FST_HORSE
ID FST_HORSE Reviewed; 344 AA.
AC O62650;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Follistatin {ECO:0000303|PubMed:10331189};
DE Short=FS;
DE AltName: Full=Activin-binding protein {ECO:0000250|UniProtKB:P21674};
DE Flags: Precursor;
GN Name=FST {ECO:0000250|UniProtKB:P19883};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Follicular cell;
RX PubMed=10331189; DOI=10.1292/jvms.61.201;
RA Sugawara Y., Yamanouchi K., Naito K., Tachi C., Tojo H., Sawasaki T.;
RT "Molecular cloning of cDNA for equine follistatin and its gene expression
RT in the reproductive tissues of the mare.";
RL J. Vet. Med. Sci. 61:201-207(1999).
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 -!- SUBUNIT: Monomer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted.
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DR EMBL; AB010829; BAA25699.1; -; mRNA.
DR RefSeq; NP_001075280.1; NM_001081811.2.
DR AlphaFoldDB; O62650; -.
DR SMR; O62650; -.
DR STRING; 9796.ENSECAP00000015558; -.
DR MEROPS; I01.966; -.
DR PaxDb; O62650; -.
DR Ensembl; ENSECAT00000019030; ENSECAP00000015558; ENSECAG00000017783.
DR GeneID; 100033825; -.
DR KEGG; ecb:100033825; -.
DR CTD; 10468; -.
DR VGNC; VGNC:18145; FST.
DR GeneTree; ENSGT00940000157072; -.
DR HOGENOM; CLU_050745_0_0_1; -.
DR InParanoid; O62650; -.
DR OrthoDB; 1460520at2759; -.
DR Proteomes; UP000002281; Chromosome 21.
DR Bgee; ENSECAG00000017783; Expressed in trophoblast and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0048185; F:activin binding; IBA:GO_Central.
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:0030154; P:cell differentiation; IBA:GO_Central.
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:0032926; P:negative regulation of activin receptor signaling pathway; IBA:GO_Central.
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:0030510; P:regulation of BMP signaling pathway; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
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; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..344
FT /note="Follistatin"
FT /id="PRO_0000010102"
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 264..318
FT /note="Kazal-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT REGION 314..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; 38002 MW; 1803577D2D9BE4AA CRC64;
MVRPRHQPGG LCLLLLLLCQ FMEDRSAQAG NCWLRQAKNG RCQVLYKTEL SKEECCSTGR
LSTSWTEEDV NDNTLFKWMI FNGGAPNCIP CKETCDNVDC GPGKKCRMNK KNKPRCVCAP
DCSNITWKGP VCGLDGKTYR NECALLKARC KEQPELEVQY QGKCKKTCRD VNCPGSSTCV
VDQTNNAYCV TCNRICPEPT SSEQYLCGND GVTYSSACHL RKATCLLGRS IGLAYEGKCI
KAKSCEDIQC TGGKKCLWDF KVGRGRCSLC DELCPDSKSE EPVCASDNAT YASECAMKEA
ACSSGVLLEV KHSGSCNSIS EDTEEEEEDE DQDYSFPISS ILEW
