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Database: UniProt
Entry: A0A1U7QNK7_MESAU
LinkDB: A0A1U7QNK7_MESAU
Original site: A0A1U7QNK7_MESAU 
ID   A0A1U7QNK7_MESAU        Unreviewed;       344 AA.
AC   A0A1U7QNK7;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Follistatin {ECO:0000256|ARBA:ARBA00039758};
DE   AltName: Full=Activin-binding protein {ECO:0000256|ARBA:ARBA00042260};
GN   Name=Fst {ECO:0000313|RefSeq:XP_005082827.1};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_005082827.1};
RN   [1] {ECO:0000313|RefSeq:XP_005082827.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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       {ECO:0000256|ARBA:ARBA00037743}.
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DR   RefSeq; XP_005082827.1; XM_005082770.3.
DR   AlphaFoldDB; A0A1U7QNK7; -.
DR   STRING; 10036.ENSMAUP00000006702; -.
DR   GeneID; 101835278; -.
DR   KEGG; maua:101835278; -.
DR   CTD; 10468; -.
DR   eggNOG; KOG3649; Eukaryota.
DR   OrthoDB; 2875444at2759; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0048185; F:activin binding; IEA:Ensembl.
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: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: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:0001501; P:skeletal system development; IEA:Ensembl.
DR   CDD; cd00104; KAZAL_FS; 2.
DR   Gene3D; 3.30.60.30; -; 3.
DR   Gene3D; 3.90.290.10; TGF-beta binding (TB) domain; 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   PANTHER; PTHR10913:SF45; AGRIN; 1.
DR   PANTHER; PTHR10913; FOLLISTATIN-RELATED; 1.
DR   Pfam; PF09289; FOLN; 1.
DR   Pfam; PF21333; FST_N; 1.
DR   Pfam; PF07648; Kazal_2; 3.
DR   SMART; SM00274; FOLN; 3.
DR   SMART; SM00280; KAZAL; 3.
DR   SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 3.
DR   SUPFAM; SSF57581; TB module/8-cys domain; 1.
DR   PROSITE; PS51465; KAZAL_2; 3.
DR   PROSITE; PS51364; TB; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..344
FT                   /note="Follistatin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010545461"
FT   DOMAIN          30..91
FT                   /note="TB"
FT                   /evidence="ECO:0000259|PROSITE:PS51364"
FT   DOMAIN          117..166
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51465"
FT   DOMAIN          190..241
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51465"
FT   DOMAIN          268..318
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51465"
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"
SQ   SEQUENCE   344 AA;  37889 MW;  FFCEA101B2037F99 CRC64;
     MVCARHQPGG LCLLLLLLCQ FMEDRSAQAG NCWLRQAKNG RCQVLYKTEL SKEECCSTGR
     LSTSWTEEDV NDNTLFKWMI FNGGAPNCIP CKETCENVDC GPGKKCRMNK KNKPRCVCAP
     DCSNITWKGP VCGLDGKTYR NECALLKARC KEQPELEVQY QGKCKKTCRD VLCPGSSTCV
     VDQTNNAYCV TCNRICPEPA SSEQYLCGND GVTYSSACHL RKATCLLGRS IGLAYEGKCI
     KAKSCEDIQC GGGKKCLWDF KVGRGRCSLC DELCPDSKSD EPVCASDNAT YASECAMKEA
     ACSSGVLLEV KHSGSCNSIS EDTEEEEEEE DQDYNFPISS ILEW
//
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