ID A0A1S2ZGE6_ERIEU Unreviewed; 367 AA.
AC A0A1S2ZGE6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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_007518977.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007518977.1};
RN [1] {ECO:0000313|RefSeq:XP_007518977.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_007518977.1; XM_007518915.2.
DR AlphaFoldDB; A0A1S2ZGE6; -.
DR STRING; 9365.ENSEEUP00000012815; -.
DR GeneID; 103109800; -.
DR CTD; 10468; -.
DR eggNOG; KOG3649; Eukaryota.
DR InParanoid; A0A1S2ZGE6; -.
DR OrthoDB; 2875444at2759; -.
DR Proteomes; UP000079721; Unplaced.
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 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:UP000079721};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 53..114
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 140..189
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 213..264
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 291..341
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT REGION 338..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..357
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 367 AA; 40617 MW; E82C743A80028FDE CRC64;
MTFKTVFSKA VWKTNCGVKM GSTFLQPRHQ PGGLCLLLLL LCQFMEDRSA QAGNCWLRQA
KNGRCQVLYK TELSKEECCS TGRLSTSWTE EDVNDNTLFK WMIFNGGAPN CIPCKETCEN
VDCGPGKKCR MNKKNKPRCV CAPDCSNITW KGPVCGMDGK TYRNECALLK ARCKEQPELE
VQYQGKCKKT CRDVFCPGSS TCVVDQTNNA YCVTCNRICP EPSSSEQYLC GNDGVTYSSA
CHLRKATCLL GRSIGLAYEG KCIKAKSCED IQCTGGKKCL WDFKVGRGRC SLCDELCPET
KSEEPVCASD NATYASECAM KEAACSSGVL LEVKHSGSCN SISEDTEEEE EDEDQDYSFP
ISSILEW
//
