ZFP42_MOUSE
ID ZFP42_MOUSE Reviewed; 288 AA.
AC P22227; Q4KMN3; Q7TPU3;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 25-MAY-2022, entry version 169.
DE RecName: Full=Zinc finger protein 42;
DE Short=Zfp-42;
DE AltName: Full=Reduced expression protein 1;
DE Short=REX-1;
DE Short=mREX-1;
GN Name=Zfp42; Synonyms=Rex-1, Rex1;
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 [MRNA], AND INDUCTION.
RC TISSUE=Embryonic stem cell;
RX PubMed=2511439; DOI=10.1128/mcb.9.12.5623-5629.1989;
RA Hosler B.A., Larosa G.J., Grippo J.F., Gudas L.J.;
RT "Expression of REX-1, a gene containing zinc finger motifs, is rapidly
RT reduced by retinoic acid in F9 teratocarcinoma cells.";
RL Mol. Cell. Biol. 9:5623-5629(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8474450; DOI=10.1128/mcb.13.5.2919-2928.1993;
RA Hosler B.A., Rogers M.B., Kozak C.A., Gudas L.J.;
RT "An octamer motif contributes to the expression of the retinoic acid-
RT regulated zinc finger gene Rex-1 (Zfp-42) in F9 teratocarcinoma cells.";
RL Mol. Cell. Biol. 13:2919-2928(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129/Sv X 129SvCp, and C57BL/6J;
RC TISSUE=Blastocyst, and Embryonic stem cell;
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).
RN [4]
RP INDUCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=1821852; DOI=10.1242/dev.113.3.815;
RA Rogers M.B., Hosler B.A., Gudas L.J.;
RT "Specific expression of a retinoic acid-regulated, zinc-finger gene, Rex-1,
RT in preimplantation embryos, trophoblast and spermatocytes.";
RL Development 113:815-824(1991).
RN [5]
RP INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=15749260; DOI=10.1016/j.reprotox.2004.10.008;
RA Zhang H., Guo D., Wang L., Zhao Y., Cheng Y., Qiao Z.;
RT "Effect of nicotine on Oct-4 and Rex-1 expression of mouse embryonic stem
RT cells.";
RL Reprod. Toxicol. 19:473-478(2005).
RN [6]
RP INDUCTION.
RX PubMed=16714766; DOI=10.1074/jbc.m601811200;
RA Shi W., Wang H., Pan G., Geng Y., Guo Y., Pei D.;
RT "Regulation of the pluripotency marker Rex-1 by Nanog and Sox2.";
RL J. Biol. Chem. 281:23319-23325(2006).
RN [7]
RP INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=16908534; DOI=10.1128/mcb.00508-06;
RA Hamazaki T., Kehoe S.M., Nakano T., Terada N.;
RT "The Grb2/Mek pathway represses Nanog in murine embryonic stem cells.";
RL Mol. Cell. Biol. 26:7539-7549(2006).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16960129; DOI=10.1634/stemcells.2006-0017;
RA Zhang J.-Z., Gao W., Yang H.-B., Zhang B., Zhu Z.-Y., Xue Y.-F.;
RT "Screening for genes essential for mouse embryonic stem cell self-renewal
RT using a subtractive RNA interference library.";
RL Stem Cells 24:2661-2668(2006).
RN [9]
RP FUNCTION.
RX PubMed=21085182; DOI=10.1038/nature09496;
RA Navarro P., Oldfield A., Legoupi J., Festuccia N., Dubois A., Attia M.,
RA Schoorlemmer J., Rougeulle C., Chambers I., Avner P.;
RT "Molecular coupling of Tsix regulation and pluripotency.";
RL Nature 468:457-460(2010).
RN [10]
RP UBIQUITINATION AT LYS-213 AND LYS-215 BY RNF12.
RX PubMed=22596162; DOI=10.1038/nature11070;
RA Gontan C., Achame E.M., Demmers J., Barakat T.S., Rentmeester E.,
RA van Ijcken W., Grootegoed J.A., Gribnau J.;
RT "RNF12 initiates X-chromosome inactivation by targeting REX1 for
RT degradation.";
RL Nature 485:386-390(2012).
CC -!- FUNCTION: Involved in the reprogramming of X-chromosome inactivation
CC during the acquisition of pluripotency. Required for efficient
CC elongation of TSIX, a non-coding RNA antisense to XIST. Binds DXPas34
CC enhancer within the TSIX promoter. Involved in ES cell self-renewal.
CC {ECO:0000269|PubMed:16960129, ECO:0000269|PubMed:21085182}.
