FSTA_DANRE
ID FSTA_DANRE Reviewed; 322 AA.
AC Q9YHV4; A5PMK3; A7MC96; Q6DC45;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Follistatin-A;
DE Short=FS;
DE AltName: Full=Activin-binding protein;
DE AltName: Full=Follistatin-1;
DE Short=zFst1;
DE Flags: Precursor;
GN Name=fsta; Synonyms=fst, fst1; ORFNames=si:dkey-111k10.2, si:dkeyp-88a5.1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Gastrula;
RX PubMed=9882485; DOI=10.1006/dbio.1998.9003;
RA Bauer H., Meier A., Hild M., Stachel S., Economides A., Hazelett D.,
RA Harland R.M., Hammerschmidt M.;
RT "Follistatin and noggin are excluded from the zebrafish organizer.";
RL Dev. Biol. 204:488-507(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16890217; DOI=10.1016/j.ydbio.2006.07.002;
RA Dal-Pra S., Fuerthauer M., Van-Celst J., Thisse B., Thisse C.;
RT "Noggin1 and Follistatin-like2 function redundantly to Chordin to
RT antagonize BMP activity.";
RL Dev. Biol. 298:514-526(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo, and Larva;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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) (By similarity). Inhibits
CC bmp-signaling during later stages of development including late phases
CC of dorsoventral patterning, to refine the early pattern set up by the
CC interaction of chordino and bmp2/4. Not involved in organizer function
CC or early phases of dorsoventral pattern formation. {ECO:0000250,
CC ECO:0000269|PubMed:16890217, ECO:0000269|PubMed:9882485}.
CC -!- SUBUNIT: Monomer. {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9YHV4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9YHV4-2; Sequence=VSP_034660;
CC -!- TISSUE SPECIFICITY: Not expressed in the organizer region. Expression
CC in gastrulating embryos is confined to anterior and paraxial regions,
CC which give rise to head mesoderm and the first five somites. In
CC addition, expressed transiently in a subset of cells in the posterior
CC notochord anlage. Later, expression is seen in brain, eyes and somites.
CC {ECO:0000269|PubMed:16890217, ECO:0000269|PubMed:9882485}.
CC -!- DEVELOPMENTAL STAGE: First expressed at mid-gastrulation.
CC {ECO:0000269|PubMed:9882485}.
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 EMBL; AF084948; AAD09175.1; -; mRNA.
DR EMBL; DQ317968; ABC48669.1; -; mRNA.
DR EMBL; BX530078; CAN87942.1; -; Genomic_DNA.
DR EMBL; BX537294; CAN87834.1; -; Genomic_DNA.
DR EMBL; BC078241; AAH78241.1; -; mRNA.
DR EMBL; BC152095; AAI52096.1; -; mRNA.
DR RefSeq; NP_571112.3; NM_131037.3. [Q9YHV4-1]
DR AlphaFoldDB; Q9YHV4; -.
DR SMR; Q9YHV4; -.
DR STRING; 7955.ENSDARP00000122591; -.
DR MEROPS; I01.966; -.
DR PaxDb; Q9YHV4; -.
DR Ensembl; ENSDART00000051065; ENSDARP00000051064; ENSDARG00000052846. [Q9YHV4-1]
DR Ensembl; ENSDART00000146237; ENSDARP00000122591; ENSDARG00000052846. [Q9YHV4-2]
DR Ensembl; ENSDART00000163302; ENSDARP00000136983; ENSDARG00000113185. [Q9YHV4-1]
DR GeneID; 100004116; -.
DR KEGG; dre:100004116; -.
DR CTD; 100004116; -.
DR ZFIN; ZDB-GENE-990714-11; fsta.
DR eggNOG; KOG3649; Eukaryota.
DR GeneTree; ENSGT00940000157072; -.
DR HOGENOM; CLU_050745_0_0_1; -.
DR InParanoid; Q9YHV4; -.
DR OMA; RWTIFNG; -.
DR PhylomeDB; Q9YHV4; -.
DR TreeFam; TF106409; -.
DR Reactome; R-DRE-2473224; Antagonism of Activin by Follistatin.
DR PRO; PR:Q9YHV4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 5.
DR Bgee; ENSDARG00000052846; Expressed in swim bladder and 19 other tissues.
DR GO; GO:0005576; C:extracellular region; NAS:ZFIN.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0048185; F:activin binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0048263; P:determination of dorsal identity; IMP:ZFIN.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IDA:ZFIN.
DR GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IMP:ZFIN.
DR GO; GO:0030901; P:midbrain development; IMP:ZFIN.
DR GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0009994; P:oocyte differentiation; NAS:ZFIN.
DR GO; GO:0043049; P:otic placode formation; IGI:ZFIN.
DR GO; GO:0030510; P:regulation of BMP signaling pathway; IBA:GO_Central.
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 Alternative splicing; Developmental protein; Disulfide bond; Glycoprotein;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..322
FT /note="Follistatin-A"
FT /id="PRO_0000010109"
FT DOMAIN 33..106
FT /note="TB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 97..120
FT /note="Follistatin-like 1"
FT DOMAIN 103..169
FT /note="Kazal-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 170..193
FT /note="Follistatin-like 2"
FT DOMAIN 189..244
FT /note="Kazal-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 247..271
FT /note="Follistatin-like 3"
FT DOMAIN 267..321
FT /note="Kazal-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 35..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 45..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 59..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 98..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 103..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 121..153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 125..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 135..167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 195..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 199..221
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 210..242
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 273..305
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 277..298
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 287..319
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT VAR_SEQ 296..322
FT /note="SECAMKQAACSLGVLLEVKHSGSCNCK -> TITEDQEDDDDEEDQDYMAYV
FT QLSPVLDG (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_034660"
FT CONFLICT 216
FT /note="V -> I (in Ref. 1; AAD09175)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="A -> S (in Ref. 2; ABC48669, 3; CAN87942 and 4;
FT AAH78241)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 322 AA; 35517 MW; 728F2A2D85674A13 CRC64;
MLRMLKRQQL HPGMILLLFW LCYLIEDQKV QAGNCWLQQG KNGRCQVLYM PGMSREECCR
SGRLGTSWTE EDVPNSTLFR WMIFNGGAPN CIPCKETCDN VDCGPGKRCK MNRRSKPRCV
CAPDCSNVTW KGPVCGSDGK TYRDECALLK SKCKGHPDLE VQYQGKCKKT CRDVLCPGSS
TCVVDQTNNA YCVTCNRICP EVMSPDQYLC GNDGIVYASA CHLRRATCLL GRSIGVAYEG
KCIKAKSCDD IHCSAGKKCL WDAKMSRGRC AVCAESCPES RSEEAVCASD NTTYPSECAM
KQAACSLGVL LEVKHSGSCN CK
