ID I3MKN9_ICTTR Unreviewed; 330 AA.
AC I3MKN9;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Follistatin {ECO:0000256|ARBA:ARBA00039758};
DE AltName: Full=Activin-binding protein {ECO:0000256|ARBA:ARBA00042260};
GN Name=FST {ECO:0000313|Ensembl:ENSSTOP00000011893.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000011893.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000011893.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Binds directly to activin and functions as an activin
CC antagonist. Specific inhibitor of the biosynthesis and secretion of
CC pituitary follicle stimulating hormone (FSH).
CC {ECO:0000256|ARBA:ARBA00037743}.
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DR EMBL; AGTP01014278; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; I3MKN9; -.
DR STRING; 43179.ENSSTOP00000011893; -.
DR Ensembl; ENSSTOT00000013270.3; ENSSTOP00000011893.3; ENSSTOG00000013273.3.
DR eggNOG; KOG3649; Eukaryota.
DR GeneTree; ENSGT00940000157072; -.
DR HOGENOM; CLU_050745_0_0_1; -.
DR InParanoid; I3MKN9; -.
DR TreeFam; TF106409; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0048185; F:activin binding; IEA:Ensembl.
DR GO; GO:0038102; F:activin receptor antagonist activity; IEA:Ensembl.
DR GO; GO:0036305; P:ameloblast differentiation; IEA:Ensembl.
DR GO; GO:0030509; P:BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0008585; P:female gonad development; IEA:Ensembl.
DR GO; GO:0007276; P:gamete generation; IEA:Ensembl.
DR GO; GO:0031069; P:hair follicle morphogenesis; IEA:Ensembl.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0043616; P:keratinocyte proliferation; IEA:Ensembl.
DR GO; GO:0030857; P:negative regulation of epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR GO; GO:0007389; P:pattern specification process; IEA:Ensembl.
DR GO; GO:0051798; P:positive regulation of hair follicle development; IEA:Ensembl.
DR GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
DR CDD; cd00104; KAZAL_FS; 2.
DR Gene3D; 3.30.60.30; -; 3.
DR Gene3D; 3.90.290.10; TGF-beta binding (TB) domain; 1.
DR InterPro; IPR003645; Fol_N.
DR InterPro; IPR015369; Follistatin/Osteonectin_EGF.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR017878; TB_dom.
DR InterPro; IPR036773; TB_dom_sf.
DR PANTHER; PTHR10913:SF45; AGRIN; 1.
DR PANTHER; PTHR10913; FOLLISTATIN-RELATED; 1.
DR Pfam; PF09289; FOLN; 1.
DR Pfam; PF21333; FST_N; 1.
DR Pfam; PF07648; Kazal_2; 3.
DR SMART; SM00274; FOLN; 3.
DR SMART; SM00280; KAZAL; 3.
DR SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 3.
DR SUPFAM; SSF57581; TB module/8-cys domain; 1.
DR PROSITE; PS51465; KAZAL_2; 3.
DR PROSITE; PS51364; TB; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..330
FT /note="Follistatin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012429468"
FT DOMAIN 17..78
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 104..153
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 177..228
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 254..304
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT REGION 301..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..320
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 330 AA; 36520 MW; 38710E3743A7DC58 CRC64;
LLLLLCQFME DRSAQAGNCW LRQAKNGRCQ VLYKTELSKE ECCSTGRLST SWTEEDVNDN
TLFKWMIFNG GAPNCIPCKE TCENVDCGPG KKCRMNKKNK PRCVCAPDCS NITWKGPVCG
LDGKTYRNEC ALLKARCKEQ PELEVQYQGK CKKTCRDVYC PGSSTCVVDQ TNNAYCVTCN
RICPEPTSSE QYLCGNDGVT YSSACHLRKA TCLLGRSIGL AYEGKCITKS CEDIQCSGGK
KCLWDFKVGR GRCSLCDELC PDSKSDEPVC ASDNATYANE CAMKEAACSS GVLLEVKHSG
SCNSISEDTE EEEEDEDQDY SFPISSILEW
//
