ID PAX3_MOUSE Reviewed; 479 AA. AC P24610; Q3UFQ9; Q8BRE7; Q9CXI6; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 2. DT 24-JAN-2024, entry version 200. DE RecName: Full=Paired box protein Pax-3; GN Name=Pax3; Synonyms=Pax-3; 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=2022185; DOI=10.1002/j.1460-2075.1991.tb08054.x; RA Goulding M.D., Chalepakis G., Deutsch U., Erselius J.R., Gruss P.; RT "Pax-3, a novel murine DNA binding protein expressed during early RT neurogenesis."; RL EMBO J. 10:1135-1147(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Head; 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 [MRNA] OF 219-260, DISEASE, AND FUNCTION. RX PubMed=1682057; DOI=10.1016/0092-8674(91)90071-6; RA Epstein D.J., Vekemans M., Gros P.; RT "Splotch (Sp2H), a mutation affecting development of the mouse neural tube, RT shows a deletion within the paired homeodomain of Pax-3."; RL Cell 67:767-774(1991). RN [4] RP INTERACTION WITH TBX18. RX PubMed=18644785; DOI=10.1074/jbc.m802723200; RA Farin H.F., Mansouri A., Petry M., Kispert A.; RT "T-box protein Tbx18 interacts with the paired box protein Pax3 in the RT development of the paraxial mesoderm."; RL J. Biol. Chem. 283:25372-25380(2008). RN [5] RP FUNCTION, AND INTERACTION WITH PAXBP1. RX PubMed=22862948; DOI=10.1016/j.stem.2012.05.022; RA Diao Y., Guo X., Li Y., Sun K., Lu L., Jiang L., Fu X., Zhu H., Sun H., RA Wang H., Wu Z.; RT "Pax3/7BP is a Pax7- and Pax3-binding protein that regulates the RT proliferation of muscle precursor cells by an epigenetic mechanism."; RL Cell Stem Cell 11:231-241(2012). RN [6] RP VARIANT SPD ARG-42. RX PubMed=8406487; DOI=10.1006/geno.1993.1333; RA Vogan K.J., Epstein D.J., Trasler D.G., Gros P.; RT "The splotch-delayed (Spd) mouse mutant carries a point mutation within the RT paired box of the Pax-3 gene."; RL Genomics 17:364-369(1993). CC -!- FUNCTION: Transcription factor that may regulate cell proliferation, CC migration and apoptosis. Involved in neural development and myogenesis. CC Transcriptional activator of MITF, acting synergistically with SOX10 CC (By similarity). {ECO:0000250|UniProtKB:P23760, CC ECO:0000269|PubMed:1682057, ECO:0000269|PubMed:22862948}. CC -!- SUBUNIT: Can bind to DNA as homodimer or a heterodimer with PAX7. CC Interacts with DAXX. Interacts with PAXBP1; the interaction links PAX3 CC to a WDR5-containing histone methyltransferase complex. Interacts with CC TBX18. Interacts with SOX10 (By similarity). CC {ECO:0000250|UniProtKB:P23760, ECO:0000269|PubMed:18644785, CC ECO:0000269|PubMed:22862948}. CC -!- INTERACTION: CC P24610; P13405: Rb1; NbExp=3; IntAct=EBI-1208116, EBI-971782; CC P24610; P55036: PSMD4; Xeno; NbExp=3; IntAct=EBI-1208116, EBI-359318; CC P24610; P54727: RAD23B; Xeno; NbExp=4; IntAct=EBI-1208116, EBI-954531; CC P24610; P28749: RBL1; Xeno; NbExp=3; IntAct=EBI-1208116, EBI-971402; CC P24610; Q08999: RBL2; Xeno; NbExp=3; IntAct=EBI-1208116, EBI-971439; CC P24610; P0CG47: UBB; Xeno; NbExp=2; IntAct=EBI-1208116, EBI-413034; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P23760}. CC -!- DEVELOPMENTAL STAGE: Expressed during early neurogenesis. CC -!- DISEASE: Note=The Splotch (Sp) mouse mutant displays defects in neural CC tube closure in the form of exencephaly and spina bifida. The splotch- CC delayed (Spd) phenotype is less severe than the other Sp alleles. CC {ECO:0000269|PubMed:1682057}. CC -!- SIMILARITY: Belongs to the paired homeobox family. {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; X59358; CAA42008.1; -; mRNA. DR EMBL; AK014337; BAB29280.1; -; mRNA. DR EMBL; AK045018; BAC32185.1; -; mRNA. DR EMBL; AK148354; BAE28501.1; -; mRNA. DR EMBL; S66429; AAB20359.1; -; mRNA. DR EMBL; S66433; AAB20360.1; -; mRNA. DR CCDS; CCDS15082.1; -. DR PIR; S15031; S15031. DR RefSeq; NP_001152992.1; NM_001159520.1. DR RefSeq; NP_032807.3; NM_008781.4. DR AlphaFoldDB; P24610; -. DR SMR; P24610; -. DR BioGRID; 202030; 22. DR CORUM; P24610; -. DR IntAct; P24610; 9. DR MINT; P24610; -. DR STRING; 10090.ENSMUSP00000004994; -. DR iPTMnet; P24610; -. DR PhosphoSitePlus; P24610; -. DR MaxQB; P24610; -. DR PaxDb; 10090-ENSMUSP00000004994; -. DR PeptideAtlas; P24610; -. DR Antibodypedia; 4602; 590 antibodies from 45 providers. DR DNASU; 18505; -. DR Ensembl; ENSMUST00000087086.7; ENSMUSP00000084320.7; ENSMUSG00000004872.16. DR GeneID; 18505; -. DR KEGG; mmu:18505; -. DR UCSC; uc007bqb.2; mouse. DR AGR; MGI:97487; -. DR CTD; 5077; -. DR MGI; MGI:97487; Pax3. DR VEuPathDB; HostDB:ENSMUSG00000004872; -. DR eggNOG; KOG0849; Eukaryota. DR GeneTree; ENSGT00940000156504; -. DR HOGENOM; CLU_019281_8_0_1; -. DR InParanoid; P24610; -. DR OrthoDB; 5398393at2759; -. DR PhylomeDB; P24610; -. DR Reactome; R-MMU-3214847; HATs acetylate histones. DR BioGRID-ORCS; 18505; 2 hits in 79 CRISPR screens. DR ChiTaRS; Pax3; mouse. DR PRO; PR:P24610; -. DR Proteomes; UP000000589; Chromosome 1. DR RNAct; P24610; Protein. DR Bgee; ENSMUSG00000004872; Expressed in trunk somite and 144 other cell types or tissues. DR ExpressionAtlas; P24610; baseline and differential. