ID   FOXL2_RABIT             Reviewed;         384 AA.
AC   Q6VFT5;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Forkhead box protein L2;
GN   Name=FOXL2;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=14684984; DOI=10.1159/000074338;
RA   Cocquet J., De Baere E., Gareil M., Pannetier M., Xia X., Fellous M.,
RA   Veitia R.A.;
RT   "Structure, evolution and expression of the FOXL2 transcription unit.";
RL   Cytogenet. Genome Res. 101:206-211(2003).
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; AY340972; AAQ91846.1; -; Genomic_DNA.
DR   RefSeq; NP_001164586.1; NM_001171115.1.
DR   AlphaFoldDB; Q6VFT5; -.
DR   SMR; Q6VFT5; -.
DR   PRIDE; Q6VFT5; -.
DR   GeneID; 100328926; -.
DR   KEGG; ocu:100328926; -.
DR   CTD; 668; -.
DR   InParanoid; Q6VFT5; -.
DR   Proteomes; UP000001811; Unplaced.
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   Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..384
FT                   /note="Forkhead box protein L2"
FT                   /id="PRO_0000246180"
FT   DNA_BIND        56..150
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          277..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        281..298
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..347
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   384 AA;  39385 MW;  F5E64ED6D2180A40 CRC64;
     MMASYPEPEE AAGALLAPES GRAAKEPEAP PPSPGKGGGG GGGGGSAAEK PDPAQKPPYS
     YVALIAMAIR ESAEKRLTLS GIYQYIIAKF PFYEKNKKGW QNSIRHNLSL NECFIKVPRE
     GGGERKGNYW TLDPACEDMF EKGNYRRRRR MKRPFRPPPA HFQPGKGLFG AAGAAGGCGV
     AGAGADGYGY LAPPKYLQSG FLNNSWPLPQ PPSPMPYASC QMAAAAAAAA AAAAAAGPGS
     PGAAAVVKGL AGPAASYGPY SRVQSMALPP GVVNSYNGLG GPPAAPPPPP PPPPPPHPHP
     HPHAHHLHAA AAPPPAPPHH GAAAPPPGQL SPASPATAAP PAPAPTSAPG LQFACARQPE
     LAMMHCSYWD HDSKTGALHS RLDL