FST_RAT
ID FST_RAT Reviewed; 344 AA.
AC P21674; Q80XW7;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Follistatin {ECO:0000303|PubMed:2725528};
DE Short=FS;
DE AltName: Full=Activin-binding protein {ECO:0000303|PubMed:8472873};
DE Flags: Precursor;
GN Name=Fst {ECO:0000312|RGD:2633};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Ovary;
RX PubMed=2725528; DOI=10.1210/mend-3-4-651;
RA Shimasaki S., Koga M., Buscaglia M.L., Simmons D.M., Bicsak T.A., Ling N.;
RT "Follistatin gene expression in the ovary and extragonadal tissues.";
RL Mol. Endocrinol. 3:651-659(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
RX PubMed=8472873; DOI=10.1016/0303-7207(93)90080-4;
RA Miyanaga K., Shimasaki S.;
RT "Structural and functional characterization of the rat follistatin
RT (activin-binding protein) gene promoter.";
RL Mol. Cell. Endocrinol. 92:99-109(1993).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 93-165 ALONE AND IN COMPLEX WITH
RP HEPARIN ANALOGS, AND DISULFIDE BONDS.
RX PubMed=12867435; DOI=10.1074/jbc.m211284200;
RA Innis C.A., Hyvonen M.;
RT "Crystal structures of the heparan sulfate-binding domain of follistatin.
RT Insights into ligand binding.";
RL J. Biol. Chem. 278:39969-39977(2003).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 93-241 IN COMPLEX WITH ACTIVIN A,
RP AND DISULFIDE BONDS.
RX PubMed=16482217; DOI=10.1038/sj.emboj.7601000;
RA Harrington A.E., Morris-Triggs S.A., Ruotolo B.T., Robinson C.V.,
RA Ohnuma S., Hyvonen M.;
RT "Structural basis for the inhibition of activin signalling by
RT follistatin.";
RL EMBO J. 25:1035-1045(2006).
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 -!- INTERACTION:
CC P21674; P08476: INHBA; Xeno; NbExp=2; IntAct=EBI-5746973, EBI-8077140;
CC -!- SUBCELLULAR LOCATION: Secreted.
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DR EMBL; M31591; AAB60704.1; -; Genomic_DNA.
DR EMBL; M31586; AAB60704.1; JOINED; Genomic_DNA.
DR EMBL; M31587; AAB60704.1; JOINED; Genomic_DNA.
DR EMBL; M31588; AAB60704.1; JOINED; Genomic_DNA.
DR EMBL; M31589; AAB60704.1; JOINED; Genomic_DNA.
DR EMBL; M31590; AAB60704.1; JOINED; Genomic_DNA.
DR EMBL; S58913; AAP13905.1; -; Genomic_DNA.
DR PIR; I57698; I57698.
DR RefSeq; NP_036693.1; NM_012561.2.
DR PDB; 1LR7; X-ray; 1.50 A; A=93-165.
DR PDB; 1LR8; X-ray; 2.10 A; A=93-165.
DR PDB; 1LR9; X-ray; 2.50 A; A=93-165.
DR PDB; 2ARP; X-ray; 2.00 A; F=93-241.
DR PDBsum; 1LR7; -.
DR PDBsum; 1LR8; -.
DR PDBsum; 1LR9; -.
DR PDBsum; 2ARP; -.
DR AlphaFoldDB; P21674; -.
DR SMR; P21674; -.
DR BioGRID; 246544; 1.
DR IntAct; P21674; 2.
DR MINT; P21674; -.
DR STRING; 10116.ENSRNOP00000015680; -.
DR MEROPS; I01.966; -.
DR GlyGen; P21674; 2 sites.
DR PhosphoSitePlus; P21674; -.
DR PaxDb; P21674; -.
DR PRIDE; P21674; -.
DR Ensembl; ENSRNOT00000015680; ENSRNOP00000015680; ENSRNOG00000011631.
DR GeneID; 24373; -.
DR KEGG; rno:24373; -.
DR CTD; 10468; -.
DR RGD; 2633; Fst.
DR eggNOG; KOG3649; Eukaryota.
DR GeneTree; ENSGT00940000157072; -.
DR HOGENOM; CLU_050745_0_0_1; -.
DR InParanoid; P21674; -.
DR OMA; RWTIFNG; -.
DR OrthoDB; 1460520at2759; -.
DR PhylomeDB; P21674; -.
DR TreeFam; TF106409; -.
DR Reactome; R-RNO-2473224; Antagonism of Activin by Follistatin.
DR EvolutionaryTrace; P21674; -.
DR PRO; PR:P21674; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000011631; Expressed in ovary and 16 other tissues.
DR Genevisible; P21674; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048185; F:activin binding; ISO:RGD.
DR GO; GO:0038102; F:activin receptor antagonist activity; ISO:RGD.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; IDA:RGD.
DR GO; GO:0036305; P:ameloblast differentiation; IEA:Ensembl.
DR GO; GO:0030509; P:BMP signaling pathway; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0008585; P:female gonad development; ISO:RGD.
DR GO; GO:0007276; P:gamete generation; ISO:RGD.
DR GO; GO:0031069; P:hair follicle morphogenesis; ISO:RGD.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISO:RGD.
DR GO; GO:0043616; P:keratinocyte proliferation; ISO:RGD.
DR GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; ISO:RGD.
DR GO; GO:0045596; P:negative regulation of cell differentiation; ISO:RGD.
DR GO; GO:0030857; P:negative regulation of epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0046882; P:negative regulation of follicle-stimulating hormone secretion; TAS:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; ISO:RGD.
DR GO; GO:0007389; P:pattern specification process; ISO:RGD.
DR GO; GO:0051798; P:positive regulation of hair follicle development; ISO:RGD.
DR GO; GO:0030510; P:regulation of BMP signaling pathway; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; ISO:RGD.
DR Gene3D; 3.90.290.10; -; 1.
DR IDEAL; IID50202; -.
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 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..344
FT /note="Follistatin"
FT /id="PRO_0000010106"
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 315..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"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:1LR7"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:1LR7"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:1LR7"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1LR7"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:1LR7"
FT HELIX 142..151
FT /evidence="ECO:0007829|PDB:1LR7"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:1LR7"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:2ARP"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:2ARP"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:2ARP"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:2ARP"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:2ARP"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:2ARP"
FT HELIX 217..227
FT /evidence="ECO:0007829|PDB:2ARP"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:2ARP"
SQ SEQUENCE 344 AA; 37838 MW; 864244CF05436552 CRC64;
MVCARHQPGG LCLLLLLLCQ FMEDRSAQAG NCWLRQAKNG RCQVLYKTEL SKEECCSTGR
LSTSWTEEDV NDNTLFKWMI FNGGAPNCIP CKETCENVDC GPGKKCRMNK KNKPRCVCAP
DCSNITWKGP VCGLDGKTYR NECALLKARC KEQPELEVQY QGKCKKTCRD VFCPGSSTCV
VDQTNNAYCV TCNRICPEPS SSEQSLCGND GVTYSSACHL RKATCLLGRS IGLAYEGKCI
KAKSCEDIQC GGGKKCLWDF KVGRGRCSLC DELCPDSKSD EPVCASDNAT YASECAMKEA
ACSSGVLLEV KHSGSCNSIS EETEEEEEEE DQDYSFPISS TLEW
