FOXJ3_MOUSE
ID FOXJ3_MOUSE Reviewed; 623 AA.
AC Q8BUR3; A2AA37; A2AA38; Q3UTD8;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Forkhead box protein J3;
GN Name=Foxj3; Synonyms=Kiaa1041;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Egg;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Olfactory epithelium;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Spleen, and Testis;
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).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19914232; DOI=10.1016/j.ydbio.2009.11.015;
RA Alexander M.S., Shi X., Voelker K.A., Grange R.W., Garcia J.A.,
RA Hammer R.E., Garry D.J.;
RT "Foxj3 transcriptionally activates Mef2c and regulates adult skeletal
RT muscle fiber type identity.";
RL Dev. Biol. 337:396-404(2010).
RN [7]
RP INDUCTION.
RX PubMed=23047984; DOI=10.1152/ajpendo.00097.2012;
RA Yamamoto H., Morino K., Nishio Y., Ugi S., Yoshizaki T., Kashiwagi A.,
RA Maegawa H.;
RT "MicroRNA-494 regulates mitochondrial biogenesis in skeletal muscle through
RT mitochondrial transcription factor A and Forkhead box j3.";
RL Am. J. Physiol. 303:E1419-1427(2012).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=27739607; DOI=10.1002/mrd.22750;
RA Ni L., Xie H., Tan L.;
RT "Multiple roles of FOXJ3 in spermatogenesis: A lesson from Foxj3
RT conditional knockout mouse models.";
RL Mol. Reprod. Dev. 83:1060-1069(2016).
CC -!- FUNCTION: Transcriptional activator of MEF2C involved in the regulation
CC of adult muscle fiber type identity and skeletal muscle regeneration
CC (PubMed:19914232). Plays an important role in spermatogenesis
CC (PubMed:27739607). Required for the survival of spermatogonia and
CC participates in spermatocyte meiosis (PubMed:27739607).
CC {ECO:0000269|PubMed:19914232, ECO:0000269|PubMed:27739607}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BUR3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BUR3-2; Sequence=VSP_010368;
CC -!- TISSUE SPECIFICITY: Highly expressed in spermatogonia, spermatocytes,
CC and round spermatids within the testis (at protein level).
CC {ECO:0000269|PubMed:27739607}.
CC -!- DEVELOPMENTAL STAGE: Accumulates in the testis starting at postnatal
CC day 3, and remains at a steady level from 1 to 3 weeks in age.
CC {ECO:0000269|PubMed:27739607}.
CC -!- INDUCTION: Increased markedly during skeletal muscle differentiation
CC (at protein level). {ECO:0000269|PubMed:23047984}.
CC -!- DISRUPTION PHENOTYPE: Null mice have an abnormal skeletal muscle fiber
CC type ratio in males as well as defects in muscle regeneration following
CC injury (PubMed:19914232). Male germ-cell-specific conditional knockout
CC results in complete male infertility, early loss of spermatogonia and
CC meiotic arrest in spermatocytes (PubMed:27739607). Spermatocytes show
CC significantly reduced expression meiotic arrest-related genes
CC (PubMed:27739607). {ECO:0000269|PubMed:19914232,
CC ECO:0000269|PubMed:27739607}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98081.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK082840; BAC38648.1; -; mRNA.
DR EMBL; AK129271; BAC98081.1; ALT_INIT; mRNA.
DR EMBL; AK139508; BAE24042.1; -; mRNA.
DR EMBL; AL645563; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC058231; AAH58231.1; -; mRNA.
DR CCDS; CCDS18585.1; -. [Q8BUR3-1]
DR CCDS; CCDS71462.1; -. [Q8BUR3-2]
DR RefSeq; NP_001277625.1; NM_001290696.1. [Q8BUR3-2]
DR RefSeq; NP_766287.1; NM_172699.3. [Q8BUR3-1]
DR RefSeq; XP_006503080.1; XM_006503017.3. [Q8BUR3-1]
DR RefSeq; XP_011238799.1; XM_011240497.2.
DR RefSeq; XP_017175639.1; XM_017320150.1.
DR AlphaFoldDB; Q8BUR3; -.
DR SMR; Q8BUR3; -.
DR STRING; 10090.ENSMUSP00000035746; -.
DR iPTMnet; Q8BUR3; -.
DR PhosphoSitePlus; Q8BUR3; -.
DR EPD; Q8BUR3; -.
DR jPOST; Q8BUR3; -.
DR MaxQB; Q8BUR3; -.
