ID PAX6_MOUSE Reviewed; 422 AA. AC P63015; P32117; P70601; Q3UTV5; Q62222; Q64037; Q8CEI5; Q8VDB5; Q921Q8; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 31-AUG-2004, sequence version 1. DT 27-MAR-2024, entry version 186. DE RecName: Full=Paired box protein Pax-6; DE AltName: Full=Oculorhombin; GN Name=Pax6; Synonyms=Pax-6, Sey; 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] (ISOFORMS 1 AND 5A), AND PARTIAL PROTEIN RP SEQUENCE. RX PubMed=1687460; DOI=10.1242/dev.113.4.1435; RA Walther C., Gruss P.; RT "Pax-6, a murine paired box gene, is expressed in the developing CNS."; RL Development 113:1435-1449(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 5A), AND VARIANT PRO-259. RC STRAIN=C3H/HeJ; TISSUE=Head; RX PubMed=11779807; DOI=10.1093/genetics/159.4.1689; RA Favor J., Peters H., Hermann T., Schmahl W., Chatterjee B., RA Neuhauser-Klaus A., Sandulache R.; RT "Molecular characterization of Pax6(2Neu) through Pax6(10Neu): an extension RT of the Pax6 allelic series and the identification of two possible hypomorph RT alleles in the mouse Mus musculus."; RL Genetics 159:1689-1700(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC STRAIN=C57BL/6J; TISSUE=Cerebellum; 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5A). RC STRAIN=Czech II; TISSUE=Eye, and 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-131 (ISOFORM 1). RX PubMed=1685142; DOI=10.1016/0888-7543(91)90151-4; RA Walther C., Guenet J.-L., Simon D., Deutsch U., Jostes B., Goulding M.D., RA Plachov D., Balling R., Gruss P.; RT "Pax: a murine multigene family of paired box-containing genes."; RL Genomics 11:424-434(1991). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 45-422 (ISOFORM 1). RC TISSUE=Embryo; RX PubMed=1612585; DOI=10.1016/0888-7543(92)90239-o; RA Ton C.C.T., Miwa H., Saunders G.F.; RT "Small eye (Sey): cloning and characterization of the murine homolog of the RT human aniridia gene."; RL Genomics 13:251-256(1992). RN [7] RP INVOLVEMENT IN SEY. RX PubMed=1684639; DOI=10.1038/354522a0; RA Hill R.E., Favor J., Hogan B.L.M., Ton C.C.T., Saunders G.F., Hanson I.M., RA Prosser J., Jordan T., Hastie N.D., van Heyningen V.; RT "Mouse small eye results from mutations in a paired-like homeobox- RT containing gene."; RL Nature 354:522-525(1991). RN [8] RP FUNCTION IN PANCREAS. RX PubMed=9163426; DOI=10.1038/387406a0; RA St Onge L., Sosa-Pineda B., Chowdhury K., Mansouri A., Gruss P.; RT "Pax6 is required for differentiation of glucagon-producing alpha-cells in RT mouse pancreas."; RL Nature 387:406-409(1997). RN [9] RP INTERACTION WITH MAF AND MAFB. RX PubMed=17901057; DOI=10.1074/jbc.m702795200; RA Gosmain Y., Avril I., Mamin A., Philippe J.; RT "Pax-6 and c-Maf functionally interact with the alpha-cell-specific DNA RT element G1 in vivo to promote glucagon gene expression."; RL J. Biol. Chem. 282:35024-35034(2007). RN [10] RP INTERACTION WITH TRIM11, UBIQUITINATION, AND DEVELOPMENTAL STAGE. RX PubMed=18628401; DOI=10.1101/gad.471708; RA Tuoc T.C., Stoykova A.; RT "Trim11 modulates the function of neurogenic transcription factor Pax6 RT through ubiquitin-proteosome system."; RL Genes Dev. 22:1972-1986(2008). RN [11] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND RP SUMOYLATION. RX PubMed=21084637; DOI=10.1073/pnas.1007866107; RA Yan Q., Gong L., Deng M., Zhang L., Sun S., Liu J., Ma H., Yuan D., RA Chen P.C., Hu X., Liu J., Qin J., Xiao L., Huang X.Q., Zhang J., Li D.W.; RT "Sumoylation activates the transcriptional activity of Pax-6, an important RT transcription factor for eye and brain development."; RL Proc. Natl. Acad. Sci. U.S.A. 107:21034-21039(2010). RN [12] RP FUNCTION, INTERACTION WITH