CC -!- INTERACTION:
CC P22227; Q9WTV7: Rlim; NbExp=8; IntAct=EBI-2313372, EBI-15657872;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16960129}.
CC -!- TISSUE SPECIFICITY: Restricted to testis, to germ cells in the early
CC stages of spermatogenesis. Not expressed in spermatids, nor
CC spermatozoa. Expressed in embryonic stem (ES) cells.
CC {ECO:0000269|PubMed:15749260, ECO:0000269|PubMed:16908534,
CC ECO:0000269|PubMed:16960129, ECO:0000269|PubMed:1821852}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the inner cell mass of 4.5 dpc
CC blastocysts, as well as in the polar trophoblast. At 6 dpc, abundant in
CC the extraembryonic ectoderm and the ectoplacental cone. At this stage,
CC not detected in the embryonic ectoderm. At 7 dpc, restricted to the
CC extraembryonic ectoderm and the ectoplacental cone. Also expressed in
CC the placenta. Expressed in male germ cells undergoing meiosis.
CC {ECO:0000269|PubMed:1821852}.
CC -!- INDUCTION: Up-regulated by NANOG, up-regulation which is increased by
CC SOX2 and POU5F1. Up-regulated by nicotine; up-regulation which is
CC prevented with tubocurarine, a nicotinic acetylcholine receptor
CC antagonist. Down-regulated by sodium vanadate and retinoic acid (RA).
CC In ES cells, down-regulation correlates with differentiation.
CC {ECO:0000269|PubMed:15749260, ECO:0000269|PubMed:16714766,
CC ECO:0000269|PubMed:16908534, ECO:0000269|PubMed:1821852,
CC ECO:0000269|PubMed:2511439}.
CC -!- PTM: Polyubiquitinated by RNF12, leading to proteasomal degradation.
CC {ECO:0000269|PubMed:22596162}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M28382; AAA40053.1; -; mRNA.
DR EMBL; M97812; AAA19700.1; -; Genomic_DNA.
DR EMBL; BC053399; AAH53399.1; -; mRNA.
DR EMBL; BC098467; AAH98467.1; -; mRNA.
DR CCDS; CCDS22267.1; -.
DR PIR; A33828; A33828.
DR RefSeq; NP_033582.2; NM_009556.3.
DR AlphaFoldDB; P22227; -.
DR SMR; P22227; -.
DR BioGRID; 204664; 16.
DR DIP; DIP-54911N; -.
DR IntAct; P22227; 4.
DR MINT; P22227; -.
DR STRING; 10090.ENSMUSP00000080765; -.
DR iPTMnet; P22227; -.
DR PhosphoSitePlus; P22227; -.
DR jPOST; P22227; -.
DR MaxQB; P22227; -.
DR PaxDb; P22227; -.
DR PeptideAtlas; P22227; -.
DR PRIDE; P22227; -.
DR ProteomicsDB; 275357; -.
DR DNASU; 22702; -.
DR GeneID; 22702; -.
DR KEGG; mmu:22702; -.
DR CTD; 132625; -.
DR MGI; MGI:99187; Zfp42.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; P22227; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P22227; -.
DR BioGRID-ORCS; 22702; 3 hits in 71 CRISPR screens.
DR PRO; PR:P22227; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P22227; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0031519; C:PcG protein complex; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:NTNU_SB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IMP:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:NTNU_SB.
DR GO; GO:2000653; P:regulation of genetic imprinting; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007286; P:spermatid development; IMP:MGI.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..288
FT /note="Zinc finger protein 42"
FT /id="PRO_0000047300"
FT ZN_FING 170..194
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 227..251
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 258..281
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 213
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:22596162"
FT CROSSLNK 215
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:22596162"
FT CONFLICT 13
FT /note="T -> A (in Ref. 3; AAH53399)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="T -> R (in Ref. 3; AAH53399)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="A -> T (in Ref. 3; AAH53399)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="G -> D (in Ref. 3; AAH53399)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 288 AA; 32398 MW; 4B1ABFDF372A7D7B CRC64;
MNEQKMNEQM KKTAKTSGQK GPGGRALDRL TLKQDEARPV QNTRVEAPRV TYTIRDESEI
SPETEEDGFP DGYLECIIRG EFSEPILEED FLFKSFESLE EVEQNLSRQV LEASSLLESS
LEYMTKGTKQ EKTEVTQETP PLRVGASSLL AGGPAEKPEG GVYCGVLSML ECPQAGCKKK
LRGKTALRKH MLVHGPRRHV CAECGKAFTE SSKLKRHFLV HTGEKPYQCT FEGCGKRFSL
DFNLRTHIRI HTGERRFVCP FDGCEKSFIQ SNNQKIHILT HAKAGKKC
