ZFAT_MOUSE
ID ZFAT_MOUSE Reviewed; 1237 AA.
AC Q7TS63; B2C322;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Zinc finger protein ZFAT;
DE AltName: Full=Zinc finger protein 406;
GN Name=Zfat; Synonyms=Gm922, Zfat1, Zfp406, Znf406;
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] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J;
RX PubMed=18329245; DOI=10.1016/j.ygeno.2008.01.009;
RA Koyanagi M., Nakabayashi K., Fujimoto T., Gu N., Baba I., Takashima Y.,
RA Doi K., Harada H., Kato N., Sasazuki T., Shirasawa S.;
RT "ZFAT expression in B and T lymphocytes and identification of ZFAT-
RT regulated genes.";
RL Genomics 91:451-457(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Olfactory epithelium;
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 [3]
RP STRUCTURE BY NMR OF 345-374 AND 451-478.
RG RIKEN structural genomics initiative (RSGI);
RL Submitted (MAR-2007) to the PDB data bank.
CC -!- FUNCTION: May be involved in transcriptional regulation. Overexpression
CC causes down-regulation of a number of genes involved in the immune
CC response. Some genes are also up-regulated.
CC {ECO:0000269|PubMed:18329245}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18329245}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:18329245}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7TS63-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TS63-2; Sequence=VSP_034940, VSP_034941;
CC -!- TISSUE SPECIFICITY: Detected in spleen and thymus but not in liver,
CC muscle, heart, kidney, brain, bone marrow or pancreas. Expressed in
CC CD19+, CD4+ and CD8+ lymphocytes but not in CD11b+ lymphocytes or
CC peritoneal macrophages (at protein level).
CC {ECO:0000269|PubMed:18329245}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during the transition from
CC CD4-/CD8- to CD4+/CD8+ thymocytes. {ECO:0000269|PubMed:18329245}.
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DR EMBL; EU221277; ABY67968.1; -; mRNA.
DR EMBL; BC053930; AAH53930.1; -; mRNA.
DR CCDS; CCDS49623.1; -. [Q7TS63-1]
DR CCDS; CCDS49624.1; -. [Q7TS63-2]
DR RefSeq; NP_001139360.1; NM_001145888.1. [Q7TS63-1]
DR RefSeq; NP_941046.1; NM_198644.2. [Q7TS63-2]
DR PDB; 2ELW; NMR; -; A=352-381.
DR PDB; 2ELX; NMR; -; A=458-485.
DR PDB; 2RV4; NMR; -; A=352-381.
DR PDB; 2RV5; NMR; -; A=458-485.
DR PDBsum; 2ELW; -.
DR PDBsum; 2ELX; -.
DR PDBsum; 2RV4; -.
DR PDBsum; 2RV5; -.
DR AlphaFoldDB; Q7TS63; -.
DR BMRB; Q7TS63; -.
DR SMR; Q7TS63; -.
DR BioGRID; 237734; 15.
DR STRING; 10090.ENSMUSP00000125257; -.
DR iPTMnet; Q7TS63; -.
DR PhosphoSitePlus; Q7TS63; -.
DR PaxDb; Q7TS63; -.
DR PRIDE; Q7TS63; -.
DR ProteomicsDB; 298519; -. [Q7TS63-1]
DR ProteomicsDB; 299544; -. [Q7TS63-2]
DR Antibodypedia; 27498; 41 antibodies from 16 providers.
DR DNASU; 380993; -.
DR Ensembl; ENSMUST00000160248; ENSMUSP00000125257; ENSMUSG00000022335. [Q7TS63-1]
DR Ensembl; ENSMUST00000162054; ENSMUSP00000125732; ENSMUSG00000022335. [Q7TS63-2]
DR GeneID; 380993; -.
DR KEGG; mmu:380993; -.
DR UCSC; uc007wbd.2; mouse. [Q7TS63-2]
DR UCSC; uc011zto.1; mouse. [Q7TS63-1]
DR CTD; 57623; -.
DR MGI; MGI:2681865; Zfat.
DR VEuPathDB; HostDB:ENSMUSG00000022335; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000156658; -.
DR HOGENOM; CLU_008355_0_0_1; -.
DR InParanoid; Q7TS63; -.
DR OMA; HSIFMCK; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q7TS63; -.
DR TreeFam; TF350017; -.
DR BioGRID-ORCS; 380993; 10 hits in 72 CRISPR screens.
DR ChiTaRS; Zfat; mouse.
DR EvolutionaryTrace; Q7TS63; -.
DR PRO; PR:Q7TS63; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q7TS63; protein.