DR PaxDb; Q8BUR3; -.
DR PRIDE; Q8BUR3; -.
DR ProteomicsDB; 271794; -. [Q8BUR3-1]
DR ProteomicsDB; 271795; -. [Q8BUR3-2]
DR Antibodypedia; 32193; 197 antibodies from 27 providers.
DR DNASU; 230700; -.
DR Ensembl; ENSMUST00000044564; ENSMUSP00000035746; ENSMUSG00000032998. [Q8BUR3-1]
DR Ensembl; ENSMUST00000106310; ENSMUSP00000101917; ENSMUSG00000032998. [Q8BUR3-2]
DR GeneID; 230700; -.
DR KEGG; mmu:230700; -.
DR UCSC; uc008umt.2; mouse. [Q8BUR3-1]
DR UCSC; uc008umu.2; mouse. [Q8BUR3-2]
DR CTD; 22887; -.
DR MGI; MGI:2443432; Foxj3.
DR VEuPathDB; HostDB:ENSMUSG00000032998; -.
DR eggNOG; KOG2294; Eukaryota.
DR GeneTree; ENSGT00940000160362; -.
DR HOGENOM; CLU_030503_0_0_1; -.
DR InParanoid; Q8BUR3; -.
DR OMA; QSLSQQX; -.
DR OrthoDB; 1270467at2759; -.
DR PhylomeDB; Q8BUR3; -.
DR TreeFam; TF333250; -.
DR BioGRID-ORCS; 230700; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Foxj3; mouse.
DR PRO; PR:Q8BUR3; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8BUR3; protein.
DR Bgee; ENSMUSG00000032998; Expressed in animal zygote and 271 other tissues.
DR ExpressionAtlas; Q8BUR3; baseline and differential.
DR Genevisible; Q8BUR3; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
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; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007141; P:male meiosis I; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR CDD; cd00059; FH; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR001766; Fork_head_dom.
DR InterPro; IPR045912; FOXJ2/3-like.
DR InterPro; IPR018122; TF_fork_head_CS_1.
DR InterPro; IPR030456; TF_fork_head_CS_2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR46078; PTHR46078; 1.
DR Pfam; PF00250; Forkhead; 1.
DR PRINTS; PR00053; FORKHEAD.
DR SMART; SM00339; FH; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00657; FORK_HEAD_1; 1.
DR PROSITE; PS00658; FORK_HEAD_2; 1.
DR PROSITE; PS50039; FORK_HEAD_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Differentiation; DNA-binding; Meiosis; Nucleus;
KW Phosphoprotein; Reference proteome; Spermatogenesis; Transcription;
KW Transcription regulation.
FT CHAIN 1..623
FT /note="Forkhead box protein J3"
FT /id="PRO_0000091856"
FT DNA_BIND 78..173
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 143..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..402
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPW0"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPW0"
FT VAR_SEQ 177..210
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_010368"
SQ SEQUENCE 623 AA; 68954 MW; 4D449A868C8EB04E CRC64;
MGLYGQACPS VTSLRMTSEL ESSLTSMDWL PQLTMRAAIQ KSDATQNAHG TGISKKNALL
DPNTTLDQEE VQQHKDGKPP YSYASLITFA INSSPKKKMT LSEIYQWICD NFPYYREAGS
GWKNSIRHNL SLNKCFLKVP RSKDDPGKGS YWAIDTNPKE DTLPTRPKKR ARSVERASTP
YSIDSDSLGM ECIISGSASP TLAINTVTNK VTLYNADQDG SDSPRSSLNN SLSDQSLASV
NLNSVGSVHS YTPVTNHPEP VSQPLTPQQQ QQPQYNLPER EKQLLFTEYN FEDLSASFRS
LYKSVFEQSL SQQGLMSIPS ESSQQSHTSC SYQHSPSSTV TSHPHSNQSS LPNNHSGLSA
TGSNSVAQVS LSHPQMHPQP SPHTPHRPHG LPQHPQRPQH PAPHPQQHSQ LQPPHSQHPP
PHQHIQHHPN HQHQTLAHQP PPPPQQVSCN SGVSSDWYAT LDMLKESCRI ASSVNWSDVD
LSQFQGLMES MRQADLKNWS LDQVQFADLC SSLNQFFTQT GLIHSQSNVP QNVCHGAMHP
AKPSQHIGAG NLYIDSRQSL PPSVMPPPGY PHIPQALNTP GTTMAGHHGA MNQQHMMPSQ
AFPMRRPLPP DDIQDDFDWD SIV
