PRD14_MOUSE
ID PRD14_MOUSE Reviewed; 561 AA.
AC E9Q3T6; Q3URU1;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=PR domain zinc finger protein 14;
DE EC=2.1.1.-;
DE AltName: Full=PR domain-containing protein 14;
GN Name=Prdm14;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 50-561.
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 [3]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18622394; DOI=10.1038/ng.186;
RA Yamaji M., Seki Y., Kurimoto K., Yabuta Y., Yuasa M., Shigeta M.,
RA Yamanaka K., Ohinata Y., Saitou M.;
RT "Critical function of Prdm14 for the establishment of the germ cell lineage
RT in mice.";
RL Nat. Genet. 40:1016-1022(2008).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=20953172; DOI=10.1038/nature09531;
RA Chia N.Y., Chan Y.S., Feng B., Lu X., Orlov Y.L., Moreau D., Kumar P.,
RA Yang L., Jiang J., Lau M.S., Huss M., Soh B.S., Kraus P., Li P., Lufkin T.,
RA Lim B., Clarke N.D., Bard F., Ng H.H.;
RT "A genome-wide RNAi screen reveals determinants of human embryonic stem
RT cell identity.";
RL Nature 468:316-320(2010).
RN [5]
RP INTERACTION WITH CBFA2T2.
RX PubMed=27281218; DOI=10.1038/nature18004;
RA Tu S., Narendra V., Yamaji M., Vidal S.E., Rojas L.A., Wang X., Kim S.Y.,
RA Garcia B.A., Tuschl T., Stadtfeld M., Reinberg D.;
RT "Co-repressor CBFA2T2 regulates pluripotency and germline development.";
RL Nature 534:387-390(2016).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 184-373 IN COMPLEX WITH CBFA2T2,
RP FUNCTION, AND MUTAGENESIS OF TYR-339.
RX PubMed=26523391; DOI=10.7554/elife.10150;
RA Nady N., Gupta A., Ma Z., Swigut T., Koide A., Koide S., Wysocka J.;
RT "ETO family protein Mtgr1 mediates Prdm14 functions in stem cell
RT maintenance and primordial germ cell formation.";
RL Elife 4:E10150-E10150(2015).
CC -!- FUNCTION: Transcription factor that has both positive and negative
CC roles on transcription (By similarity). Plays a role in cellular
CC pluripotency. Essential for germ cell development at 2 levels: the
CC reacquisition of potential pluripotency, including SOX2 up-regulation,
CC and successful epigenetic reprogramming, characterized by EHMT1
CC repression. Its association with CBFA2T2 is required for the functions
CC in pluripotency and germ cell formation. {ECO:0000250,
CC ECO:0000269|PubMed:18622394, ECO:0000269|PubMed:26523391}.
CC -!- SUBUNIT: Interacts with CBFA2T2. {ECO:0000269|PubMed:26523391,
CC ECO:0000269|PubMed:27281218}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Restricted to embryonic stem cells and primordial
CC germ cells. Not detected in epiblast-derived stem cells.
CC {ECO:0000269|PubMed:18622394, ECO:0000269|PubMed:20953172}.
CC -!- DEVELOPMENTAL STAGE: At 3.5 dpc, weak and transient expression in the
CC inner cell mass cells of blastocysts. This expression disappears by 5.5
CC dpc. Expression starts again in committed PGCs around 6.5 dpc in the
CC extraembryonic mesoderm contiguous from the most proximal epiblast (at
CC protein level). Expression persists specifically in PGCs until about
CC 13.5-14.5 dpc both in females and males. {ECO:0000269|PubMed:18622394}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice are born with an expected Mendelian
CC ratio and looked grossly normal. However, both females and males are
CC sterile, ovaries and testes being completely devoid of germ cells.
CC {ECO:0000269|PubMed:18622394}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; AC091248; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK141218; BAE24596.1; -; mRNA.
DR CCDS; CCDS48221.1; -.
DR RefSeq; NP_001074678.2; NM_001081209.2.
DR PDB; 5ECJ; X-ray; 3.05 A; A/B=184-373.
DR PDBsum; 5ECJ; -.
DR AlphaFoldDB; E9Q3T6; -.
DR SMR; E9Q3T6; -.
DR BioGRID; 238771; 1.
DR DIP; DIP-62031N; -.
DR IntAct; E9Q3T6; 1.
DR STRING; 10090.ENSMUSP00000044245; -.
DR PhosphoSitePlus; E9Q3T6; -.
DR PaxDb; E9Q3T6; -.
DR PRIDE; E9Q3T6; -.
DR Antibodypedia; 12206; 425 antibodies from 34 providers.
DR Ensembl; ENSMUST00000047577; ENSMUSP00000044245; ENSMUSG00000042414.
DR GeneID; 383491; -.
DR KEGG; mmu:383491; -.
DR UCSC; uc007aik.1; mouse.
DR CTD; 63978; -.
DR MGI; MGI:3588194; Prdm14.
DR VEuPathDB; HostDB:ENSMUSG00000042414; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000159454; -.
DR HOGENOM; CLU_034551_1_0_1; -.
DR InParanoid; E9Q3T6; -.
