FOXJ2_MOUSE
ID FOXJ2_MOUSE Reviewed; 565 AA.
AC Q9ES18;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Forkhead box protein J2;
DE AltName: Full=Fork head homologous X;
GN Name=Foxj2; Synonyms=Fhx;
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], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Brain;
RX PubMed=11025217; DOI=10.1016/s0925-4773(00)00410-x;
RA Granadino B., Arias-de-la-Fuente C., Perez-Sanchez C., Parraga M.,
RA Lopez-Fernandez L.A., del Mazo J., Rey-Campos J.;
RT "Fhx (Foxj2) expression is activated during spermatogenesis and very early
RT in embryonic development.";
RL Mech. Dev. 97:157-160(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=16376864; DOI=10.1016/j.brainres.2005.11.022;
RA Wijchers P.J.E.C., Hoekman M.F.M., Burbach J.P.H., Smidt M.P.;
RT "Identification of forkhead transcription factors in cortical and
RT dopaminergic areas of the adult murine brain.";
RL Brain Res. 1068:23-33(2006).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=27316861; DOI=10.1002/mrd.22671;
RA Miao H., Miao C.X., Li N., Han J.;
RT "FOXJ2 controls meiosis during spermatogenesis in male mice.";
RL Mol. Reprod. Dev. 83:684-691(2016).
CC -!- FUNCTION: Transcriptional activator. Able to bind to two different type
CC of DNA binding sites (By similarity). Plays an important role in
CC spermatogenesis, especially in spermatocyte meiosis (PubMed:11025217,
CC PubMed:15489334). {ECO:0000250|UniProtKB:Q9P0K8,
CC ECO:0000269|PubMed:11025217, ECO:0000269|PubMed:15489334}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Spermtaocytes (at protein level). Expressed in
CC adult brain, heart skeletal muscle, lung, kidney and gonads. Liver,
CC small intestine, and spleen also show expression but at lower levels.
CC In the testis, expressed from pachytene spermatocytes to round
CC spermatids, but not in spermatogonia. In addition to the germ lineage,
CC also expressed in Sertoli cells of the testis. In the ovary, only
CC granulosa cells of the follicles show expression. In the brain,
CC expressed in the piriform cortex, hippocampus, habenula and in the
CC granula cell layer in the cerebellum. {ECO:0000269|PubMed:11025217,
CC ECO:0000269|PubMed:16376864, ECO:0000269|PubMed:27316861}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. Zygotic
CC expression first begins in 8-cell stage embryos, with expression
CC increasing in blastocysts. In embryos, both cell layers of the
CC blastocyst: the trophectoderm (TE) and the inner cell mass (ICM) show
CC expression. {ECO:0000269|PubMed:11025217}.
CC -!- DISRUPTION PHENOTYPE: Male germ-cell-specific conditional knockout
CC results in complete male infertility and meiotic arrest in
CC spermatocytes. Spermatocytes show aberrant chromosomal synapsis and DNA
CC double-strand breaks (DSB) repair and significantly reduced expression
CC of DSB repair-associated genes and meiotic arrest-related genes.
CC {ECO:0000269|PubMed:27316861}.
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DR EMBL; AF253052; AAG30406.1; -; mRNA.
DR EMBL; BC040395; AAH40395.1; -; mRNA.
DR CCDS; CCDS20503.1; -.
DR RefSeq; NP_068699.1; NM_021899.3.
DR AlphaFoldDB; Q9ES18; -.
DR SMR; Q9ES18; -.
DR BioGRID; 208639; 1.
DR IntAct; Q9ES18; 1.
DR STRING; 10090.ENSMUSP00000003238; -.
DR iPTMnet; Q9ES18; -.
DR PhosphoSitePlus; Q9ES18; -.
DR EPD; Q9ES18; -.
DR MaxQB; Q9ES18; -.
DR PaxDb; Q9ES18; -.
DR PRIDE; Q9ES18; -.
DR ProteomicsDB; 267617; -.
DR Antibodypedia; 1748; 169 antibodies from 20 providers.
DR DNASU; 60611; -.
DR Ensembl; ENSMUST00000003238; ENSMUSP00000003238; ENSMUSG00000003154.
DR Ensembl; ENSMUST00000177927; ENSMUSP00000137645; ENSMUSG00000003154.
DR GeneID; 60611; -.
DR KEGG; mmu:60611; -.
DR UCSC; uc012esh.1; mouse.
DR CTD; 55810; -.
DR MGI; MGI:1926805; Foxj2.
DR VEuPathDB; HostDB:ENSMUSG00000003154; -.
DR eggNOG; KOG2294; Eukaryota.
DR GeneTree; ENSGT00940000161053; -.
DR HOGENOM; CLU_034661_0_0_1; -.
DR InParanoid; Q9ES18; -.
DR OMA; SHFSELM; -.
DR OrthoDB; 1270467at2759; -.
DR PhylomeDB; Q9ES18; -.
DR TreeFam; TF333250; -.
DR BioGRID-ORCS; 60611; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Foxj2; mouse.
DR PRO; PR:Q9ES18; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9ES18; protein.
DR Bgee; ENSMUSG00000003154; Expressed in tarsal region and 251 other tissues.
DR ExpressionAtlas; Q9ES18; baseline and differential.
DR Genevisible; Q9ES18; MM.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
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:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
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:0016525; P:negative regulation of angiogenesis; ISO:MGI.
DR GO; GO:0110059; P:negative regulation of blood vessel endothelial cell differentiation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; 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; 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; PS00658; FORK_HEAD_2; 1.
DR PROSITE; PS50039; FORK_HEAD_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Differentiation; DNA-binding; Meiosis; Nucleus;
KW Phosphoprotein; Reference proteome; Spermatogenesis; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9P0K8"
FT CHAIN 2..565
FT /note="Forkhead box protein J2"
FT /id="PRO_0000091854"
FT DNA_BIND 66..143
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 29..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..311
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0K8"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0K8"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0K8"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0K8"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0K8"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0K8"
SQ SEQUENCE 565 AA; 61570 MW; 9178AFF3F9227AD4 CRC64;
MASDLESSLT SIDWLPQLTL RATIEKLGSA SQAGPPGGAR KCSPGSPTDP NATLSKDEAA
VHQDGKPRYS YATLITYAIN SSPAKKMTLS EIYRWICDNF PYYKNAGIGW KNSIRHNLSL
NKCFRKVPRP RDDPGKGSYW TIDTCPDISR KRRHPPDDDL SQDSPEQEAS KSPRGGVPGS
GEASLSHEGT PQMSLQSPSS VANYSQGPGS VDGGAVAAGA PGQESTEGAP PLYNTNHDFK
FSYSEINFQD LSWSFRNLYK SMLERSSSSQ HGFSSLLGDM PPSNNYYVYQ QQQQQQPPPQ
PQPPPQQPQP QQQQAPTQGP SNVGGAPPLH TPSPDGCTTP GGKQAGAEGY GPPTGMAMHP
PPLQHGGYHP HQHHPHSHPA QQPPQPQAQS QASINSTGFA FPPDWCSNID SLKESFKMVN
RLNWSSIEQS QFSELMESLR QAEQRNWTLD QHHIANLCDS LNHFLTQTGH MPQQGGSHRP
PAPSRITDSC ALTSGKPEPS MNQVNSYGHP QASHLYPGPA PMYPISTQDS AGYNRPAHHM
VPRPPVPPPG ANEEITDDFD WDLIT