TLE6, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RP AND INDUCTION BY TNFSF11-INDUCED OSTEOCLASTOGENESIS. RX PubMed=23990468; DOI=10.1074/jbc.m113.461848; RA Kogawa M., Hisatake K., Atkins G.J., Findlay D.M., Enoki Y., Sato T., RA Gray P.C., Kanesaki-Yatsuka Y., Anderson P.H., Wada S., Kato N., Fukuda A., RA Katayama S., Tsujimoto M., Yoda T., Suda T., Okazaki Y., Matsumoto M.; RT "The paired-box homeodomain transcription factor Pax6 binds to the upstream RT region of the TRAP gene promoter and suppresses receptor activator of NF- RT kappaB ligand (RANKL)-induced osteoclast differentiation."; RL J. Biol. Chem. 288:31299-31312(2013). CC -!- FUNCTION: Transcription factor with important functions in the CC development of the eye, nose, central nervous system and pancreas. CC Required for the differentiation of pancreatic islet alpha cells CC (PubMed:9163426). Competes with PAX4 in binding to a common element in CC the glucagon, insulin and somatostatin promoters. Regulates CC specification of the ventral neuron subtypes by establishing the CC correct progenitor domains (By similarity). Acts as a transcriptional CC repressor of NFATC1-mediated gene expression (PubMed:23990468). CC {ECO:0000250, ECO:0000269|PubMed:23990468, ECO:0000269|PubMed:9163426}. CC -!- SUBUNIT: Interacts with MAF and MAFB (PubMed:17901057). Interacts with CC TRIM11; this interaction leads to ubiquitination and proteasomal CC degradation, as well as inhibition of transactivation, possibly in part CC by preventing PAX6 binding to consensus DNA sequences CC (PubMed:18628401). Interacts with TLE6/GRG6 (PubMed:23990468). CC {ECO:0000269|PubMed:17901057, ECO:0000269|PubMed:18628401, CC ECO:0000269|PubMed:23990468}. CC -!- INTERACTION: CC P63015; O35845: Smarca4; NbExp=2; IntAct=EBI-1395428, EBI-371515; CC P63015; P63166: Sumo1; NbExp=2; IntAct=EBI-1395428, EBI-80152; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23990468}. CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus CC {ECO:0000250|UniProtKB:P63016}. CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus CC {ECO:0000269|PubMed:21084637}. Cytoplasm {ECO:0000269|PubMed:21084637}. CC -!- SUBCELLULAR LOCATION: [Isoform 5a]: Nucleus CC {ECO:0000250|UniProtKB:P63016}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P63015-1; Sequence=Displayed; CC Name=5a; Synonyms=Pax6-5a; CC IsoId=P63015-2; Sequence=VSP_011530; CC Name=3; Synonyms=p32; CC IsoId=P63015-3; Sequence=VSP_054294; CC -!- TISSUE SPECIFICITY: Expressed in osteoclasts. CC {ECO:0000269|PubMed:23990468}. CC -!- TISSUE SPECIFICITY: [Isoform 1]: Dominant isoform expressed in the eye, CC including in the retina and cornea (PubMed:21084637). Abundantly CC expressed in the lens epithelium (PubMed:21084637). CC {ECO:0000269|PubMed:21084637}. CC -!- TISSUE SPECIFICITY: [Isoform 3]: Dominant isoform expressed in the eye, CC including in the retina and cornea (PubMed:21084637). Weakly expressed CC in the lens epithelium (PubMed:21084637). CC {ECO:0000269|PubMed:21084637}. CC -!- DEVELOPMENTAL STAGE: Expressed in the developing eye, nose, brain and CC pancreas (PubMed:21084637). At 9 dpc, expressed in the telencephalon, CC diencephalon, neural tube, optic vesicle and pancreas. Throughout CC development, expression continues in the dorsal and ventral pancreas. CC Expressed during cortical neurogenesis from 11 to 18 dpc. High levels CC in the early radial glial progenitors from 11 to 14 dpc and gradually CC decrease thereafter (at protein level). During corticogenesis, the CC protein level declines faster than that of the mRNA, due to proteasomal CC degradation (PubMed:18628401). {ECO:0000269|PubMed:18628401, CC ECO:0000269|PubMed:21084637}. CC -!