FOXL2_PIG
ID FOXL2_PIG Reviewed; 377 AA.
AC Q6VFT6;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Forkhead box protein L2;
GN Name=FOXL2;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
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; AY340971; AAQ91845.1; -; Genomic_DNA.
DR RefSeq; NP_001231594.1; NM_001244665.1.
DR AlphaFoldDB; Q6VFT6; -.
DR SMR; Q6VFT6; -.
DR STRING; 9823.ENSSSCP00000019349; -.
DR PaxDb; Q6VFT6; -.
DR PRIDE; Q6VFT6; -.
DR Ensembl; ENSSSCT00070016063; ENSSSCP00070013295; ENSSSCG00070008330.
DR GeneID; 100622956; -.
DR KEGG; ssc:100622956; -.
DR CTD; 668; -.
DR eggNOG; KOG2294; Eukaryota.
DR HOGENOM; CLU_023357_1_0_1; -.
DR InParanoid; Q6VFT6; -.
DR OrthoDB; 1270467at2759; -.
DR TreeFam; TF316127; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 13.
DR GO; GO:0005634; C:nucleus; ISS:AgBase.
DR GO; GO:0043028; F:cysteine-type endopeptidase regulator activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:AgBase.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:AgBase.
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:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0006309; P:apoptotic DNA fragmentation; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0048048; P:embryonic eye morphogenesis; ISS:AgBase.
DR GO; GO:0002074; P:extraocular skeletal muscle development; ISS:UniProtKB.
DR GO; GO:0019101; P:female somatic sex determination; ISS:AgBase.
DR GO; GO:0060014; P:granulosa cell differentiation; ISS:AgBase.
DR GO; GO:0001541; P:ovarian follicle development; ISS:AgBase.
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:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:AgBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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..377
FT /note="Forkhead box protein L2"
FT /id="PRO_0000246179"
FT DNA_BIND 55..149
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..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..338
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 34
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 377 AA; 38918 MW; 29E8A7B619CE991A CRC64;
MMASYPEPED AAGALLAPET GRTAKEPEAP PPLSPGKGGG GGASTAPEKP DPAQKPPYSY
VALIAMAIRE SAEKRLTLSG IYQYIIAKFP FYEKNKKGWQ NSIRHNLSLN ECFIKVPREG
GGERKGNYWT LDPACEDMFE KGNYRRRRRM KRPFRPPPAH FQPGKGLFGA GGAAGGCGVA
GAGADGYGYL APPKYLQSGF LNNSWPLPQP PSPMPYASCQ MAAAAAAAAA AAAAAGPGSP
GAAAVVKGLA GPAASYGPYS RVQSMALPPG VVNSYNGLGG PPAAPPPPPH PHSHPHAHHL
HAAAAPPPAP PHHGAAAPPP GQLSPASPAT AAPPAPAPTN APGLQFACAR QPELAMMHCS
YWDHDSKTGA LHSRLDL
