FST_XENLA
ID FST_XENLA Reviewed; 341 AA.
AC P31515; Q5D032; Q91376;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Follistatin;
DE Short=FS;
DE AltName: Full=Activin-binding protein;
DE AltName: Full=XFS-319;
DE Flags: Precursor;
GN Name=fst;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), AND CHARACTERIZATION.
RC TISSUE=Tail bud;
RX PubMed=8168135; DOI=10.1016/0092-8674(94)90320-4;
RA Hemmati-Brivanlou A., Kelly O.G., Melton D.A.;
RT "Follistatin, an antagonist of activin, is expressed in the Spemann
RT organizer and displays direct neuralizing activity.";
RL Cell 77:283-295(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PARTIAL NUCLEOTIDE SEQUENCE (ISOFORM LONG).
RC TISSUE=Ovary;
RX PubMed=1704219; DOI=10.1016/0006-291x(91)91521-d;
RA Tashiro K., Yamada R., Asano M., Hashimoto M., Muramatsu M., Shiokawa K.;
RT "Expression of mRNA for activin-binding protein (follistatin) during early
RT embryonic development of Xenopus laevis.";
RL Biochem. Biophys. Res. Commun. 174:1022-1027(1991).
RN [4]
RP PROTEIN SEQUENCE OF N-TERMINUS, AND CHARACTERIZATION.
RX PubMed=8365557; DOI=10.1006/dbio.1993.1227;
RA Fukui A., Nakamura T., Sugino K., Takio K., Uchiyama H., Asashima M.,
RA Sugino H.;
RT "Isolation and characterization of Xenopus follistatin and activins.";
RL Dev. Biol. 159:131-139(1993).
CC -!- FUNCTION: Binds directly to activin and functions as an activin
CC antagonist which plays a role in neural induction. The short isoform is
CC a more potent inhibitor of activin than the long isoform. Specific
CC inhibitor of the biosynthesis and secretion of pituitary follicle
CC stimulating hormone (FSH).
CC -!- SUBUNIT: Monomer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P31515-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P31515-2; Sequence=VSP_001568;
CC -!- TISSUE SPECIFICITY: Spemann organizer and notochord.
CC -!- DEVELOPMENTAL STAGE: The short isoform is present maternally while the
CC long isoform is expressed at gastrula stages. Detected in a few cells
CC of the Spemann organizer at the onset of gastrulation. During
CC gastrulation expression continues in the prechordal plate and the
CC anterior portion of the notochord anlage. Beginning at early neurula
CC stages, expression is initiated at new sites in the head mesoderm;
CC hypochord; pronephros; eyes; fore-, mid-, and hindbrain; and the
CC midbrain-hindbrain junction.
CC -!- INDUCTION: By activin.
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DR EMBL; S69801; AAB30638.1; -; mRNA.
DR EMBL; BC068649; AAH68649.1; -; mRNA.
DR PIR; A53502; A53502.
DR RefSeq; NP_001084059.1; NM_001090590.1. [P31515-1]
DR AlphaFoldDB; P31515; -.
DR SMR; P31515; -.
DR MEROPS; I01.966; -.
DR DNASU; 399282; -.
DR GeneID; 399282; -.
DR KEGG; xla:399282; -.
DR CTD; 399282; -.
DR Xenbase; XB-GENE-486300; fst.L.
DR OMA; RWTIFNG; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 399282; Expressed in heart and 15 other tissues.
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 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000269|PubMed:8365557"
FT CHAIN 30..341
FT /note="Follistatin"
FT /id="PRO_0000010110"
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 100..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 321..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 42..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 56..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 95..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 100..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 118..150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 122..143
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 132..164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 192..225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 196..218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 207..239
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 270..302
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 274..295
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 284..316
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT VAR_SEQ 318..341
FT /note="SIVEDTEEEEEEEEPDYSFVISSW -> CK (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:8168135"
FT /id="VSP_001568"
FT CONFLICT 268
FT /note="A -> G (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="C -> S (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 341 AA; 37543 MW; 5D26E7BE70890171 CRC64;
MLNERIQPGM IFLLTVSLCH FMEYRAVQAG NCWLQQSKNG RCQVLYRTEL SKEECCKTGR
LGTSWTEEDV PNSTLFKWMI FHGGAPHCIP CKETCENVDC GPGKKCKMNK KNKPRCVCAP
DCSNITWKGS VCGIDGKTYK DECALLKAKC KGVPELDVQY QGKCKKTCRD VLCPGSSSCV
VDQTNNAYCV TCNRICPEPT SPDQYLCGND GITYGSACHL RKATCLLGRS IGLAYEGKCI
KAKSCEDIQC SAGKKCLWDS RVGRGRCALC DDLCGESKSD DTVCASDNTT YPSECAMKQA
ACSTGILLEV KHSGSCNSIV EDTEEEEEEE EPDYSFVISS W