- DEVELOPMENTAL STAGE: [Isoform 1]: Abundantly expressed in the newborn CC eye. {ECO:0000269|PubMed:21084637}. CC -!- DEVELOPMENTAL STAGE: [Isoform 3]: Expressed in the developing eye at CC 9.5 dpc, the expression becomes much stronger and additionally CC expressed in the neural tube and optic and lens vesicles at 11.5 dpc. CC Expression is then reduced by 12.5 dpc and becomes significantly CC decreased from 14.5 dpc to 18.5 dpc of embryonic development. CC {ECO:0000269|PubMed:21084637}. CC -!- DEVELOPMENTAL STAGE: [Isoform 5a]: Significantly expressed in the CC newborn eye. {ECO:0000269|PubMed:21084637}. CC -!- INDUCTION: Induced by TNFSF11/RANKL-induced osteoclastogenesis. CC {ECO:0000269|PubMed:23990468}. CC -!- PTM: Ubiquitinated by TRIM11, leading to ubiquitination and proteasomal CC degradation. {ECO:0000269|PubMed:18628401}. CC -!- PTM: [Isoform 3]: Sumoylated by SUMO1 at 'Lys-91'. CC {ECO:0000269|PubMed:21084637}. CC -!- DISEASE: Note=Defects in Pax6 are the cause of a condition known as CC small eye (Sey) which results in the complete lack of eyes and nasal CC primordia. {ECO:0000269|PubMed:1684639}. CC -!- SIMILARITY: Belongs to the paired homeobox family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA40109.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; X63963; CAA45379.1; -; mRNA. DR EMBL; X63963; CAA45380.1; -; mRNA. DR EMBL; Y19196; CAC80516.1; -; Genomic_DNA. DR EMBL; Y19199; CAC80519.1; -; Genomic_DNA. DR EMBL; AK028059; BAC25729.1; -; mRNA. DR EMBL; AK139054; BAE23875.1; -; mRNA. DR EMBL; BC011272; AAH11272.1; -; mRNA. DR EMBL; BC036957; AAH36957.1; -; mRNA. DR EMBL; M77842; AAA40109.1; ALT_INIT; mRNA. DR CCDS; CCDS16499.1; -. [P63015-2] DR CCDS; CCDS57181.1; -. [P63015-1] DR PIR; S42234; S42234. DR RefSeq; NP_001231127.1; NM_001244198.2. [P63015-2] DR RefSeq; NP_001231129.1; NM_001244200.2. [P63015-2] DR RefSeq; NP_001231130.1; NM_001244201.2. [P63015-1] DR RefSeq; NP_001231131.1; NM_001244202.2. [P63015-1] DR RefSeq; NP_001297073.1; NM_001310144.1. [P63015-1] DR RefSeq; NP_001297074.1; NM_001310145.1. [P63015-3] DR RefSeq; NP_001297075.1; NM_001310146.1. [P63015-3] DR RefSeq; NP_038655.1; NM_013627.6. [P63015-2] DR AlphaFoldDB; P63015; -. DR SMR; P63015; -. DR BioGRID; 202033; 21. DR DIP; DIP-38879N; -. DR IntAct; P63015; 9. DR MINT; P63015; -. DR STRING; 10090.ENSMUSP00000087870; -. DR GlyGen; P63015; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P63015; -. DR PhosphoSitePlus; P63015; -. DR MaxQB; P63015; -. DR PaxDb; 10090-ENSMUSP00000087870; -. DR ProteomicsDB; 294331; -. [P63015-1] DR ProteomicsDB; 294332; -. [P63015-2] DR ProteomicsDB; 294333; -. [P63015-3] DR Pumba; P63015; -. DR Antibodypedia; 12821; 1083 antibodies from 49 providers. DR DNASU; 18508; -. DR Ensembl; ENSMUST00000090391.13; ENSMUSP00000087870.6; ENSMUSG00000027168.22. [P63015-2] DR Ensembl; ENSMUST00000090397.13; ENSMUSP00000087878.7; ENSMUSG00000027168.22. [P63015-1] DR Ensembl; ENSMUST00000111082.8; ENSMUSP00000106711.2; ENSMUSG00000027168.22. [P63015-1] DR Ensembl; ENSMUST00000111083.10; ENSMUSP00000106712.3; ENSMUSG00000027168.22. [P63015-1] DR Ensembl; ENSMUST00000111085.8; ENSMUSP00000106714.2; ENSMUSG00000027168.22. [P63015-2] DR Ensembl; ENSMUST00000111086.11; ENSMUSP00000106715.3; ENSMUSG00000027168.22. [P63015-2] DR Ensembl; ENSMUST00000111087.10; ENSMUSP00000106716.3; ENSMUSG00000027168.22. [P63015-1] DR Ensembl; ENSMUST00000167211.9; ENSMUSP00000129344.3; ENSMUSG00000027168.22. [P63015-2] DR GeneID; 18508; -. DR KEGG; mmu:18508; -. DR UCSC; uc008lku.2; mouse. [P63015-2] DR UCSC; uc008lkv.2; mouse. [P63015-1] DR AGR; MGI:97490; -. DR CTD; 5080; -. DR MGI; MGI:97490; Pax6. DR