FIZ1_MOUSE
ID FIZ1_MOUSE Reviewed; 500 AA.
AC Q9WTJ4; Q91W14; Q9CTG3;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Flt3-interacting zinc finger protein 1;
GN Name=Fiz1;
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], INTERACTION WITH FLT3, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6 X DBA/2; TISSUE=Hematopoietic stem cell;
RX PubMed=10409713; DOI=10.1074/jbc.274.30.21478;
RA Wolf I., Rohrschneider L.R.;
RT "Fiz1, a novel zinc finger protein interacting with the receptor tyrosine
RT kinase Flt3.";
RL J. Biol. Chem. 274:21478-21484(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 239-500.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [4]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12566383; DOI=10.1093/hmg/ddg035;
RA Mitton K.P., Swain P.K., Khanna H., Dowd M., Apel I.J., Swaroop A.;
RT "Interaction of retinal bZIP transcription factor NRL with Flt3-interacting
RT zinc-finger protein Fiz1: possible role of Fiz1 as a transcriptional
RT repressor.";
RL Hum. Mol. Genet. 12:365-373(2003).
CC -!- FUNCTION: May be a transcriptional repressor of NRL function in
CC photoreceptors. Does not repress CRX-mediated transactivation (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with FLT3 cytoplasmic catalytic domain, following
CC receptor stimulation, in a kinase-independent manner. Does not interact
CC with other structurally related receptor tyrosine kinases, including
CC KIT, CSF1R and PDGFR. Interacts with NRL (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409713}. Nucleus
CC {ECO:0000269|PubMed:10409713}.
CC -!- TISSUE SPECIFICITY: Widely expressed. In the retina, highest expression
CC in the ganglion cell layer. {ECO:0000269|PubMed:10409713,
CC ECO:0000269|PubMed:12566383}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the retina at 14.5 dpc.
CC {ECO:0000269|PubMed:12566383}.
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DR EMBL; AF126747; AAD45499.1; -; mRNA.
DR EMBL; AF126746; AAD45498.1; -; mRNA.
DR EMBL; BC006633; AAH06633.1; -; mRNA.
DR EMBL; AK003641; BAB22907.1; -; mRNA.
DR CCDS; CCDS20751.1; -.
DR RefSeq; NP_001103798.1; NM_001110328.1.
DR RefSeq; NP_001103799.1; NM_001110329.1.
DR RefSeq; NP_001103800.1; NM_001110330.1.
DR RefSeq; NP_035943.3; NM_011813.3.
DR RefSeq; XP_006539970.1; XM_006539907.3.
DR AlphaFoldDB; Q9WTJ4; -.
DR BioGRID; 204770; 4.
DR IntAct; Q9WTJ4; 2.
DR MINT; Q9WTJ4; -.
DR STRING; 10090.ENSMUSP00000128105; -.
DR iPTMnet; Q9WTJ4; -.
DR PhosphoSitePlus; Q9WTJ4; -.
DR EPD; Q9WTJ4; -.
DR MaxQB; Q9WTJ4; -.
DR PaxDb; Q9WTJ4; -.
DR PRIDE; Q9WTJ4; -.
DR ProteomicsDB; 271698; -.
DR Antibodypedia; 33128; 152 antibodies from 23 providers.
DR DNASU; 23877; -.
DR Ensembl; ENSMUST00000077385; ENSMUSP00000076603; ENSMUSG00000061374.
DR Ensembl; ENSMUST00000165320; ENSMUSP00000128105; ENSMUSG00000061374.
DR Ensembl; ENSMUST00000167804; ENSMUSP00000126765; ENSMUSG00000061374.
DR Ensembl; ENSMUST00000207030; ENSMUSP00000147082; ENSMUSG00000061374.
DR Ensembl; ENSMUST00000208944; ENSMUSP00000147011; ENSMUSG00000061374.
DR GeneID; 23877; -.
DR KEGG; mmu:23877; -.
DR UCSC; uc009eze.2; mouse.
DR CTD; 84922; -.
DR MGI; MGI:1344336; Fiz1.
DR VEuPathDB; HostDB:ENSMUSG00000061374; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000153306; -.
DR HOGENOM; CLU_047914_0_0_1; -.
DR InParanoid; Q9WTJ4; -.
DR OMA; DCERDFN; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9WTJ4; -.
DR TreeFam; TF337381; -.
DR BioGRID-ORCS; 23877; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Fiz1; mouse.
DR PRO; PR:Q9WTJ4; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9WTJ4; protein.
DR Bgee; ENSMUSG00000061374; Expressed in cerebellum ventricular layer and 271 other tissues.
DR ExpressionAtlas; Q9WTJ4; baseline and differential.
DR Genevisible; Q9WTJ4; MM.
DR GO; GO:0000785; C:chromatin; IDA:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISS:ARUK-UCL.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:ARUK-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IGI:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:ARUK-UCL.
DR GO; GO:0006468; P:protein phosphorylation; IGI:MGI.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00355; ZnF_C2H2; 11.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..500
FT /note="Flt3-interacting zinc finger protein 1"
FT /id="PRO_0000046938"
FT ZN_FING 29..51
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 57..79
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 85..107
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 113..136
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 204..226
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 232..254
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 336..357
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 363..386
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 418..440
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 446..468
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 474..496
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96SL8"
FT CONFLICT 404
FT /note="G -> D (in Ref. 2; AAH06633)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 500 AA; 52685 MW; 9F0F553ABD7F7F45 CRC64;
MEDSSLPVVP APIAAPGPAP SATAPRVPFH CSECGKSFRY RSDLRRHFAR HTALKPHACP
RCGKGFKHSF NLANHLRSHT GERPYRCSAC PKGFRDSTGL LHHQVVHTGE KPYCCLVCEL
RFSSRSSLGR HLKRQHRGTL PSPLQPSPGL PPLSSPCSVC CNVGPCSVCG GGGSSGGEGL
EGAGATSWGL AEAAAAAAAS LPPFACGACA RRFDHGRELA AHWAAHTDVK PFKCPRCERD
FNAPALLERH KLTHDLQGSN APPTQVWASG GGPEVAGEGD ASEVGAAPQT WDAGLLLSPT
GAGVPKLEAL LPGDEGSGND QAPAAAAEAS SEDTLYQCDC GTFFASAPAL ASHLEAHSGP
ATYGCGHCGA LYAALAALEE HRRASHGEGS GEAAPDGEGN QAAGGPGPGS SSRSKKIFGC
SECEKLFRSP RDLERHVLVH TGEKPFPCLE CGKFFRHECY LKRHRLLHGT ERPFPCHICG
KGFITLSNLS RHLKLHRGMD