DR OMA; WYPIPHL; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; E9Q3T6; -.
DR TreeFam; TF106412; -.
DR BioGRID-ORCS; 383491; 0 hits in 73 CRISPR screens.
DR PRO; PR:E9Q3T6; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; E9Q3T6; protein.
DR Bgee; ENSMUSG00000042414; Expressed in cleaving embryo and 11 other tissues.
DR Genevisible; E9Q3T6; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:MGI.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IC:NTNU_SB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IDA:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IMP:NTNU_SB.
DR GO; GO:0001708; P:cell fate specification; IMP:MGI.
DR GO; GO:0000902; P:cell morphogenesis; IMP:MGI.
DR GO; GO:0007566; P:embryo implantation; IMP:MGI.
DR GO; GO:0009566; P:fertilization; IMP:MGI.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0007281; P:germ cell development; IMP:UniProtKB.
DR GO; GO:0030718; P:germ-line stem cell population maintenance; IMP:MGI.
DR GO; GO:0034972; P:histone H3-R26 methylation; IDA:MGI.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IMP:MGI.
DR GO; GO:0060817; P:inactivation of paternal X chromosome; IMP:MGI.
DR GO; GO:0001827; P:inner cell mass cell fate commitment; IDA:MGI.
DR GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:1902093; P:positive regulation of flagellated sperm motility; IMP:UniProtKB.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IMP:UniProtKB.
DR GO; GO:0044030; P:regulation of DNA methylation; IMP:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IGI:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0019827; P:stem cell population maintenance; IMP:MGI.
DR CDD; cd19198; PR-SET_PRDM14; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR044408; PRDM14_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; PF00856; SET; 1.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00317; SET; 1.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF57667; SSF57667; 3.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Metal-binding; Methyltransferase; Nucleus;
KW Reference proteome; Repeat; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..561
FT /note="PR domain zinc finger protein 14"
FT /id="PRO_0000417666"
FT DOMAIN 241..356
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT ZN_FING 390..416
FT /note="C2H2-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 422..445
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 451..473
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 479..501
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 507..530
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 536..558
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..373
FT /note="Interaction with CBFA2T2"
FT /evidence="ECO:0000269|PubMed:26523391,
FT ECO:0000269|PubMed:27281218"
FT BINDING 355
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT MUTAGEN 339
FT /note="Y->R: Impairs interaction with CBFA2T2."
FT /evidence="ECO:0000269|PubMed:26523391"
FT CONFLICT 50
FT /note="Q -> E (in Ref. 1; BAE24596)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="Q -> L (in Ref. 1; BAE24596)"
FT /evidence="ECO:0000305"
FT HELIX 189..197
FT /evidence="ECO:0007829|PDB:5ECJ"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:5ECJ"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:5ECJ"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:5ECJ"
FT STRAND 243..250
FT /evidence="ECO:0007829|PDB:5ECJ"
FT STRAND 253..262
FT /evidence="ECO:0007829|PDB:5ECJ"
FT STRAND 276..279
FT /evidence="ECO:0007829|PDB:5ECJ"
FT STRAND 292..297
FT /evidence="ECO:0007829|PDB:5ECJ"
FT STRAND 300..306
FT /evidence="ECO:0007829|PDB:5ECJ"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:5ECJ"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:5ECJ"
FT STRAND 328..333
FT /evidence="ECO:0007829|PDB:5ECJ"
FT STRAND 336..343
FT /evidence="ECO:0007829|PDB:5ECJ"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:5ECJ"
FT STRAND 359..362
FT /evidence="ECO:0007829|PDB:5ECJ"
FT STRAND 365..368
FT /evidence="ECO:0007829|PDB:5ECJ"
SQ SEQUENCE 561 AA; 63374 MW; 03D83B5365C9FBAB CRC64;
MALPPSGETQ SQDKANYLPQ SNPHHLTTYY AHAPGYSHFR NLATTEEEFQ PWKLAAAVLE
SQAMAPLDAF RMTAPLLNPG LAVQSEPLYN LPWYKLSPWN RIPQFTPEVP RFLDSTEHRS
SGSSNQNLVL GGGGGQISGQ RWEAENLLLP SPVIASLLPD GIKSSQSISV PQTLNQEGKL
PFCGFNFTEE ELSFVLYGAI ASPEHPTDLQ HAISGILVPT ESSGSNHLHK TLDKDSLQLP
EGLCLMQTSF GDVPHFGVFC SDFIAKGVRF GPFRGRVVNA SEVKAHRDNS RMWEIFEDGH
LSHFIDGKGS GNWMSYVNCA RFPKEQNLLA VQHQGQIFYE SCRDIQRNQE LLVWYGNGYE
KFLGVPMNLR VTEQGGQQLS ESSEESAEGY RCERCGKVFT YKYYRDKHLK YTPCVDKGDR
KFPCSLCQRS FEKRDRLRIH ILHVHERHRP YLCSTCGKSF SQSSSLNKHM RVHSGDRPYQ
CVYCTKKFTA SSILRTHIRQ HSGEKPFKCK HCGKAFASHA AHDSHVRRSH KDNGRSSCDI
CGKGFLDQEA FYAHMRLHKT C
