FEZF2_MOUSE
ID FEZF2_MOUSE Reviewed; 455 AA.
AC Q9ESP5; Q9D298;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Fez family zinc finger protein 2;
DE AltName: Full=Forebrain embryonic zinc finger-like protein 2;
DE AltName: Full=Zinc finger protein 312;
DE AltName: Full=Zinc finger protein Fez-like;
GN Name=Fezf2; Synonyms=Fez, Fezl, Zfp312;
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].
RX PubMed=11025224; DOI=10.1016/s0925-4773(00)00418-4;
RA Hashimoto H., Yabe T., Hirata T., Shimizu T., Bae Y.-K., Yamanaka Y.,
RA Hirano T., Hibi M.;
RT "Expression of the zinc finger gene fez-like in zebrafish forebrain.";
RL Mech. Dev. 97:191-195(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=16314561; DOI=10.1073/pnas.0509032102;
RA Chen J.-G., Rasin M.-R., Kwan K.Y., Sestan N.;
RT "Zfp312 is required for subcortical axonal projections and dendritic
RT morphology of deep-layer pyramidal neurons of the cerebral cortex.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:17792-17797(2005).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16157277; DOI=10.1016/j.neuron.2005.08.030;
RA Molyneaux B.J., Arlotta P., Hirata T., Hibi M., Macklis J.D.;
RT "Fezl is required for the birth and specification of corticospinal motor
RT neurons.";
RL Neuron 47:817-831(2005).
RN [6]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=16540508; DOI=10.1242/dev.02329;
RA Hirata T., Nakazawa M., Yoshihara S., Miyachi H., Kitamura K.,
RA Yoshihara Y., Hibi M.;
RT "Zinc-finger gene Fez in the olfactory sensory neurons regulates
RT development of the olfactory bulb non-cell-autonomously.";
RL Development 133:1433-1443(2006).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16971467; DOI=10.1242/dev.02585;
RA Hirata T., Nakazawa M., Muraoka O., Nakayama R., Suda Y., Hibi M.;
RT "Zinc-finger genes Fez and Fez-like function in the establishment of
RT diencephalon subdivisions.";
RL Development 133:3993-4004(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Transcription repressor. Required for the specification of
CC corticospinal motor neurons and other subcerebral projection neurons.
CC May play a role in layer and neuronal subtype-specific patterning of
CC subcortical projections and axonal fasciculation. Controls the
CC development of dendritic arborization and spines of large layer V
CC pyramidal neurons. Plays a role in rostro-caudal patterning of the
CC diencephalon and in prethalamic formation.
CC {ECO:0000269|PubMed:16157277, ECO:0000269|PubMed:16314561,
CC ECO:0000269|PubMed:16540508, ECO:0000269|PubMed:16971467}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16314561}.
CC -!- TISSUE SPECIFICITY: Highly expressed in neocortical layer V, moderately
CC expressed in layer VI. Expressed in subcortically projecting neurons.
CC {ECO:0000269|PubMed:16157277, ECO:0000269|PubMed:16314561}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the olfactory epithelium,
CC hypothalamus, ventrolateral pallium and prethalamus at mid-gestation.
CC At 12.5 dpc, highly enriched in the postmigratory pyramidal neurons
CC forming the cortical plate situated beneath the pial surface. At 13.5
CC dpc, expressed in the ventricular zone and subventricular zone at low
CC levels, expression is much higher in the developing cortical plate,
CC where postmitotic neurons are positioned. During late embryonic and
CC early postnatal development, expression disappears from cortical
CC progenitors and becomes restricted to the subplate and the prospective
CC layer V and VI pyramidal neurons. {ECO:0000269|PubMed:16157277,
CC ECO:0000269|PubMed:16314561, ECO:0000269|PubMed:16540508}.
CC -!- DISRUPTION PHENOTYPE: In null mutant mice, no subcerebral projection
CC neurons are born and no cortical projections to the brainstem or the
CC spinal cord ever develop. In contrast, other populations of neurons are
CC unaffected. There seems to be a redundant role for FEZF1 and FEZF2 in
CC diencephalon development. {ECO:0000269|PubMed:16540508,
CC ECO:0000269|PubMed:16971467}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AB042399; BAB17670.1; -; mRNA.
DR EMBL; AK019996; BAB31958.1; -; mRNA.
DR EMBL; BC055718; AAH55718.1; -; mRNA.
DR CCDS; CCDS26818.1; -.
DR RefSeq; NP_536681.2; NM_080433.3.
DR AlphaFoldDB; Q9ESP5; -.
