PAX6_MOUSE
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 03-AUG-2022, entry version 177.
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};
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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 iPTMnet; P63015; -.
DR PhosphoSitePlus; P63015; -.
DR MaxQB; P63015; -.
DR PaxDb; P63015; -.
DR PRIDE; P63015; -.
DR ProteomicsDB; 294331; -. [P63015-1]
DR ProteomicsDB; 294332; -. [P63015-2]
DR ProteomicsDB; 294333; -. [P63015-3]
DR Antibodypedia; 12821; 935 antibodies from 49 providers.
DR DNASU; 18508; -.
DR Ensembl; ENSMUST00000090391; ENSMUSP00000087870; ENSMUSG00000027168. [P63015-2]
DR Ensembl; ENSMUST00000090397; ENSMUSP00000087878; ENSMUSG00000027168. [P63015-1]
DR Ensembl; ENSMUST00000111082; ENSMUSP00000106711; ENSMUSG00000027168. [P63015-1]
DR Ensembl; ENSMUST00000111083; ENSMUSP00000106712; ENSMUSG00000027168. [P63015-1]
DR Ensembl; ENSMUST00000111085; ENSMUSP00000106714; ENSMUSG00000027168. [P63015-2]
DR Ensembl; ENSMUST00000111086; ENSMUSP00000106715; ENSMUSG00000027168. [P63015-2]
DR Ensembl; ENSMUST00000111087; ENSMUSP00000106716; ENSMUSG00000027168. [P63015-1]
DR Ensembl; ENSMUST00000167211; ENSMUSP00000129344; ENSMUSG00000027168. [P63015-2]
DR GeneID; 18508; -.
DR KEGG; mmu:18508; -.
DR UCSC; uc008lku.2; mouse. [P63015-2]
DR UCSC; uc008lkv.2; mouse. [P63015-1]
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; WYPSGAG; -.
DR OrthoDB; 1152885at2759; -.
DR TreeFam; TF320146; -.
DR BioGRID-ORCS; 18508; 2 hits in 72 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 171 other tissues.
DR ExpressionAtlas; P63015; baseline and differential.
DR Genevisible; P63015; MM.
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:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
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:0016573; P:histone acetylation; IMP: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: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:0010942; P:positive regulation of cell death; ISO: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: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:0070094; P:positive regulation of glucagon secretion; ISO:MGI.
DR GO; GO:0120008; P:positive regulation of glutamatergic neuron differentiation; 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:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0033365; P:protein localization to organelle; IMP:MGI.
DR GO; GO:0006468; P:protein phosphorylation; 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: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:0006355; P:regulation of transcription, DNA-templated; TAS:MGI.
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; 1.10.10.10; -; 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; PTHR45636; 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; SSF46689; 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.
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
