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Follistatin (FS) (Activin-binding protein)

 FST_MOUSE               Reviewed;         344 AA.
P47931; A6H6P0;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
25-OCT-2017, entry version 131.
RecName: Full=Follistatin;
Short=FS;
AltName: Full=Activin-binding protein;
Flags: Precursor;
Name=Fst;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Ovary;
PubMed=7600958;
Albano R.M., Arkell R., Beddington R.S.P., Smith J.C.;
"Expression of inhibin subunits and follistatin during
postimplantation mouse development: decidual expression of activin and
expression of follistatin in primitive streak, somites and
hindbrain.";
Development 120:803-813(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 3-340.
STRAIN=CBA X NMR1; TISSUE=Ovary;
PubMed=7956942; DOI=10.1210/endo.135.5.7956942;
Tuuri T., Eramaa M., Hilden K., Ritvos O.;
"Activin-binding protein follistatin messenger ribonucleic acid and
secreted protein levels are induced by chorionic gonadotropin in
cultured human granulosa-luteal cells.";
Endocrinology 135:2196-2203(1994).
-!- FUNCTION: Binds directly to activin and functions as an activin
antagonist. Specific inhibitor of the biosynthesis and secretion
of pituitary follicle stimulating hormone (FSH).
-!- SUBUNIT: Monomer. {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- DEVELOPMENTAL STAGE: Embryonic expression first occurs in the
primitive streak, followed by expression in head mesoderm,
somites, and specific rhombomeres of the hindbrain, and later in
midbrain and diencephalon. No expression is seen in the node or
notochord.
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EMBL; Z29532; CAA82648.1; -; mRNA.
EMBL; BC144926; AAI44927.1; -; mRNA.
EMBL; BC145945; AAI45946.1; -; mRNA.
EMBL; X83377; CAA58291.1; -; mRNA.
PIR; S45321; S45321.
RefSeq; NP_001288302.1; NM_001301373.1.
RefSeq; NP_001288304.1; NM_001301375.1.
RefSeq; NP_032072.1; NM_008046.3.
UniGene; Mm.4913; -.
ProteinModelPortal; P47931; -.
BioGrid; 199751; 1.
STRING; 10090.ENSMUSP00000022287; -.
MEROPS; I01.966; -.
PhosphoSitePlus; P47931; -.
MaxQB; P47931; -.
PaxDb; P47931; -.
PeptideAtlas; P47931; -.
PRIDE; P47931; -.
GeneID; 14313; -.
KEGG; mmu:14313; -.
UCSC; uc007rxn.2; mouse.
CTD; 10468; -.
MGI; MGI:95586; Fst.
eggNOG; ENOG410IP0F; Eukaryota.
eggNOG; ENOG410YM8Q; LUCA.
HOGENOM; HOG000261649; -.
HOVERGEN; HBG051666; -.
InParanoid; P47931; -.
KO; K04661; -.
PhylomeDB; P47931; -.
TreeFam; TF106409; -.
PRO; PR:P47931; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_FST; -.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0048185; F:activin binding; ISO:MGI.
GO; GO:0030509; P:BMP signaling pathway; IGI:MGI.
GO; GO:0008585; P:female gonad development; IMP:MGI.
GO; GO:0007276; P:gamete generation; IGI:MGI.
GO; GO:0031069; P:hair follicle morphogenesis; IMP:MGI.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISO:MGI.
GO; GO:0043616; P:keratinocyte proliferation; IMP:MGI.
GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; ISO:MGI.
GO; GO:0045596; P:negative regulation of cell differentiation; IMP:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
GO; GO:0007389; P:pattern specification process; IMP:MGI.
GO; GO:0051798; P:positive regulation of hair follicle development; ISO:MGI.
GO; GO:0001501; P:skeletal system development; IGI:MGI.
InterPro; IPR003645; Fol_N.
InterPro; IPR015369; Follistatin/Osteonectin_EGF.
InterPro; IPR002350; Kazal_dom.
InterPro; IPR036058; Kazal_dom_sf.
InterPro; IPR017878; TB_dom.
InterPro; IPR036773; TB_dom_sf.
Pfam; PF09289; FOLN; 1.
Pfam; PF07648; Kazal_2; 3.
SMART; SM00274; FOLN; 3.
SMART; SM00280; KAZAL; 3.
SUPFAM; SSF100895; SSF100895; 3.
SUPFAM; SSF57581; SSF57581; 1.
PROSITE; PS51465; KAZAL_2; 3.
PROSITE; PS51364; TB; 1.
2: Evidence at transcript level;
Complete proteome; Disulfide bond; Glycoprotein; Reference proteome;
Repeat; Secreted; Signal.
SIGNAL 1 29 {ECO:0000255}.
CHAIN 30 344 Follistatin.
/FTId=PRO_0000010104.
DOMAIN 30 103 TB. {ECO:0000255|PROSITE-
ProRule:PRU00697}.
DOMAIN 94 117 Follistatin-like 1.
DOMAIN 112 166 Kazal-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 167 190 Follistatin-like 2.
DOMAIN 186 241 Kazal-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 244 268 Follistatin-like 3.
DOMAIN 264 318 Kazal-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
COMPBIAS 321 333 Asp/Glu-rich (highly acidic).
CARBOHYD 124 124 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 288 288 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 32 55 {ECO:0000250|UniProtKB:P19883,
ECO:0000255|PROSITE-ProRule:PRU00697}.
DISULFID 42 88 {ECO:0000250|UniProtKB:P19883,
ECO:0000255|PROSITE-ProRule:PRU00697}.
DISULFID 56 91 {ECO:0000250|UniProtKB:P19883,
ECO:0000255|PROSITE-ProRule:PRU00697}.
DISULFID 95 106 {ECO:0000250|UniProtKB:P19883}.
DISULFID 100 116 {ECO:0000250|UniProtKB:P19883}.
DISULFID 118 150 {ECO:0000250|UniProtKB:P19883}.
DISULFID 122 143 {ECO:0000250|UniProtKB:P19883}.
DISULFID 132 164 {ECO:0000250|UniProtKB:P19883}.
DISULFID 168 179 {ECO:0000250|UniProtKB:P19883}.
DISULFID 173 189 {ECO:0000250|UniProtKB:P19883}.
DISULFID 192 225 {ECO:0000250|UniProtKB:P19883}.
DISULFID 196 218 {ECO:0000250|UniProtKB:P19883}.
DISULFID 207 239 {ECO:0000250|UniProtKB:P19883}.
DISULFID 245 256 {ECO:0000250|UniProtKB:P19883}.
DISULFID 250 267 {ECO:0000250|UniProtKB:P19883}.
DISULFID 270 302 {ECO:0000250|UniProtKB:P19883}.
DISULFID 274 295 {ECO:0000250|UniProtKB:P19883}.
DISULFID 284 316 {ECO:0000250|UniProtKB:P19883}.
CONFLICT 241 242 KA -> T (in Ref. 1; CAA82648).
{ECO:0000305}.
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


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