VEuPathDB; HostDB:ENSMUSG00000027168; -. DR eggNOG; KOG0849; Eukaryota. DR GeneTree; ENSGT00940000155391; -. DR HOGENOM; CLU_019281_1_0_1; -. DR InParanoid; P63015; -. DR OMA; PYWPRIQ; -. DR OrthoDB; 5398393at2759; -. DR TreeFam; TF320146; -. DR BioGRID-ORCS; 18508; 2 hits in 77 CRISPR screens. DR ChiTaRS; Pax6; mouse. DR PRO; PR:P63015; -. DR Proteomes; UP000000589; Chromosome 2. DR RNAct; P63015; Protein. DR Bgee; ENSMUSG00000027168; Expressed in retinal neural layer and 175 other cell types or tissues. DR ExpressionAtlas; P63015; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005667; C:transcription regulator complex; TAS:MGI. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0031490; F:chromatin DNA binding; IDA:MGI. DR GO; GO:0070410; F:co-SMAD binding; IDA:BHF-UCL. DR GO; GO:0003677; F:DNA binding; IDA:MGI. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:BHF-UCL. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:MGI. DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI. DR GO; GO:0035035; F:histone acetyltransferase binding; IDA:BHF-UCL. DR GO; GO:0071837; F:HMG box domain binding; IPI:UniProtKB. DR GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; ISO:MGI. DR GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL. DR GO; GO:0070412; F:R-SMAD binding; IDA:BHF-UCL. DR GO; GO:0003723; F:RNA binding; IDA:MGI. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB. DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:BHF-UCL. 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:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB. DR GO; GO:0001221; F:transcription coregulator binding; IPI:BHF-UCL. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB. DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central. DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI. DR GO; GO:0048708; P:astrocyte differentiation; IMP:MGI. DR GO; GO:0007411; P:axon guidance; IMP:MGI. DR GO; GO:0007409; P:axonogenesis; IMP:MGI. DR GO; GO:0001568; P:blood vessel development; ISO:MGI. DR GO; GO:0007420; P:brain development; IMP:MGI. DR GO; GO:0043010; P:camera-type eye development; IMP:MGI. DR GO; GO:0030154; P:cell differentiation; IMP:MGI. DR GO; GO:0045165; P:cell fate commitment; IMP:MGI. DR GO; GO:0001709; P:cell fate determination; IMP:MGI. DR GO; GO:0008283; P:cell population proliferation; IMP:MGI. DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEA:Ensembl. DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl. DR GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl. DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI. DR GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IEA:Ensembl. DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl. DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl. DR GO; GO:0021987; P:cerebral cortex development; IMP:MGI. DR GO; GO:0021796; P:cerebral cortex regionalization; IMP:MGI. DR GO; GO:0006338; P:chromatin remodeling; IMP:MGI. DR GO; GO:0021902; P:commitment of neuronal cell to specific neuron type in forebrain; IMP:MGI. DR GO; GO:0061303; P:cornea development in camera-type eye; ISO:MGI. DR GO; GO:0080111; P:DNA demethylation; IMP:MGI. DR GO; GO:0006306; P:DNA methylation; IMP:MGI. DR GO; GO:0009950; P:dorsal/ventral axis specification; IMP:MGI. DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:MGI. DR GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IGI:MGI. DR GO; GO:0002064; P:epithelial cell development; ISO:MGI. DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:MGI. DR GO; GO:0042462; P:eye photoreceptor cell development; IMP:MGI. DR GO; GO:0030900; P:forebrain development; IMP:MGI. DR GO; GO:0021798; P:forebrain dorsal/ventral