHGSDVYFTT SKDIPAGTEL
RVWYAAFYAK KMDKPMLKQA CSSVQAAGTP EPSVSVEPER GQWVCKVCSN TFLELQLLNE
HLLGHLEQAK SLPAGGQQHE AASEKEPDAP RMEPPTAAES KSIQSVMVTK EPKKKPRRGR
KPKASKVEQP LVIIKDKEPS EHVAEIITEI PPDEPVSATP DERIMELVLG KLAAPTNEAS
SVPKFPHHPS STIALKRGLV LSSRHGVRRK LVRQLGEHKR IHQCGTCSKV FQNSSNLSRH
VRSHGECAHG DKLFKCEECS KLFSRKESLK QHVSYKHSRN EVDGEYRYRC GSCGKTFRME
SALEFHNCRT DDKTFQCEMC FRFFSTNSNL SKHKKKHGDK KFACEVCSKM FYRKDVMLDH
QRRHLDGVRR VKREDLEASG ESLVRYKKEP SGCPVCGKVF SCRSNMNKHL LTHGDKKYTC
EICGRKFFRV DVLRDHIHVH FKDIALMDDH QREEFIGKIG ISSEENDDNS DESADSEPHK
YSCKRCQLTF GRGKEYLKHI MEVHKEKGHG CSICHRRFAL KATYHAHMVI HRENLPDPNV
QKYIHPCEIC GRIFNSIGNL ERHKLIHTGV KSHACEQCGK SFARKDMLKE HMRVHDNIRE
YLCAECGKGM KTKHALRHHM KLHKGIKEYE CKECHRKFAQ KVNMLKHYKR HTGIKDFMCE
LCGKTFSERN TMETHKLIHT VGKQWTCSVC DKKYVTEYML QKHVQLTHDK VEAQSCQLCG
TKVSTRASMS RHMRRKHPEV LAVRIDDLDH LPETTTIDAS SIGIVQPALG LEQEELAEGK
HGKAAKRSHK RKQKPEEEAG APVPEDTTFS EYPEKEPEFT GSVGDETNSA VQSIQQVVVT
LGDPNVTAPS SSVGLTNITV TPITTAAGTQ FTNLQPVAVG HLTNPDRQLQ LDNSILTVTF
DTVSGSAMLH NRQNDVQIHP QPEATNPQSV AHFINLTTLV NSITPLGNQL SEQHPLTWRA
VPQTDVLQPP QAPAAPQQAV QPQVQNEQQQ MYSY
