PRDM5_MOUSE
ID PRDM5_MOUSE Reviewed; 599 AA.
AC Q9CXE0; B2RSK8;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=PR domain zinc finger protein 5;
DE EC=2.1.1.-;
DE AltName: Full=PR domain-containing protein 5;
GN Name=Prdm5;
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=Liver;
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].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Sequence-specific DNA-binding transcription factor. Represses
CC transcription at least in part by recruitment of the histone
CC methyltransferase EHMT2/G9A and histone deacetylases such as HDAC1.
CC Regulates hematopoiesis-associated protein-coding and microRNA (miRNA)
CC genes (By similarity). May regulate the expression of proteins involved
CC in extracellular matrix development and maintenance, connective tissue
CC components and molecules regulating cell migration and adhesion. May
CC cause G2/M arrest and apoptosis in cancer cells (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with EHMT2/G9A, GFI1 and HDAC1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; AK014501; BAB29400.1; -; mRNA.
DR EMBL; CH466523; EDK98780.1; -; Genomic_DNA.
DR EMBL; BC138901; AAI38902.1; -; mRNA.
DR EMBL; BC138902; AAI38903.1; -; mRNA.
DR CCDS; CCDS20208.1; -.
DR RefSeq; NP_081823.2; NM_027547.2.
DR AlphaFoldDB; Q9CXE0; -.
DR SMR; Q9CXE0; -.
DR BioGRID; 214249; 31.
DR IntAct; Q9CXE0; 1.
DR STRING; 10090.ENSMUSP00000031976; -.
DR PhosphoSitePlus; Q9CXE0; -.
DR PaxDb; Q9CXE0; -.
DR PRIDE; Q9CXE0; -.
DR ProteomicsDB; 291557; -.
DR Antibodypedia; 26690; 252 antibodies from 29 providers.
DR DNASU; 70779; -.
DR Ensembl; ENSMUST00000031976; ENSMUSP00000031976; ENSMUSG00000029913.
DR GeneID; 70779; -.
DR KEGG; mmu:70779; -.
DR UCSC; uc009cek.1; mouse.
DR CTD; 11107; -.
DR MGI; MGI:1918029; Prdm5.
DR VEuPathDB; HostDB:ENSMUSG00000029913; -.
DR eggNOG; KOG1721; Eukaryota.
DR eggNOG; KOG2461; Eukaryota.
DR GeneTree; ENSGT00940000158340; -.
DR HOGENOM; CLU_002678_75_0_1; -.
DR InParanoid; Q9CXE0; -.
DR OMA; IRTHTRX; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9CXE0; -.
DR TreeFam; TF106478; -.
DR BioGRID-ORCS; 70779; 3 hits in 76 CRISPR screens.
DR ChiTaRS; Prdm5; mouse.
DR PRO; PR:Q9CXE0; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9CXE0; protein.
DR Bgee; ENSMUSG00000029913; Expressed in humerus cartilage element and 204 other tissues.
DR ExpressionAtlas; Q9CXE0; baseline and differential.
DR Genevisible; Q9CXE0; MM.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISS:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016575; P:histone deacetylation; ISS:UniProtKB.
DR GO; GO:0051567; P:histone H3-K9 methylation; ISS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:1903053; P:regulation of extracellular matrix organization; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd19190; PR-SET_PRDM5; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR044415; PRDM5_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 InterPro; IPR017125; Znf_PRDM5-like.
DR Pfam; PF00096; zf-C2H2; 9.
DR PIRSF; PIRSF037162; PRDM; 1.
DR SMART; SM00317; SET; 1.
DR SMART; SM00355; ZnF_C2H2; 15.
DR SUPFAM; SSF57667; SSF57667; 8.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 15.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 15.
PE 2: Evidence at transcript level;
KW Activator; Chromatin regulator; DNA-binding; Metal-binding;
KW Methyltransferase; Nucleus; Reference proteome; Repeat; Repressor;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..599
FT /note="PR domain zinc finger protein 5"
FT /id="PRO_0000230794"
FT DOMAIN 8..124
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT ZN_FING 167..190
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 199..221
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 231..256
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 264..286
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 289..311
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 317..339
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 345..367
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 373..395
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 401..424
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 430..452
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 458..480
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 486..508
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 514..536
FT /note="C2H2-type 13; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 542..564
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 571..594
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CONFLICT 531..532
FT /note="EH -> AT (in Ref. 1; BAB29400)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 599 AA; 69550 MW; 545824C2A54DAAF6 CRC64;
MLGMYVPDRF ALKSSRVQDG MGLYTARRVR KGEKFGPFAG EKRMPEDLDE NMDYRLMWEV
RGSKGEVLYI LDATNPRHSN WLRFVHEAPS QERKNLAAIQ EGENIFYLAV DDIETDTELL
IGYLDSDVEA EEEEQQALTM TKEGKVDHSK GQLAAGSKGH LGCEEDFACP QCESSFPSEE
VLTEHLQSLH QKPTGEKEFK CENCGKKFPV RQALQRHFEQ HRKACRGEAR FVCKADSCGK
RLKSKDALRR HQENVHTGDP KRKLICSVCN RKCTSVSSLQ EHRKIHEIFD CQECMKKFIS
ANQLKRHMIT HSEKRPYNCE ICNKSFKRLD QVGAHKVIHS EDKPYQCKLC GKGFAHRNVY
KNHKKTHSEE RPFQCDACKA LFRTPFSLQR HLLIHNSERT FKCHHCDATF KRKDTLNVHV
QVVHERHKKY RCELCNKAFV TPSVLRSHKK THTGEKEKVC PYCGQKFASS GTLRVHIRSH
TGERPYQCPY CEKGFSKNDG LKMHIRTHTR EKPYQCSECS KAFSQKRGLD EHKRTHTGEK
PFQCDVCDLA FSLKKMLIRH KMTHNPNRPM AECHFCHKKF TRNDYLKVHM DNIHGVADS