pattern formation; IMP:MGI. DR GO; GO:0021905; P:forebrain-midbrain boundary formation; IMP:MGI. DR GO; GO:0010467; P:gene expression; IMP:MGI. DR GO; GO:0002067; P:glandular epithelial cell differentiation; IMP:MGI. DR GO; GO:0042593; P:glucose homeostasis; ISO:MGI. DR GO; GO:0021986; P:habenula development; IMP:MGI. DR GO; GO:0030902; P:hindbrain development; ISO:MGI. DR GO; GO:1901142; P:insulin metabolic process; ISO:MGI. DR GO; GO:0022027; P:interkinetic nuclear migration; ISO:MGI. DR GO; GO:0061072; P:iris morphogenesis; ISO:MGI. DR GO; GO:0030216; P:keratinocyte differentiation; IMP:MGI. DR GO; GO:0032808; P:lacrimal gland development; IMP:MGI. DR GO; GO:0098598; P:learned vocalization behavior or vocal learning; ISO:MGI. DR GO; GO:0002088; P:lens development in camera-type eye; IMP:MGI. DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI. DR GO; GO:2000178; P:negative regulation of neural precursor cell proliferation; IMP:MGI. DR GO; GO:0007406; P:negative regulation of neuroblast proliferation; IMP:MGI. DR GO; GO:0045665; P:negative regulation of neuron differentiation; IGI:MGI. DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:MGI. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0007399; P:nervous system development; IMP:BHF-UCL. DR GO; GO:0001755; P:neural crest cell migration; ISO:MGI. DR GO; GO:0061351; P:neural precursor cell proliferation; IMP:MGI. DR GO; GO:0007405; P:neuroblast proliferation; IMP:MGI. DR GO; GO:0030182; P:neuron differentiation; IMP:MGI. DR GO; GO:0001764; P:neuron migration; IMP:MGI. DR GO; GO:0021772; P:olfactory bulb development; ISO:MGI. DR GO; GO:0061034; P:olfactory bulb mitral cell layer development; ISO:MGI. DR GO; GO:0021778; P:oligodendrocyte cell fate specification; IMP:MGI. DR GO; GO:0021543; P:pallium development; IMP:MGI. DR GO; GO:0003322; P:pancreatic A cell development; IMP:BHF-UCL. DR GO; GO:0003310; P:pancreatic A cell differentiation; ISO:MGI. DR GO; GO:0021983; P:pituitary gland development; IMP:MGI. DR GO; GO:0042660; P:positive regulation of cell fate specification; ISO:MGI. DR GO; GO:1904798; P:positive regulation of core promoter binding; ISS:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:BHF-UCL. DR GO; GO:0030858; P:positive regulation of epithelial cell differentiation; IMP:MGI. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL. DR GO; GO:0120008; P:positive regulation of glutamatergic neuron differentiation; ISO:MGI. DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:MGI. DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IMP:MGI. DR GO; GO:2001224; P:positive regulation of neuron migration; ISO:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB. DR GO; GO:0033365; P:protein localization to organelle; IMP:MGI. DR GO; GO:0003002; P:regionalization; IMP:MGI. DR GO; GO:0009786; P:regulation of asymmetric cell division; IMP:MGI. DR GO; GO:0030334; P:regulation of cell migration; IMP:MGI. DR GO; GO:0006355; P:regulation of DNA-templated transcription; TAS:MGI. DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI. DR GO; GO:0050767; P:regulation of neurogenesis; IMP:MGI. DR GO; GO:0045664; P:regulation of neuron differentiation; IMP:MGI. DR GO; GO:0010975; P:regulation of neuron projection development; ISO:MGI. DR GO; GO:0048505; P:regulation of timing of cell differentiation; IMP:MGI. