FST_MOUSE
ID FST_MOUSE Reviewed; 344 AA.
AC P47931; A6H6P0;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Follistatin {ECO:0000303|PubMed:7600958};
DE Short=FS;
DE AltName: Full=Activin-binding protein {ECO:0000303|PubMed:7956942};
DE Flags: Precursor;
GN Name=Fst {ECO:0000312|MGI:MGI:95586};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Ovary;
RX PubMed=7600958; DOI=10.1242/dev.120.4.803;
RA Albano R.M., Arkell R., Beddington R.S.P., Smith J.C.;
RT "Expression of inhibin subunits and follistatin during postimplantation
RT mouse development: decidual expression of activin and expression of
RT follistatin in primitive streak, somites and hindbrain.";
RL Development 120:803-813(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-341 (ISOFORM 1).
RC STRAIN=CBA X NMR1; TISSUE=Ovary;
RX PubMed=7956942; DOI=10.1210/endo.135.5.7956942;
RA Tuuri T., Eramaa M., Hilden K., Ritvos O.;
RT "Activin-binding protein follistatin messenger ribonucleic acid and
RT secreted protein levels are induced by chorionic gonadotropin in cultured
RT human granulosa-luteal cells.";
RL Endocrinology 135:2196-2203(1994).
RN [4]
RP ROLE IN MUSCLE HYPERTROPHY.
RX PubMed=27182554; DOI=10.1172/jci.insight.85477;
RA Davey J.R., Watt K.I., Parker B.L., Chaudhuri R., Ryall J.G.,
RA Cunningham L., Qian H., Sartorelli V., Sandri M., Chamberlain J.,
RA James D.E., Gregorevic P.;
RT "Integrated expression analysis of muscle hypertrophy identifies Asb2 as a
RT negative regulator of muscle mass.";
RL JCI Insight 1:0-0(2016).
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.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P47931-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P47931-2; Sequence=VSP_060082;
CC -!- DEVELOPMENTAL STAGE: Embryonic expression first occurs in the primitive
CC streak, followed by expression in head mesoderm, somites, and specific
CC rhombomeres of the hindbrain, and later in midbrain and diencephalon.
CC No expression is seen in the node or notochord.
CC -!- MISCELLANEOUS: Induces muscle hypertrophy when injected into the
CC tibialis anterior muscle with reduced response in older mice.
CC {ECO:0000269|PubMed:27182554}.
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DR EMBL; Z29532; CAA82648.1; -; mRNA.
DR EMBL; BC144926; AAI44927.1; -; mRNA.
DR EMBL; BC145945; AAI45946.1; -; mRNA.
DR EMBL; X83377; CAA58291.1; -; mRNA.
DR CCDS; CCDS36787.1; -. [P47931-2]
DR CCDS; CCDS88534.1; -. [P47931-1]
DR PIR; S45321; S45321.
DR RefSeq; NP_001288302.1; NM_001301373.1. [P47931-1]
DR RefSeq; NP_001288304.1; NM_001301375.1.
DR RefSeq; NP_032072.1; NM_008046.3. [P47931-2]
DR AlphaFoldDB; P47931; -.
DR SMR; P47931; -.
DR BioGRID; 199751; 2.
DR STRING; 10090.ENSMUSP00000022287; -.
DR MEROPS; I01.966; -.
DR GlyGen; P47931; 2 sites.
DR PhosphoSitePlus; P47931; -.
DR CPTAC; non-CPTAC-3710; -.
DR MaxQB; P47931; -.
DR PaxDb; P47931; -.
DR PeptideAtlas; P47931; -.
DR PRIDE; P47931; -.
DR ProteomicsDB; 266877; -. [P47931-1]
DR Antibodypedia; 11023; 596 antibodies from 38 providers.
DR DNASU; 14313; -.
DR Ensembl; ENSMUST00000022287; ENSMUSP00000022287; ENSMUSG00000021765. [P47931-1]
DR Ensembl; ENSMUST00000231252; ENSMUSP00000156375; ENSMUSG00000021765. [P47931-2]
DR GeneID; 14313; -.
DR KEGG; mmu:14313; -.
DR UCSC; uc007rxn.2; mouse. [P47931-1]
DR CTD; 10468; -.
DR MGI; MGI:95586; Fst.
DR VEuPathDB; HostDB:ENSMUSG00000021765; -.
DR eggNOG; KOG3649; Eukaryota.
DR GeneTree; ENSGT00940000157072; -.
DR InParanoid; P47931; -.
DR OMA; RWTIFNG; -.
DR OrthoDB; 1460520at2759; -.
DR PhylomeDB; P47931; -.
DR TreeFam; TF106409; -.
DR Reactome; R-MMU-2473224; Antagonism of Activin by Follistatin.
DR BioGRID-ORCS; 14313; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Fst; mouse.
DR PRO; PR:P47931; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; P47931; protein.
DR Bgee; ENSMUSG00000021765; Expressed in cumulus cell and 239 other tissues.
DR ExpressionAtlas; P47931; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0048185; F:activin binding; ISO:MGI.
DR GO; GO:0038102; F:activin receptor antagonist activity; ISO:MGI.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; ISO:MGI.
DR GO; GO:0036305; P:ameloblast differentiation; IMP:MGI.
DR GO; GO:0030509; P:BMP signaling pathway; IGI:MGI.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0008585; P:female gonad development; IMP:MGI.
DR GO; GO:0007276; P:gamete generation; IGI:MGI.
DR GO; GO:0031069; P:hair follicle morphogenesis; IMP:MGI.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISO:MGI.
DR GO; GO:0043616; P:keratinocyte proliferation; IMP:MGI.
DR GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; ISO:MGI.
DR GO; GO:0030857; P:negative regulation of epithelial cell differentiation; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
DR GO; GO:0007389; P:pattern specification process; IMP:MGI.
DR GO; GO:0051798; P:positive regulation of hair follicle development; ISO:MGI.
DR GO; GO:0030510; P:regulation of BMP signaling pathway; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; IGI:MGI.
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 Alternative splicing; Disulfide bond; Glycoprotein; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..344
FT /note="Follistatin"
FT /id="PRO_0000010104"
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 VAR_SEQ 241..242
FT /note="KA -> T (in isoform 2)"
FT /id="VSP_060082"
SQ SEQUENCE 344 AA; 37866 MW; 935B6CBB213176F9 CRC64;
MVCARHQPGG LCLLLLLLCQ FMEDRSAQAG NCWLRQAKNG RCQVLYKTEL SKEECCSTGR
LSTSWTEEDV NDNTLFKWMI FNGGAPNCIP CKETCENVDC GPGKKCRMNK KNKPRCVCAP
DCSNITWKGP VCGLDGKTYR NECALLKARC KEQPELEVQY QGKCKKTCRD VFCPGSSTCV
VDQTNNAYCV TCNRICPEPS SSEQYLCGND GVTYSSACHL RKATCLLGRS IGLAYEGKCI
KAKSCEDIQC GGGKKCLWDS KVGRGRCSLC DELCPDSKSD EPVCASDNAT YASECAMKEA
ACSSGVLLEV KHSGSCNSIS EETEEEEEEE DQDYSFPISS ILEW
