FST_CHICK
ID FST_CHICK Reviewed; 343 AA.
AC Q90844; Q90680; Q9PS97;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Follistatin;
DE Short=FS;
DE AltName: Full=Activin-binding protein;
DE Flags: Precursor;
GN Name=FST;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=8625798; DOI=10.1242/dev.122.2.473;
RA Graham A., Lumsden A.;
RT "Interactions between rhombomeres modulate Krox-20 and follistatin
RT expression in the chick embryo hindbrain.";
RL Development 122:473-480(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=7554497; DOI=10.1002/dvg.1020170108;
RA Connolly D.J., Patel K., Seleiro E.A., Wilkinson D.G., Cooke J.;
RT "Cloning, sequencing, and expressional analysis of the chick homologue of
RT follistatin.";
RL Dev. Genet. 17:65-77(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 177-250.
RC TISSUE=Embryonic ovary;
RX PubMed=7576634; DOI=10.1016/0896-6273(95)90176-0;
RA Darland D.C., Link B.A., Nishi R.;
RT "Activin A and follistatin expression in developing targets of ciliary
RT ganglion neurons suggests a role in regulating neurotransmitter
RT phenotype.";
RL Neuron 15:857-866(1995).
CC -!- FUNCTION: Binds directly to activin and functions as an activin
CC antagonist. Inhibits activin A signaling in the iris and regulates
CC somatostatin phenotype in ciliary ganglion neurons. Specific inhibitor
CC of the biosynthesis and secretion of pituitary follicle stimulating
CC hormone (FSH).
CC -!- SUBUNIT: Monomer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Ciliary ganglion neurons. Levels are higher in the
CC iris than the choroid.
CC -!- DEVELOPMENTAL STAGE: Levels increase in the iris from embryonic day 9
CC (E9) to E16 in contrast to the choroid where it remains low relative to
CC iris. During early hindbrain development strongly expressed in
CC rhombomeres R2, R4, R5 and R6 but not in R3. Expression in R3 is seen
CC at later stages and is dependent on neighboring interactions.
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DR EMBL; X87609; CAA60915.1; -; mRNA.
DR EMBL; U34589; AAA92005.1; -; mRNA.
DR PIR; S55369; S55369.
DR RefSeq; NP_990531.1; NM_205200.1.
DR AlphaFoldDB; Q90844; -.
DR SMR; Q90844; -.
DR STRING; 9031.ENSGALP00000023997; -.
DR MEROPS; I01.966; -.
DR PaxDb; Q90844; -.
DR GeneID; 396119; -.
DR KEGG; gga:396119; -.
DR CTD; 10468; -.
DR VEuPathDB; HostDB:geneid_396119; -.
DR eggNOG; KOG3649; Eukaryota.
DR HOGENOM; CLU_050745_0_0_1; -.
DR InParanoid; Q90844; -.
DR OrthoDB; 1460520at2759; -.
DR PhylomeDB; Q90844; -.
DR PRO; PR:Q90844; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0048185; F:activin binding; NAS:AgBase.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0005518; F:collagen binding; IBA:GO_Central.
DR GO; GO:0050840; F:extracellular matrix binding; IBA:GO_Central.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; IMP:AgBase.
DR GO; GO:1902870; P:negative regulation of amacrine cell differentiation; IMP:AgBase.
DR GO; GO:1902864; P:negative regulation of embryonic camera-type eye development; IMP:AgBase.
DR GO; GO:1902876; P:negative regulation of embryonic pattern specification; IMP:AgBase.
DR GO; GO:1902873; P:negative regulation of horizontal cell localization; IMP:AgBase.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IMP:AgBase.
DR GO; GO:1902867; P:negative regulation of retina development in camera-type eye; IMP:AgBase.
DR GO; GO:0046670; P:positive regulation of retinal cell programmed cell death; IMP:AgBase.
DR GO; GO:1901390; P:positive regulation of transforming growth factor beta activation; NAS:AgBase.
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 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..28
FT /evidence="ECO:0000255"
FT CHAIN 29..343
FT /note="Follistatin"
FT /id="PRO_0000010108"
FT DOMAIN 29..102
FT /note="TB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 93..116
FT /note="Follistatin-like 1"
FT DOMAIN 99..165
FT /note="Kazal-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 166..189
FT /note="Follistatin-like 2"
FT DOMAIN 185..240
FT /note="Kazal-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 243..267
FT /note="Follistatin-like 3"
FT DOMAIN 263..317
FT /note="Kazal-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT REGION 315..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..333
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..54
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 41..87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 55..90
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 94..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 99..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 117..149
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 121..142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 131..163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 191..224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 195..217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 206..238
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 269..301
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 273..294
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 283..315
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT CONFLICT 129
FT /note="P -> F (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="T -> S (in Ref. 3; AAA92005)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="T -> L (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="E -> G (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="R -> E (in Ref. 3; AAA92005)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 343 AA; 38193 MW; 15A78762560E1AAE CRC64;
MLNQRIHPGM LVLLMFLYHF MEDHTAQAGN CWLRQARNGR CQVLYKTDLS KEECCKSGRL
TTSWTEEDVN DNTLFKWMIF NGGAPNCIPC KETCENVDCG PGKKCKMNKK NKPRCVCAPD
CSNITWKGPV CGLDGKTYRN ECALLKARCK EQPELEVQYQ GKCKKTCRDV LCPGSSTCVV
DQTNNAYCVT CNRICPEPTS PEQYLCGNDG ITYASACHLR KATCLLGRSI GLAYEGKCIK
AKSCEDIQCS AGKKCLWDFK VGRGRCALCD ELCPESKSDE AVCASDNTTY PSECAMKEAA
CSMGVLLEVK HSGSCNSINE DPEEEEEDED QDYSFPISSI LEW