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:MGI. DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl. DR GO; GO:0009611; P:response to wounding; IEA:Ensembl. DR GO; GO:0060041; P:retina development in camera-type eye; IGI:MGI. DR GO; GO:0021593; P:rhombomere morphogenesis; ISO:MGI. DR GO; GO:0007435; P:salivary gland morphogenesis; IMP:MGI. DR GO; GO:1904937; P:sensory neuron migration; ISO:MGI. DR GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IDA:MGI. DR GO; GO:0007224; P:smoothened signaling pathway; IDA:MGI. DR GO; GO:0021978; P:telencephalon regionalization; IMP:MGI. DR GO; GO:0006366; P:transcription by RNA polymerase II; IGI:MGI. DR GO; GO:0003309; P:type B pancreatic cell differentiation; IMP:MGI. DR GO; GO:0021517; P:ventral spinal cord development; IMP:UniProtKB. DR CDD; cd00086; homeodomain; 1. DR CDD; cd00131; PAX; 1. DR Gene3D; 1.10.10.60; Homeodomain-like; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2. DR InterPro; IPR009057; Homeobox-like_sf. DR InterPro; IPR017970; Homeobox_CS. DR InterPro; IPR001356; Homeobox_dom. DR InterPro; IPR043182; PAIRED_DNA-bd_dom. DR InterPro; IPR001523; Paired_dom. DR InterPro; IPR043565; PAX_fam. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR PANTHER; PTHR45636:SF21; PAIRED BOX PROTEIN PAX-6; 1. DR PANTHER; PTHR45636; PAIRED BOX PROTEIN PAX-6-RELATED-RELATED; 1. DR Pfam; PF00046; Homeodomain; 1. DR Pfam; PF00292; PAX; 1. DR PRINTS; PR00027; PAIREDBOX. DR SMART; SM00389; HOX; 1. DR SMART; SM00351; PAX; 1. DR SUPFAM; SSF46689; Homeodomain-like; 2. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR PROSITE; PS00034; PAIRED_1; 1. DR PROSITE; PS51057; PAIRED_2; 1. DR Genevisible; P63015; MM. PE 1: Evidence at protein level; KW Alternative splicing; Cytoplasm; Developmental protein; Differentiation; KW Direct protein sequencing; Disease variant; DNA-binding; Homeobox; Nucleus; KW Paired box; Reference proteome; Transcription; Transcription regulation; KW Ubl conjugation. FT CHAIN 1..422 FT /note="Paired box protein Pax-6" FT /id="PRO_0000050186" FT DNA_BIND 4..130 FT /note="Paired" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00381" FT DNA_BIND 210..269 FT /note="Homeobox" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108" FT REGION 7..63 FT /note="PAI subdomain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00381" FT REGION 82..130 FT /note="RED subdomain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00381" FT REGION 162..201 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 269..311 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 345..422 FT /note="Required for suppression of NFATC1-mediated FT transcription" FT /evidence="ECO:0000269|PubMed:23990468" FT COMPBIAS 167..199 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 276..311 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 1..136 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_054294" FT VAR_SEQ 47 FT /note="Q -> QTHADAKVQVLDNEN (in isoform 5a)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:1687460" FT /id="VSP_011530" FT VARIANT 259 FT /note="S -> P (in Pax6(4Neu); defective)" FT /evidence="ECO:0000269|PubMed:11779807" FT CONFLICT 18 FT /note="G -> E (in Ref. 3; BAC25729)" FT /evidence="ECO:0000305" FT CONFLICT 31 FT /note="E -> Q (in Ref. 3; BAC25729)" FT /evidence="ECO:0000305" FT CONFLICT 287 FT /note="I -> T (in Ref. 6; AAA40109)" FT /evidence="ECO:0000305" FT CONFLICT 421..422 FT /note="Missing (in Ref. 6; AAA40109)" FT /evidence="ECO:0000305" SQ SEQUENCE 422 AA; 46683 MW; C33CDD2C1B13C397 CRC64; MQNSHSGVNQ LGGVFVNGRP LPDSTRQKIV ELAHSGARPC DISRILQVSN GCVSKILGRY YETGSIRPRA IGGSKPRVAT PEVVSKIAQY KRECPSIFAW EIRDRLLSEG VCTNDNIPSV SSINRVLRNL ASEKQQMGAD GMYDKLRMLN GQTGSWGTRP GWYPGTSVPG QPTQDGCQQQ EGGGENTNSI SSNGEDSDEA QMRLQLKRKL QRNRTSFTQE QIEALEKEFE RTHYPDVFAR ERLAAKIDLP EARIQVWFSN RRAKWRREEK LRNQRRQASN TPSHIPISSS FSTSVYQPIP QPTTPVSSFT SGSMLGRTDT ALTNTYSALP PMPSFTMANN LPMQPPVPSQ TSSYSCMLPT SPSVNGRSYD TYTPPHMQTH MNSQPMGTSG TTSTGLISPG VSVPVQVPGS EPDMSQYWPR LQ //