DR SMR; Q9ESP5; -.
DR STRING; 10090.ENSMUSP00000022262; -.
DR PhosphoSitePlus; Q9ESP5; -.
DR PaxDb; Q9ESP5; -.
DR PRIDE; Q9ESP5; -.
DR ProteomicsDB; 271747; -.
DR Antibodypedia; 15277; 142 antibodies from 24 providers.
DR DNASU; 54713; -.
DR Ensembl; ENSMUST00000022262; ENSMUSP00000022262; ENSMUSG00000021743.
DR Ensembl; ENSMUST00000224714; ENSMUSP00000153090; ENSMUSG00000021743.
DR GeneID; 54713; -.
DR KEGG; mmu:54713; -.
DR UCSC; uc007sfs.2; mouse.
DR CTD; 55079; -.
DR MGI; MGI:1859823; Fezf2.
DR VEuPathDB; HostDB:ENSMUSG00000021743; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000160100; -.
DR HOGENOM; CLU_021813_2_1_1; -.
DR InParanoid; Q9ESP5; -.
DR OMA; GKHKNFT; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9ESP5; -.
DR TreeFam; TF316780; -.
DR BioGRID-ORCS; 54713; 3 hits in 73 CRISPR screens.
DR PRO; PR:Q9ESP5; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9ESP5; protein.
DR Bgee; ENSMUSG00000021743; Expressed in cortical plate and 65 other tissues.
DR ExpressionAtlas; Q9ESP5; baseline and differential.
DR Genevisible; Q9ESP5; MM.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IDA: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:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:MGI.
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; IDA:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0007413; P:axonal fasciculation; IMP:MGI.
DR GO; GO:0043697; P:cell dedifferentiation; IGI:UniProtKB.
DR GO; GO:0021853; P:cerebral cortex GABAergic interneuron migration; IMP:MGI.
DR GO; GO:0021895; P:cerebral cortex neuron differentiation; IMP:MGI.
DR GO; GO:0021902; P:commitment of neuronal cell to specific neuron type in forebrain; IMP:MGI.
DR GO; GO:0016358; P:dendrite development; IMP:MGI.
DR GO; GO:0021542; P:dentate gyrus development; IMP:MGI.
DR GO; GO:0021797; P:forebrain anterior/posterior pattern specification; IGI:MGI.
DR GO; GO:0030900; P:forebrain development; IMP:MGI.
DR GO; GO:0097154; P:GABAergic neuron differentiation; IDA:MGI.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0030182; P:neuron differentiation; IGI:MGI.
DR GO; GO:0048664; P:neuron fate determination; IDA:MGI.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IGI:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:1902667; P:regulation of axon guidance; IMP:MGI.
DR GO; GO:0050767; P:regulation of neurogenesis; IGI:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0021537; P:telencephalon development; IMP:UniProtKB.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 5.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 1: Evidence at protein level;
KW Developmental protein; Differentiation; DNA-binding; Metal-binding;
KW Neurogenesis; Nucleus; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..455
FT /note="Fez family zinc finger protein 2"
FT /id="PRO_0000295121"
FT ZN_FING 272..294
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 300..322
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 328..350
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 356..378
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 384..406
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 412..435
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 27..42
FT /note="Engrailed homology 1 repressor"
FT CONFLICT 429
FT /note="K -> R (in Ref. 2; BAB31958)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 455 AA; 48931 MW; 506C648982A0345B CRC64;
MASSASLETM VPPACPRAGA SPATSKTLAF SIERIMAKTS EPRAPFEPRP AALEADSSQS
KKLLNLCSPL PCMIPLQPLG YEVPSKTLLS YSEFWKSSLR AGGGGGGGSG GGAPVCGASG
LCKTNCGVCC KAELGLAPSA LPAGRVIKPQ VINQAVGLPA SGSLYYFNYL DSTAYPPSEL
LGGHLFPSGL LNAQAPTSLA AHPKLFLLEN AKLASLAADK FPHPASYPHK ERLHAPLEQV
LKENSALTAE RGGVKSHSKL PGGSTDSKPK NFTCEVCGKV FNAHYNLTRH MPVHTGARPF
VCKVCGKGFR QASTLCRHKI IHTQEKPHKC NQCGKAFNRS STLNTHIRIH AGYKPFVCEF
CGKGFHQKGN YKNHKLTHSG EKQYKCTICN KAFHQVYNLT FHMHTHNDKK PFTCATCGKG
FCRNFDLKKH VRKLHDSVGP TATPSAKDLA RTVQS