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0005667; C:transcription regulator complex; TAS:MGI. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:MGI. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:MGI. DR GO; GO:0071837; F:HMG box domain binding; ISO:MGI. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. 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:0001221; F:transcription coregulator binding; IPI:ARUK-UCL. DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central. DR GO; GO:0055007; P:cardiac muscle cell differentiation; NAS:UniProtKB. DR GO; GO:0016477; P:cell migration; IMP:MGI. DR GO; GO:0008283; P:cell population proliferation; IMP:MGI. DR GO; GO:0048066; P:developmental pigmentation; IMP:MGI. DR GO; GO:0007507; P:heart development; IMP:MGI. DR GO; GO:0060594; P:mammary gland specification; IMP:MGI. DR GO; GO:0007517; P:muscle organ development; IMP:MGI. DR GO; GO:0051451; P:myoblast migration; IMP:MGI. DR GO; GO:0051450; P:myoblast proliferation; IMP:MGI. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI. DR GO; GO:0001755; P:neural crest cell migration; IMP:MGI. DR GO; GO:0001843; P:neural tube closure; IMP:MGI. DR GO; GO:0021915; P:neural tube development; IGI:MGI. DR GO; GO:0048663; P:neuron fate commitment; IGI:MGI. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:MGI. DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0014807; P:regulation of somitogenesis; IMP:MGI. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0035914; P:skeletal muscle cell differentiation; NAS:UniProtKB. DR GO; GO:0060538; P:skeletal muscle organ development; IMP:MGI. DR GO; GO:0021527; P:spinal cord association neuron differentiation; IGI:MGI. DR GO; GO:0072089; P:stem cell proliferation; IMP:MGI. 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; IPR022106; Pax7_C. DR InterPro; IPR043565; PAX_fam. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR PANTHER; PTHR45636:SF17; PAIRED BOX PROTEIN PAX-3; 1. DR PANTHER; PTHR45636; PAIRED BOX PROTEIN PAX-6-RELATED-RELATED; 1. DR Pfam; PF00046; Homeodomain; 1. DR Pfam; PF00292; PAX; 1. DR Pfam; PF12360; Pax7; 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; P24610; MM. PE 1: Evidence at protein level; KW Developmental protein; Disease variant; DNA-binding; Homeobox; Myogenesis; KW Neurogenesis; Nucleus; Paired box; Phosphoprotein; Reference proteome; KW Transcription; Transcription regulation. FT CHAIN 1..479 FT /note="Paired box protein Pax-3" FT /id="PRO_0000050179" FT DNA_BIND 34..161 FT /note="Paired" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00381" FT DNA_BIND 219..278 FT /note="Homeobox" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108" FT REGION 1..21 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 37..93 FT /note="PAI subdomain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00381" FT REGION 113..161 FT /note="RED subdomain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00381" FT REGION 165..228 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 309..351 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 165..190 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 209..228 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 201 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P23760" FT MOD_RES 205 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P23760" FT MOD_RES 209 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P23760" FT VARIANT 42 FT /note="G -> R (in Spd)" FT /evidence="ECO:0000269|PubMed:8406487" FT CONFLICT 140 FT /note="D -> G (in Ref. 2; BAC32185)" FT /evidence="ECO:0000305" FT CONFLICT 310 FT /note="T -> H (in Ref. 1; CAA42008)" FT /evidence="ECO:0000305" SQ SEQUENCE 479 AA; 52949 MW; 8806E551FFB755A0 CRC64; MTTLAGAVPR MMRPGPGQNY PRSGFPLEVS TPLGQGRVNQ LGGVFINGRP LPNHIRHKIV EMAHHGIRPC VISRQLRVSH GCVSKILCRY QETGSIRPGA IGGSKPKQVT TPDVEKKIEE YKRENPGMFS WEIRDKLLKD AVCDRNTVPS VSSISRILRS KFGKGEEEEA DLERKEAEES EKKAKHSIDG ILSERASAPQ SDEGSDIDSE PDLPLKRKQR RSRTTFTAEQ LEELERAFER THYPDIYTRE ELAQRAKLTE ARVQVWFSNR RARWRKQAGA NQLMAFNHLI PGGFPPTAMP TLPTYQLSET SYQPTSIPQA VSDPSSTVHR PQPLPPSTVH QSTIPSNADS SSAYCLPSTR HGFSSYTDSF VPPSGPSNPM NPTIGNGLSP QVMGLLTNHG GVPHQPQTDY ALSPLTGGLE PTTTVSASCS QRLEHMKNVD SLPTSQPYCP PTYSTAGYSM DPVTGYQYGQ YGQSKPWTF //