FST_BOVIN
ID FST_BOVIN Reviewed; 344 AA.
AC P50291; Q32XW5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Follistatin {ECO:0000303|PubMed:8011323};
DE Short=FS;
DE AltName: Full=Activin-binding protein {ECO:0000250|UniProtKB:P21674};
DE Flags: Precursor;
GN Name=FST {ECO:0000250|UniProtKB:P19883};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Holstein; TISSUE=Ovary, and Testis;
RX PubMed=8011323; DOI=10.1002/mrd.1080370405;
RA Houde A., Lussier J.G., Ethier J.-F., Gagnon C., Silversides D.W.;
RT "Cloning and tissue expression of bovine follistatin cDNA.";
RL Mol. Reprod. Dev. 37:391-397(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Rouhaud L., Forestier F., Laforet M.P., Julien R., Amarger V.;
RT "The myostatin signalling pathway: structure, expression and polymorphisms
RT of the ACVR2B and FST genes in cattle.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal spinal cord;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-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).
CC -!- SUBUNIT: Monomer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted.
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DR EMBL; L21716; AAA30522.1; -; mRNA.
DR EMBL; AY775795; AAX19140.1; -; Genomic_DNA.
DR EMBL; BC133637; AAI33638.1; -; mRNA.
DR PIR; I45894; I45894.
DR RefSeq; NP_786995.2; NM_175801.3.
DR AlphaFoldDB; P50291; -.
DR SMR; P50291; -.
DR STRING; 9913.ENSBTAP00000004318; -.
DR MEROPS; I01.966; -.
DR PaxDb; P50291; -.
DR PRIDE; P50291; -.
DR Ensembl; ENSBTAT00000004318; ENSBTAP00000004318; ENSBTAG00000003329.
DR GeneID; 327681; -.
DR KEGG; bta:327681; -.
DR CTD; 10468; -.
DR VEuPathDB; HostDB:ENSBTAG00000003329; -.
DR VGNC; VGNC:29134; FST.
DR eggNOG; KOG3649; Eukaryota.
DR GeneTree; ENSGT00940000157072; -.
DR HOGENOM; CLU_050745_0_0_1; -.
DR InParanoid; P50291; -.
DR OMA; RWTIFNG; -.
DR OrthoDB; 1460520at2759; -.
DR TreeFam; TF106409; -.
DR Proteomes; UP000009136; Chromosome 20.
DR Bgee; ENSBTAG00000003329; Expressed in granulosa cell and 103 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_0000010101"
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:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 42..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 56..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 95..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 100..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 118..150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 122..143
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 132..164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 192..225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 196..218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 207..239
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 270..302
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 274..295
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 284..316
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT CONFLICT 157
FT /note="Q -> E (in Ref. 1; AAA30522)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 344 AA; 37958 MW; A84FF34350F1AAD9 CRC64;
MARPRHQPGG LCLLLLLLCQ FMEDRSAQAG NCWLRQAKNG RCQVLYKTEL SKEECCSTGR
LSTSWTEEDV NDNTLFKWMI FNGGAPNCIP CKETCENVDC GPGKKCRMNK KNKPRCVCAP
DCSNITWKGP VCGLDGKTYR NECALLKARC KEQPELQVQY QGKCKKTCRD VFCPGSSTCV
VDQTNNAYCV TCNRICPEPT SSEQYLCGND GVTYPSACHL RKATCLLGRS IGLAYEGKCI
KAKSCDDIQC TGGKKCLWDF KVGRGRCSLC GELCPESKSE EPVCASDNAT YASECAMKEA
ACSSGVLLEV KHSGSCNSIS EDTEDEEEDE DQDYSFPISS ILEW
