ID   FST_BUBBU               Reviewed;         344 AA.
AC   A5YT95;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Follistatin {ECO:0000303|Ref.1};
DE            Short=FS;
DE   AltName: Full=Activin-binding protein {ECO:0000250|UniProtKB:P21674};
DE   Flags: Precursor;
GN   Name=FST {ECO:0000250|UniProtKB:P19883};
OS   Bubalus bubalis (Domestic water buffalo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bubalus.
OX   NCBI_TaxID=89462;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Deng J.X., Jiang H.S., Yang X.R.;
RT   "Cloning and sequence analysis of follistatin gene in buffalo.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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) (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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DR   EMBL; EF585672; ABQ96267.1; -; mRNA.
DR   AlphaFoldDB; A5YT95; -.
DR   SMR; A5YT95; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   Gene3D; 3.90.290.10; -; 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   Pfam; PF09289; FOLN; 1.
DR   Pfam; PF07648; Kazal_2; 3.
DR   SMART; SM00274; FOLN; 3.
DR   SMART; SM00280; KAZAL; 3.
DR   SUPFAM; SSF100895; SSF100895; 3.
DR   SUPFAM; SSF57581; SSF57581; 1.
DR   PROSITE; PS51465; KAZAL_2; 3.
DR   PROSITE; PS51364; TB; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Repeat; Secreted; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..344
FT                   /note="Follistatin"
FT                   /id="PRO_0000318091"
FT   DOMAIN          30..103
FT                   /note="TB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT   DOMAIN          94..117
FT                   /note="Follistatin-like 1"
FT   DOMAIN          112..166
FT                   /note="Kazal-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DOMAIN          167..190
FT                   /note="Follistatin-like 2"
FT   DOMAIN          186..241
FT                   /note="Kazal-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DOMAIN          244..268
FT                   /note="Follistatin-like 3"
FT   DOMAIN          261..318
FT                   /note="Kazal-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   REGION          316..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        320..334
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        288
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        32..55
FT                   /evidence="ECO:0000250|UniProtKB:P19883,
FT                   ECO:0000255|PROSITE-ProRule:PRU00697"
FT   DISULFID        42..88
FT                   /evidence="ECO:0000250|UniProtKB:P19883,
FT                   ECO:0000255|PROSITE-ProRule:PRU00697"
FT   DISULFID        56..91
FT                   /evidence="ECO:0000250|UniProtKB:P19883,
FT                   ECO:0000255|PROSITE-ProRule:PRU00697"
FT   DISULFID        95..106
FT                   /evidence="ECO:0000250|UniProtKB:P19883"
FT   DISULFID        100..116
FT                   /evidence="ECO:0000250|UniProtKB:P19883"
FT   DISULFID        118..150
FT                   /evidence="ECO:0000250|UniProtKB:P19883"
FT   DISULFID        122..143
FT                   /evidence="ECO:0000250|UniProtKB:P19883"
FT   DISULFID        132..164
FT                   /evidence="ECO:0000250|UniProtKB:P19883"
FT   DISULFID        168..179
FT                   /evidence="ECO:0000250|UniProtKB:P19883"
FT   DISULFID        173..189
FT                   /evidence="ECO:0000250|UniProtKB:P19883"
FT   DISULFID        192..225
FT                   /evidence="ECO:0000250|UniProtKB:P19883"
FT   DISULFID        196..218
FT                   /evidence="ECO:0000250|UniProtKB:P19883"
FT   DISULFID        207..239
FT                   /evidence="ECO:0000250|UniProtKB:P19883"
FT   DISULFID        245..256
FT                   /evidence="ECO:0000250|UniProtKB:P19883"
FT   DISULFID        250..267
FT                   /evidence="ECO:0000250|UniProtKB:P19883"
FT   DISULFID        270..302
FT                   /evidence="ECO:0000250|UniProtKB:P19883"
FT   DISULFID        274..295
FT                   /evidence="ECO:0000250|UniProtKB:P19883"
FT   DISULFID        284..316
FT                   /evidence="ECO:0000250|UniProtKB:P19883"
SQ   SEQUENCE   344 AA;  37974 MW;  6D46728E197062D1 CRC64;
     MARPRHQPGG LCLLLLLLCQ FMEDRSAQAG NCWLRQAKNG RCQVLYKTEL SKEECCSTGR
     LSTSWTEEDV NDNTLFKWMI FNGGAPNCIP CKETCENVDC GPGKKCRMNK KNKPRCVCAP
     DCSNITWKGL VCGLDGKTYR NECALLKARC KEQPELQVQY QGKCKKTCRD VFCPGSSTCV
     VDQTNNAYCV TCNRICPEPT SSEQYLCGND GVTYPSACHL RKATCLLGRS IGLAYEGKCI
     KAKSCDDIQC TGGKKCLWDF KVGRGRCSLC GELCPESKSE EPVCASDNAT YASECAMKEA
     ACSSGVLLEV KHSGSCNSIS EDTEDEEEDE DQDYSFPISS ILEW