FST_SHEEP
ID FST_SHEEP Reviewed; 337 AA.
AC P31514;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Follistatin {ECO:0000303|PubMed:1632897};
DE Short=FS;
DE AltName: Full=Activin-binding protein {ECO:0000250|UniProtKB:P21674};
DE Flags: Precursor; Fragment;
GN Name=FST {ECO:0000250|UniProtKB:P19883};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1632897; DOI=10.1677/jme.0.0080259;
RA Tisdall D.J., Hill D., Petersen G.B., Fleming J.S.;
RT "Ovine follistatin: characterization of cDNA and expression in sheep ovary
RT during the luteal phase of the oestrous cycle.";
RL J. Mol. Endocrinol. 8:259-264(1992).
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; M63123; AAA31522.1; -; mRNA.
DR PIR; I47079; I47079.
DR AlphaFoldDB; P31514; -.
DR SMR; P31514; -.
DR STRING; 9940.ENSOARP00000008709; -.
DR MEROPS; I01.966; -.
DR eggNOG; KOG3649; Eukaryota.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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..22
FT CHAIN 23..337
FT /note="Follistatin"
FT /id="PRO_0000010107"
FT DOMAIN 23..96
FT /note="TB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 87..110
FT /note="Follistatin-like 1"
FT DOMAIN 105..159
FT /note="Kazal-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 160..183
FT /note="Follistatin-like 2"
FT DOMAIN 179..234
FT /note="Kazal-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 237..261
FT /note="Follistatin-like 3"
FT DOMAIN 254..311
FT /note="Kazal-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT REGION 309..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..327
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 25..48
FT /evidence="ECO:0000250|UniProtKB:P19883,
FT ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 35..81
FT /evidence="ECO:0000250|UniProtKB:P19883,
FT ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 49..84
FT /evidence="ECO:0000250|UniProtKB:P19883,
FT ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 88..99
FT /evidence="ECO:0000250|UniProtKB:P19883"
FT DISULFID 93..109
FT /evidence="ECO:0000250|UniProtKB:P19883"
FT DISULFID 111..143
FT /evidence="ECO:0000250|UniProtKB:P19883"
FT DISULFID 115..136
FT /evidence="ECO:0000250|UniProtKB:P19883"
FT DISULFID 125..157
FT /evidence="ECO:0000250|UniProtKB:P19883"
FT DISULFID 161..172
FT /evidence="ECO:0000250|UniProtKB:P19883"
FT DISULFID 166..182
FT /evidence="ECO:0000250|UniProtKB:P19883"
FT DISULFID 185..218
FT /evidence="ECO:0000250|UniProtKB:P19883"
FT DISULFID 189..211
FT /evidence="ECO:0000250|UniProtKB:P19883"
FT DISULFID 200..232
FT /evidence="ECO:0000250|UniProtKB:P19883"
FT DISULFID 238..249
FT /evidence="ECO:0000250|UniProtKB:P19883"
FT DISULFID 243..260
FT /evidence="ECO:0000250|UniProtKB:P19883"
FT DISULFID 263..295
FT /evidence="ECO:0000250|UniProtKB:P19883"
FT DISULFID 267..288
FT /evidence="ECO:0000250|UniProtKB:P19883"
FT DISULFID 277..309
FT /evidence="ECO:0000250|UniProtKB:P19883"
FT NON_TER 1
SQ SEQUENCE 337 AA; 37082 MW; 1E8BE1BBB6B109C4 CRC64;
PGGVCLLLLL LCQFMEDRSA QAGNCWLRQA KNGRCQVLYK TELSKEECCS TGRLSTSWTE
EDVNDNTLFK WMIFNGGAPN CIPCKETCEN VDCGPGKKCR MNKKNKPRCV CAPDCSNITW
KGPVCGLDGK TYRNECALLK ARCKEQPELE VQYQGKCKKT CRDVFCPGSS TCVVDQTNNA
YCVTCNRICP EPTSSEQYLC GNDGVTYPSA CHLRKATCLL GRSIGLAYEG KCIKAKSCED
IQCTGGKKCL WDFKVGRGRC SLCGELCPES KSEEPVCASD NATYASECAM KEAACSSGVL
LEVKHSGSCN SISEDTEDEE EDEDQDYSFP ISSILEW