DR Bgee; ENSMUSG00000022335; Expressed in cleaving embryo and 128 other tissues.
DR ExpressionAtlas; Q7TS63; baseline and differential.
DR Genevisible; Q7TS63; MM.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IC:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:MGI.
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; IBA:GO_Central.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI.
DR GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0060712; P:spongiotrophoblast layer development; IMP:MGI.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00355; ZnF_C2H2; 19.
DR SUPFAM; SSF57667; SSF57667; 8.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; DNA-binding; Metal-binding;
KW Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1237
FT /note="Zinc finger protein ZFAT"
FT /id="PRO_0000047567"
FT ZN_FING 12..35
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 116..141
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 271..293
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 299..321
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 326..349
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 354..377
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 404..426
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 432..454
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 458..481
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 737..759
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 765..788
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 793..817
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 825..848
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 875..898
FT /note="C2H2-type 14; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 904..926
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 932..954
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 961..983
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 989..1012
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1036..1059
FT /note="C2H2-type 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 50..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 144..150
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034940"
FT VAR_SEQ 1063..1073
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034941"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:2ELW"
FT STRAND 362..365
FT /evidence="ECO:0007829|PDB:2RV4"
FT HELIX 366..376
FT /evidence="ECO:0007829|PDB:2ELW"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:2ELX"
FT STRAND 466..469
FT /evidence="ECO:0007829|PDB:2ELX"
FT HELIX 470..479
FT /evidence="ECO:0007829|PDB:2ELX"
SQ SEQUENCE 1237 AA; 137883 MW; 085176A902B319E9 CRC64;
METRTAENTA IFMCKCCNLF SPNQSELVTH VSEKHGEEGV NVDDVIIPLR PLNTPENPNP
SKGGDEFLVM KRKRGRPKGS TKKPSTEEEV VENLVSPSED GPLATEEGSR LAPSSLECSK
CCRKFSNTRQ LRKHICIIVL NLGEEDGDAG NESDLDLEKT YKEDDREKAS KRPRAQKTEK
VQKISGKEAG QLSGAKKPII SVVLTAHEAI PGATKIIPVE AGPPETGAPP PETTAADLVP
RRGYQEYAIQ QTPYEQPMKS SRLGPTQLKI FTCEYCNKVF KFKHSLQAHL RIHTNEKPYK
CSQCSYASAI KANLNVHLRK HTGEKFACDY CSFTCLSKGH LKVHIERVHK KIKQHCRFCK
KKYSDVKNLI KHIRDMHDPQ DKKVKEALDE LRLMTREGKR QLLYDCHICE RKFKNELDRD
RHMLVHGDKW PFACELCGHG ATKYQALELH VRKHPFVYVC ALCLKKFVSS IRLRSHIREV
HGAAQETLVF TSSINQSFCL LEPGGDIQQE ALGDQLQLAA EEFVCPEIDV RKEEACPGEA
QPEVGLRELV VPGDAHAPPP GPLATPQSES SSLSPCKLET TVVSSDLNSL GVVSDDFLLK
SDTSSAEPPA AAEATSDTQH RDSAQTQGEE VTLLLAKAKS AGPDPESSPG GRQKVGALPA
SESDSSTCLR ANPTEASDLL PTVTDGGDLG VCQPDSCTPS SEHHPGSTAF MKVLDSLQKK
QMNTSLCERI RKVYGDLECE YCGKLFWYQV HFDMHVRTHT REHLYYCSQC HYSSITKNCL
KRHVIQKHSN ILLKCPTDGC DYSTPDKYKL QAHLKVHTEL DKRSYSCPVC EKSFSEDRLI
KSHIKTNHPE VSMNTISEVL GRRVQLKGLI GKRAMKCPYC DFYFMKNGSD LQRHIWAHEG
VKPFKCSLCE YATRSKSNLK AHMNRHSTEK THLCDMCGKK FKSKGTLKSH KLLHTSDGKQ
FKCTVCDYTA AQKPQLLRHM EQHASFKPFR CAHCHYSCNI SGSLKRHYNR KHPNEEYTNV
GSGELAAEAL IQQGGLKCPV CSFVYGTKWE FNRHLKNKHG LKVVEIDGDP KWEPAAETPE
EPSTQYLYIT EAEDVQGTQA AVAALQDLRY TSESGDRLDP TAVNILQQII ELGSETHDAA
AVASVVAMAP GTVTVVKQVT DEEPSSNHTV MIQETLQQAS VELAEQHHLV VSSDDVEGIE
TVTVYTQGGE ASEFIVYVQE AVQPVEEQVG EQPAPEL