FOXL2_CAPHI
ID FOXL2_CAPHI Reviewed; 377 AA.
AC Q8MIP2;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Forkhead box protein L2;
GN Name=FOXL2;
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15885498; DOI=10.1016/j.ygeno.2005.02.011;
RA Pannetier M., Renault L., Jolivet G., Cotinot C., Pailhoux E.;
RT "Ovarian-specific expression of a new gene regulated by the goat PIS region
RT and transcribed by a FOXL2 bidirectional promoter.";
RL Genomics 85:715-726(2005).
RN [2]
RP FUNCTION AS TRANSCRIPTIONAL REGULATOR OF CYP19, AND TISSUE SPECIFICITY.
RX PubMed=16720712; DOI=10.1677/jme.1.01947;
RA Pannetier M., Fabre S., Batista F., Kocer A., Renault L., Jolivet G.,
RA Mandon-Pepin B., Cotinot C., Veitia R., Pailhoux E.;
RT "FOXL2 activates P450 aromatase gene transcription: towards a better
RT characterization of the early steps of mammalian ovarian development.";
RL J. Mol. Endocrinol. 36:399-413(2006).
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 transcriptional repressor of STAR (By similarity).
CC Participates in SMAD3-dependent transcription of FST via the intronic
CC SMAD-binding element (By similarity). Is a regulator of CYP19
CC expression. {ECO:0000250, ECO:0000269|PubMed:16720712}.
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 -!- TISSUE SPECIFICITY: Detected in the majority of somatic cells in the
CC developing ovary. {ECO:0000269|PubMed:16720712}.
CC -!- PTM: Sumoylated with SUMO1; sumoylation is required for transcriptional
CC repression activity. {ECO:0000250}.
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DR EMBL; AY112725; AAM52099.1; -; Genomic_DNA.
DR RefSeq; XP_017905386.1; XM_018049897.1.
DR AlphaFoldDB; Q8MIP2; -.
DR SMR; Q8MIP2; -.
DR GeneID; 102191377; -.
DR KEGG; chx:102191377; -.
DR CTD; 668; -.
DR OrthoDB; 1270467at2759; -.
DR Proteomes; UP000291000; Unassembled WGS sequence.
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; IDA: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:0048048; P:embryonic eye morphogenesis; ISS:AgBase.
DR GO; GO:0008210; P:estrogen metabolic process; NAS:UniProtKB.
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; IEP: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:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:AgBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA: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 1: Evidence at protein level;
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_0000246178"
FT DNA_BIND 55..149
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 1..53
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; 38802 MW; D7BD295AFCDD9E52 CRC64;
MMASYPEPED ASGALLAPET GRAAKEPEAP APPSPGKGGG GGAGAAPEKP 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
