ID   FOXL2_ELLLU             Reviewed;         373 AA.
AC   Q4VUF1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Forkhead box protein L2;
GN   Name=FOXL2;
OS   Ellobius lutescens (Transcaucasian mole vole).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Arvicolinae; Ellobius.
OX   NCBI_TaxID=39086;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15965789; DOI=10.1007/s00335-004-2019-7;
RA   Baumstark A., Hameister H., Hakhverdyan M., Bakloushinskaya I., Just W.;
RT   "Characterization of Pisrt1/Foxl2 in Ellobius lutescens and exclusion as
RT   sex-determining genes.";
RL   Mamm. Genome 16:281-289(2005).
CC   -!- FUNCTION: Transcriptional regulator. Critical factor essential for
CC       ovary differentiation and maintenance, and repression of the genetic
CC       program for somatic testis determination (By similarity). Prevents
CC       trans-differentiation of ovary to testis through transcriptional
CC       repression of the Sertoli cell-promoting gene SOX9 (By similarity). Has
CC       apoptotic activity in ovarian cells (By similarity). Suppresses ESR1-
CC       mediated transcription of PTGS2/COX2 stimulated by tamoxifen (By
CC       similarity). Activates SIRT1 transcription under cellular stress
CC       conditions (By similarity). Activates transcription of OSR2 (By
CC       similarity). Is a regulator of CYP19 expression (By similarity). Is a
CC       transcriptional repressor of STAR (By similarity). Participates in
CC       SMAD3-dependent transcription of FST via the intronic SMAD-binding
CC       element (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with ESR1. Interacts with UBE2I/UBC9. Interacts with
CC       SMAD3. Interacts with DDX20. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}.
CC   -!- PTM: Sumoylated with SUMO1; sumoylation is required for transcriptional
CC       repression activity. {ECO:0000250}.
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DR   EMBL; AY623815; AAV30684.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4VUF1; -.
DR   SMR; Q4VUF1; -.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0043028; F:cysteine-type endopeptidase regulator activity involved in apoptotic process; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; ISS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0002074; P:extraocular skeletal muscle development; ISS:UniProtKB.
DR   GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   CDD; cd00059; FH; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR001766; Fork_head_dom.
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   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   3: Inferred from homology;
KW   Differentiation; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW   Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN           1..373
FT                   /note="Forkhead box protein L2"
FT                   /id="PRO_0000254947"
FT   DNA_BIND        50..144
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          272..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        300..336
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         33
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P58012"
FT   CROSSLNK        25
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   373 AA;  38686 MW;  0AC076413501AD42 CRC64;
     MMASYPEPED AAGALLAPEN GRTVKEPEAP PPSPGKGGGT APEKPDPAQK PPYSYVALIA
     MAIRESAEKR LTLSGIYQYI IAKFPFYEKN KKGWQNSIRH NLSLNECFIK VPREGGGERK
     GNYWTLDPAC EDMFEKGNYR RRRRMKRPFR PPPAHFQPGK GLFGSGGAAG GCGVAGAGAD
     GYGYLAPPKY LQSGFLNNSW PLPQPPSPMP YASCQMAAAA AAAAAAAAAA GPGSPGAAAV
     VKGLAGPAAS YGPYSRVQSM ALPPGVVNSY NGLGGPPAAP PPPPPHPHPH PHAHHLHAAA
     APPPAPPHHG AAAPPPGQLS PSSPATAAPP APAPTSAPGL QFACARQPEL AMMHCSYWDH
     DSKTGALHSR LDL